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Information on EC 3.6.5.4 - signal-recognition-particle GTPase
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3.6.5.4 signal-recognition-particle GTPaseIUBMB Comments
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
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Word Map
- 3.6.5.4
- gtpases
- ribonucleoprotein
-
co-translational
-
translocons
-
srp-dependent
- thylakoids
-
sec
-
exit
-
light-harvesting
- myopathy
-
secyeg
-
cotranslationally
-
universally
-
gtp-binding
- myositis
- translocase
-
presecretory
- tetraloops
-
insertase
-
polytopic
-
anti-srp
-
methionine-rich
-
ribosome-associated
-
rna-protein
- preproteins
-
protein-targeting
-
signal-anchor
-
m-domain
-
ribosome-bound
-
chromodomains
- medicine
- polymyositis
-
protein-conducting
-
anti-signal
-
protein-rna
-
chlorophyll-binding
-
gtp-bound
-
walter
-
multispanning
-
imnms
-
sequence-binding
-
myositis-specific
-
tail-anchored
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
signal recognition particle, srp54, srp receptor, srp19, cpsrp43, cpsrp54, cpsrp, srp14, sralpha, cpftsy, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chloroplast signal recognition particle
cpFtsY
cpSRP
cpSRP43
cpSRP54
CtSR
EC 3.6.1.49
-
-
formerly
-
Ffh
FlhF
FtsY
GTPase
guanine triphosphatase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
ribosomal GTPase
-
-
-
-
signal recognition particle
signal recognition particle receptor
signal recognition particle receptor subunit alpha
signal recognition particle receptor subunit beta
signal-recognition-particle GTPase
SR
SR GTPase
SRalpha
SRbeta
SRbeta GTPase
SRP
SRP GTPase
SRP receptor
SRP19
accessory subunit of the signal recognition particle, SRP54 and SRP19 are the two RNA binding components forming the core of the signal recognition particle, SRP19 acts as a molecular scaffold and a chaperone, assisting the SRP RNA in adopting the conformation required for its optimal interaction with the essential subunit SRP54, and proper assembly of a functional SRP
SRP54
SRP54 GTPase
Srp72p
SRPRA
SRPRB
cpSRP43
-
C-terminal domain of the 43 kDa subunit of the chloroplast signal recognition particle
Ffh
-
in Escherichia col the SRP consists of 4.5S RNA (114 nucleotides) and a single protein, Ffh, which is responsible for signal sequence recognition
Ffh
-
in Escherichia col the SRP consists of 4.5S RNA (114 nucleotides) and a single protein, Ffh, which is responsible for signal sequence recognition
-
FtsY
-
membrane bound SRP receptor, member of SRP GTPases which form a subfamily within the signal recognition particle, MinD, BioD class of NTP binding proteins
GTPase
-
-
-
-
SRP
-
the SRP includes three critical components, a protein (Ffh), an RNA (scRNA), and a membrane receptor (FtsY)
SRP
-
the SRP includes three critical components, a protein (Ffh), an RNA (scRNA), and a membrane receptor (FtsY)
-
SRP54
GTPase subunit of the signal recognition particle, SRP54 and SRP19 are the two RNA binding components forming the core of the signal recognition particle
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
-
-
-
-
GTP + H2O = GDP + phosphate
activity is associated with the signal-recognition particle, a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (protein-synthesis-assisting)
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
CAS REGISTRY NUMBER
COMMENTARY
9059-32-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
-
cotranslational protein targeting to the plasma membrane, the Ffh-4.5S RNA ribonucleoprotein complex and the FtsY protein, respectively, form a unique complex in which both Ffh and FtsY act as GTPase activating proteins for one another, resulting in a mutual stimulation of GTP hydrolysis by both proteins, 4.5S RNA modulates the conformation of the Ffh-FtsY complex and may regulate its GTPase activity during the SRP functional cycle
-
-
?
GTP + H2O
GDP + phosphate
-
Ffh mediates SRP-dependent, cotranslational protein targeting to the plasma membrane, Ffh and FtsY, the latter being the GTPase subunit of the bacterial SRP receptor, act as GTPase activating proteins for one another, resulting in reciprocal stimulation of GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
-
-
?
GTP + H2O
GDP + phosphate
-
Ffh has a high specificity for GTP over noncognate nucleotides, domain structure
-
-
?
GTP + H2O
GDP + phosphate
-
Asp251 of the enzyme forms a bidentate interaction with not only the bound GTP but also the receptor FtsY across the dimer interface. These interactions form part of the network that seals the lateral entrance to the composite active site at the dimer interface, thereby ensuring the electrostatic and/or structural integrity of the active site and contributing to the formation of an active SRP-FtsY(receptor GTPase) complex
-
-
?
GTP + H2O
GDP + phosphate
-
RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle
-
-
?
GTP + H2O
GDP + phosphate
-
conserved bases in loop D specifically catalyze GTP hydrolysis, a guanine at residue 86 can compete with and substitute for G83 as a catalytic base, loop E controls the action of the distal end docking sites
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
-
-
?
GTP + H2O
GDP + phosphate
-
the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle
-
-
?
GTP + H2O
GDP + phosphate
-
SRP54 is a multidomain protein, the central G domain functions as GTPase, enzyme structure
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting to the plasma membrane, signal recognition particle cycle, SRP and its receptor stimulate each others GTPase activity, GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane
-
-
?
GTP + H2O
GDP + phosphate
-
complex formation of Ffh with the signal recognition particle receptor aligns the two GTP substrate molecules in a symmetrical, composite active site, and the 3-OH groups are essential for association, reciprocal activation and catalysis, this circle of twinned interactions is severed on hydrolysis, leading to complex dissociation after cargo delivery, structure
-
-
?
GTP + H2O
GDP + phosphate
-
the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate
-
-
?
additional information
?
-
light-harvesting chlorophyll a/b binding proteins are posttranslationally targeted to the thylakoid membrane by cpSRP, a heterodimer formed by cpSRP54 and cpSRP43
-
-
?
additional information
?
-
-
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
-
-
?
additional information
?
-
-
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
-
-
?
additional information
?
-
-
signal recognition particle and its membrane-bound receptor facilitate the targeting of the translational machinery, the ribosome, via recognition of a signal sequence in the nascent peptide chain
-
-
?
additional information
?
-
-
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion
-
-
?
additional information
?
-
binding analysis of wild-type FtsY and mutant FtsYDELTAN1 with inactive GMPPNP substrate homologue, structure modeling, overview
-
-
-
additional information
?
-
-
binding analysis of wild-type FtsY and mutant FtsYDELTAN1 with inactive GMPPNP substrate homologue, structure modeling, overview
-
-
-
additional information
?
-
comparison of the nucleotide-free and GTP-bound structures of FtsY, catalytic mechanism and role of Mg2+, detailed overview
-
-
-
additional information
?
-
-
comparison of the nucleotide-free and GTP-bound structures of FtsY, catalytic mechanism and role of Mg2+, detailed overview
-
-
-
additional information
?
-
-
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion
-
-
?
additional information
?
-
-
the RING-H2 type E3 ubiquitin ligase Pirh2 (p53-inducible protein with RING-H2 domain) poly-ubiquitylates the signal recognition particle receptor beta subunit in an intact RING finger domain-dependent manner in vivo and in vitro, Pirh2 preferentially utilizes lysine residues 6 and 29 of the ubiquitin to mediate the formation of polyubiquitin chains on the signal recognition particle receptor beta subunit
-
-
?
additional information
?
-
P08240; Q9Y5M8
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
P08240; Q9Y5M8
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Q9DBG7; P47758
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
-
the cpFtsY membrane-binding motif plays a critical role in the intramolecular communication that regulates cpSRP receptor functions at the membrane
-
-
?
additional information
?
-
-
signal recognition particle and its membrane-bound receptor facilitate the targeting of the translational machinery, the ribosome, via recognition of a signal sequence in the nascent peptide chain
-
-
?
additional information
?
-
-
Rpl25p plays a critical role in the recruitment of signal recognition particle to the ribosome
-
-
?
additional information
?
-
-
the signal recognition particle pathway is important for virulence factor secretion in Streptococcus pyogenes
-
-
?
additional information
?
-
-
the signal recognition particle pathway is important for virulence factor secretion in Streptococcus pyogenes
-
-
?
additional information
?
-
Thermochaetoides thermophila
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila CBS 144.50
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila CBS 144.50
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila DSM 1495
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila DSM 1495
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila IMI 039719
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
Thermochaetoides thermophila IMI 039719
both SRalpha and SRbeta are GTPases
-
-
-
additional information
?
-
-
signal recognition particle and its membrane-bound receptor facilitate the targeting of the translational machinery, the ribosome, via recognition of a signal sequence in the nascent peptide chain
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
-
cotranslational protein targeting to the plasma membrane, the Ffh-4.5S RNA ribonucleoprotein complex and the FtsY protein, respectively, form a unique complex in which both Ffh and FtsY act as GTPase activating proteins for one another, resulting in a mutual stimulation of GTP hydrolysis by both proteins, 4.5S RNA modulates the conformation of the Ffh-FtsY complex and may regulate its GTPase activity during the SRP functional cycle
-
-
?
GTP + H2O
GDP + phosphate
-
Ffh mediates SRP-dependent, cotranslational protein targeting to the plasma membrane, Ffh and FtsY, the latter being the GTPase subunit of the bacterial SRP receptor, act as GTPase activating proteins for one another, resulting in reciprocal stimulation of GTP hydrolysis
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
-
-
?
GTP + H2O
GDP + phosphate
-
the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle
-
-
?
GTP + H2O
GDP + phosphate
-
protein targeting to the plasma membrane, signal recognition particle cycle, SRP and its receptor stimulate each others GTPase activity, GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane
-
-
?
GTP + H2O
GDP + phosphate
-
the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate
-
-
?
additional information
?
-
light-harvesting chlorophyll a/b binding proteins are posttranslationally targeted to the thylakoid membrane by cpSRP, a heterodimer formed by cpSRP54 and cpSRP43
-
-
?
additional information
?
-
-
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
-
-
?
additional information
?
-
-
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
-
-
?
additional information
?
-
-
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion
-
-
?
additional information
?
-
-
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion
-
-
?
additional information
?
-
-
the cpFtsY membrane-binding motif plays a critical role in the intramolecular communication that regulates cpSRP receptor functions at the membrane
-
-
?
additional information
?
-
-
Rpl25p plays a critical role in the recruitment of signal recognition particle to the ribosome
-
-
?
additional information
?
-
-
the signal recognition particle pathway is important for virulence factor secretion in Streptococcus pyogenes
-
-
?
additional information
?
-
-
the signal recognition particle pathway is important for virulence factor secretion in Streptococcus pyogenes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
required, role of a magnesium ion during the GDP and GTP-bound states, overview. The binding of magnesium in the nucleotide site causes the reorientation of the beta-and gamma-phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions
Mg2+
Thermochaetoides thermophila
required, residues Thr64 and Ser107 are directly involved in magnesium coordination
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
signal peptide
-
isolated functional signal peptides bind nonspecifically to the RNA component of SRP and aggregate the entire signal recognition particle, leading to a loss of its intrinsic GTPase activity, this effect is an artifact of the high peptide concentrations and low salt conditions used in in vitro studies, signal sequences at the N-terminus of nascent chains in vivo do not exhibit this activity
-
additional information
-
membrane association of FtsY is stabilized by blocking its GTPase activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cpFtsY
chlorplastic cell division protein FtsY homologue, a signal recognition particle receptor protein, also shows GTPase activity
-
signal recognition particle receptor
-
SRP and its receptor stimulate each others GTPase activity, mechanism of reciprocal activation, substrate twinning activates the signal recognition particle and its receptor
-
signal recognition particle RNA
-
SRP RNA, the signal recognition particle RNA distal end triggers GTP hydrolysis in the signal recognition particle protein-SRP receptor GTPase, i.e. Ffh-FtsY GTPase, complex. An intact docking site at the distal end of SRP RNA is required to stimulate GTPase activation. Loop E plays a crucial role in GTPase activation by the SRP RNA
-
4.5S RNA
-
accelerates the association between Ffh and FtsY 400fold in their GTP-bound form and thereby stimulates GTPase activity
-
4.5S RNA
-
stimulates GTPase activity in the SRP-FtsY complex in vitro and is essential for SRP function in vivo
-
FtsY
-
GTPase subunit of the bacterial SRP receptor activates Ffh, reciprocal GTPase activation mechanism
-
FtsY
-
GTPase subunit of the bacterial SRP receptor, both Ffh and FtsY act as GTPase activating proteins for one another, resulting in a mutual stimulation of GTP hydrolysis by both proteins
-
FtsY
-
GTPase subunit of the SRP receptor activates Ffh, Ffh and FtsY reciprocally regulate each others GTPase activity
-
GTP
-
GTP binding to both the SRP and SR is a prerequisite for the formation of the SRP-SR complex in which GTP hydrolysis is activated in a composite active site
GTP
-
GTP binding to both the SRP and SR is a prerequisite for the formation of the SRP-SR complex in which GTP hydrolysis is activated in a composite active site
additional information
the FtsY GTPase is activated by formation of the targeting complex as well as upon membrane interaction, but homodimerization of FtsY also stimulates its GTPase activity
-
additional information
-
the FtsY GTPase is activated by formation of the targeting complex as well as upon membrane interaction, but homodimerization of FtsY also stimulates its GTPase activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
GTP binds tighter to Ffh than to the GTPase FtsY of the SRP receptor, kinetic data
-
additional information
additional information
-
kinetic and thermodynamic data
-
additional information
additional information
kinetic measurements are performed using a KinTek stopped-flow apparatus with active GTP-bound cpSRP54-cpFtsY complex
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, UUUU mutant
0.037
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, no RNA
0.053
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, UUCG mutant
0.14
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, GUAA mutant
0.182
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, GAAA mutant
0.223
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, wild-type RNA
0.253
GTP
-
maximal rate constant for the GTPase activity of the SRP-FtsY complex, CUUC mutant
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermochaetoides thermophila
signal recognition particle 54 kDa protein subunit with GTPase activity
UniProt
Thermochaetoides thermophila CBS 144.50
signal recognition particle 54 kDa protein subunit with GTPase activity
UniProt
Thermochaetoides thermophila DSM 1495
signal recognition particle 54 kDa protein subunit with GTPase activity
UniProt
Thermochaetoides thermophila IMI 039719
signal recognition particle 54 kDa protein subunit with GTPase activity
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
P08240; Q9Y5M8
separating SRP biogenesis in two parts, a nucleolar and a cytosolic one, is essential for correct SRP assembly
additional information
-
separating SRP biogenesis in two parts, a nucleolar and a cytosolic one, is essential for correct SRP assembly
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the SRP targets the ribosome-nascent chain complexes to the inner membrane by interacting with the SRP receptor
-
additional information
P61010; P06625
the domain of SRalpha that binds SRbeta does so by binding directly to the nucleotide bound form of the GTPase domain of SRbeta. Additional level of regulation of SRP receptor function based on regulated dissociation of the receptor subunits
-
-
chloroplasts contain a signal recognition particle that lacks RNA but contains a conserved 54000 Da GTPase and a novel 43000 Da subunit
the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane
-
the SRP targets the ribosome-nascent chain complexes to the inner membrane by interacting with the SRP receptor
-
SRP receptor alpha and beta subunits
P61010; P06625
peripheral membrane SRalpha subunit, the transmembrane SRbeta subunit is anchoring SRalpha on the endoplasmic reticulum membrane
P61010; P06625
peripheral membrane SRalpha subunit, the transmembrane SRbeta subunit is anchoring SRalpha on the endoplasmic reticulum membrane
P08240; Q9Y5M8
peripheral membrane protein subunit SRalpha, which is anchored to the membrane by the 30 kDa subunit SRbeta, that has a single N-terminal transmembrane domain and short luminal domain
Q9DBG7; P47758
peripheral membrane protein subunit SRalpha, which is anchored to the membrane by the 30 kDa subunit SRbeta, that has a single N-terminal transmembrane domain and short luminal domain
Thermochaetoides thermophila
SRbeta is an integral membrane component of the signal recognition particle (SRP) receptor
Thermochaetoides thermophila CBS 144.50
-
SRbeta is an integral membrane component of the signal recognition particle (SRP) receptor
-
Thermochaetoides thermophila DSM 1495
-
SRbeta is an integral membrane component of the signal recognition particle (SRP) receptor
-
Thermochaetoides thermophila IMI 039719
-
SRbeta is an integral membrane component of the signal recognition particle (SRP) receptor
-
-
the SRP targets the ribosome-nascent chain complexes to the inner membrane by interacting with the SRP receptor
Thermochaetoides thermophila
the SRbeta-ribosome interaction relies on SRalpha, when SRbeta is in the GTP-bound state
Thermochaetoides thermophila CBS 144.50
-
the SRbeta-ribosome interaction relies on SRalpha, when SRbeta is in the GTP-bound state
-
Thermochaetoides thermophila DSM 1495
-
the SRbeta-ribosome interaction relies on SRalpha, when SRbeta is in the GTP-bound state
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
co-evolution of two GTPases enables efficient protein targeting in an RNA-less chloroplast signal recognition particle pathway
evolution
Thermochaetoides thermophila
SR ribosome binding is evolutionarily conserved. Unlike the ribosome-binding activity of human SRalpha, CtSRalpha is unable to destabilize the interaction between protein translocase subunit Sec61beta and the Sec translocase-associated endoplasmic reticulum membrane protein Sec62, suggesting that this interaction is specific to higher eukaryotes
evolution
Thermochaetoides thermophila
the signal recognition particle receptor SRbeta belongs to the Ras-family of small monomeric GTPases, specific differences to the Arf and Sar1 families with implications for GTPase regulation are determined, overview. SRbeta is the oldest member of all small GTPases branching first in eukaryotic evolution
evolution
Thermochaetoides thermophila IMI 039719
-
SR ribosome binding is evolutionarily conserved. Unlike the ribosome-binding activity of human SRalpha, CtSRalpha is unable to destabilize the interaction between protein translocase subunit Sec61beta and the Sec translocase-associated endoplasmic reticulum membrane protein Sec62, suggesting that this interaction is specific to higher eukaryotes
-
evolution
Thermochaetoides thermophila IMI 039719
-
the signal recognition particle receptor SRbeta belongs to the Ras-family of small monomeric GTPases, specific differences to the Arf and Sar1 families with implications for GTPase regulation are determined, overview. SRbeta is the oldest member of all small GTPases branching first in eukaryotic evolution
-
evolution
Thermochaetoides thermophila DSM 1495
-
SR ribosome binding is evolutionarily conserved. Unlike the ribosome-binding activity of human SRalpha, CtSRalpha is unable to destabilize the interaction between protein translocase subunit Sec61beta and the Sec translocase-associated endoplasmic reticulum membrane protein Sec62, suggesting that this interaction is specific to higher eukaryotes
-
evolution
Thermochaetoides thermophila DSM 1495
-
the signal recognition particle receptor SRbeta belongs to the Ras-family of small monomeric GTPases, specific differences to the Arf and Sar1 families with implications for GTPase regulation are determined, overview. SRbeta is the oldest member of all small GTPases branching first in eukaryotic evolution
-
evolution
Thermochaetoides thermophila CBS 144.50
-
SR ribosome binding is evolutionarily conserved. Unlike the ribosome-binding activity of human SRalpha, CtSRalpha is unable to destabilize the interaction between protein translocase subunit Sec61beta and the Sec translocase-associated endoplasmic reticulum membrane protein Sec62, suggesting that this interaction is specific to higher eukaryotes
-
evolution
Thermochaetoides thermophila CBS 144.50
-
the signal recognition particle receptor SRbeta belongs to the Ras-family of small monomeric GTPases, specific differences to the Arf and Sar1 families with implications for GTPase regulation are determined, overview. SRbeta is the oldest member of all small GTPases branching first in eukaryotic evolution
-
malfunction
asymmetries in the catalytic center affect GTP hydrolysis, overview
malfunction
deletion of the finger loop abolishes loading of the cpSRP cargo, light-harvesting chlorophyll binding protein
malfunction
P61010; P06625
deletion of the N-terminal transmembrane domain of SRbeta does not effect receptor dimerization but reveals a cryptic translocation signal that overlaps the GTPase domain. Deletion of the G-1 region, (SRbetaD5) which comprises part of the SRbeta GTPase domain, abolishes binding to SRalpha. A mutant SRbeta containing an amino acid substitution allows the GTPase domain to bind XTP dimerizes with SRalpha most efficiently in the presence of XTP or XDP, but not ATP
malfunction
P08240; Q9Y5M8
in contrast to the Sec61beta-SRalpha cross-link species, which increase in abundance when SR is added to EKRMs (membranes stripped of ribosomes with EDTA and high salt), most other Sec61beta-derived cross-linked adducts are reduced, in particular, the cross-link between Sec61beta and Sec62. A mutant SRP receptor, which contains only the SRX domain of SRalpha (SRalpha126/betaDN), shows a much weaker reduction in Sec61beta-Sec62 crosslinking
malfunction
Q9DBG7; P47758
in contrast to the Sec61beta-SRalpha cross-link species, which increase in abundance when SR is added to EKRMs (membranes stripped of ribosomes with EDTA and high salt), most other Sec61beta-derived cross-linked adducts are reduced, in particular, the cross-link between Sec61beta and Sec62. A mutant SRP receptor, which contains only the SRX domain of SRalpha (SRalpha126/betaDN), shows a much weaker reduction in Sec61beta-Sec62 crosslinking
metabolism
-
in prokaryotic cells, the signal recognition particle consists of a SRP54 protein or Ffh and a 4.5S SRP RNA. Ffh contains a methionine-rich M domain, which binds the SRP RNA and the signal sequence on the translating ribosome. In addition, an NG domain in Ffh, comprising a GTPase G domain and a four-helix bundle N domain, forms a tight complex with a highly homologous NG domain in the SRP receptor, called FtsY in bacteria, in the presence of GTP. GTP hydrolysis at the end of the signal recognition particle cycle drives the disassembly of the Ffh-FtsY GTPase complex. The assembly of the signal recognition particle-FtsY GTPase complex and its GTPase activation require discrete conformational rearrangements in the signal recognition particle that are regulated by the RNC and the target membrane, respectively, thus ensuring the spatial and temporal precision of these molecular events during protein targeting, function of SRP RNA during co-translational protein targeting, overiew
metabolism
P08240; Q9Y5M8
two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. A second pathway promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRalpha reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes
metabolism
Q9DBG7; P47758
two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. A second pathway promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRalpha reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes
physiological function
-
the universally conserved signal recognition particle, SRP, and SRP receptor, SR, mediate the cotranslational targeting of proteins to cellular membranes. In contrast, a unique chloroplast SRP in green plants is primarily dedicated to the post-translational targeting of light harvesting chlorophyll a/b binding proteins. In both pathways, dimerization and activation between the SRP and SR GTPases mediate the delivery of cargo. Efficient assembly of the cpSRP54-cpFtsY complex is crucial for the targeting and integration of LHCP, whereas GTPase activation and/or GTP hydrolysis plays a modulatory role to help enhance the efficiency of targeting
physiological function
-
together with its receptor SR, signal recognition particle, SRP, mediates the GTP-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. The activated SRP:SR GTPase complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. The SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon
physiological function
-
the enzyme is involved in translocation of the signal recognition particle (SRP) RNA is a universally conserved and essential component of the SRP that mediates the co-translational targeting of proteins to the correct cellular membrane. During the targeting reaction, two functional ends in the signal recognition particle RNA mediate distinct functions. Whereas the RNA tetraloop facilitates initial assembly of two GTPases between the signal recognition particle and signal recognition particle receptor, this GTPase complex subsequently relocalizes about 100 A to the 5',3'-distal end of the RNA, a conformation crucial for GTPase activation and cargo handover
physiological function
P08240; Q9Y5M8
co-translational protein targeting to membranes depends on the regulated interaction of two ribonucleoprotein particles (RNPs): the ribosome and the signal recognition particle (SRP). Human SRP is composed of an SRP RNA and six proteins with the SRP GTPase SRP54 forming the targeting complex with the heterodimeric SRP receptor (SRalphabeta) at the endoplasmic reticulum membrane
physiological function
important structural dynamics relevant to cpSRP54's role in the post- and co-translational signaling processes
physiological function
P61010; P06625
the signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life
physiological function
the signal recognition particle (SRP) is an essential ribonucleoprotein particle that mediates the co-translational targeting of newly synthesized proteins to cellular membranes
physiological function
Thermochaetoides thermophila
the signal recognition particle receptor (SR) targets nascent protein chains to the endoplasmic reticulum. The eukaryotic SR consists of the two GTPases SRalpha and SRbeta. SRbeta-GTP interacts with ribosomes only in presence of SRalpha
physiological function
P08240; Q9Y5M8
two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. Both SRalpha and SRbeta are GTPases. SR inhibits translocation of Sec62-dependent substrates
physiological function
Q9DBG7; P47758
two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. Both SRalpha and SRbeta are GTPases. SR inhibits translocation of Sec62-dependent substrates
physiological function
Thermochaetoides thermophila IMI 039719
-
the signal recognition particle receptor (SR) targets nascent protein chains to the endoplasmic reticulum. The eukaryotic SR consists of the two GTPases SRalpha and SRbeta. SRbeta-GTP interacts with ribosomes only in presence of SRalpha
-
physiological function
Thermochaetoides thermophila DSM 1495
-
the signal recognition particle receptor (SR) targets nascent protein chains to the endoplasmic reticulum. The eukaryotic SR consists of the two GTPases SRalpha and SRbeta. SRbeta-GTP interacts with ribosomes only in presence of SRalpha
-
physiological function
Thermochaetoides thermophila CBS 144.50
-
the signal recognition particle receptor (SR) targets nascent protein chains to the endoplasmic reticulum. The eukaryotic SR consists of the two GTPases SRalpha and SRbeta. SRbeta-GTP interacts with ribosomes only in presence of SRalpha
-
additional information
-
concerted complex assembly and GTPase activation occurs in the chloroplast signal recognition particle. In contrast to the cytosolic homologues, GTPase activation in the chloroplast SRP-SR complex contributes marginally to the targeting of LHC proteins. Complex assembly and GTPase activation are highly coupled in the chloroplast SRP and SR and suggest that the chloroplast GTPases may forego the GTPase activation step as a key regulatory point. Homology model of the cpSRP54·cpFtsY complex based on superposition of the crystal structure of apo-cpFtsY onto that of Thermus aquaticus SR, i.e. FtsY, in complex with Ffh. Thermodynamic and kinetics for formation of the cpSRP54-cpFtsY complex, formed by wild-types and mutants, detailed overview. IBD loops play essential roles in both complex assembly and GTPase activation
additional information
-
bidentate interaction between the Ffh-FtsY GTPase complex and the distal end of the SRP RNA, overview. By modifying the GTPase docking interface, the efficiency of activation of the Ffh-FtsY GTPase complex can be specifically tuned. A guanine at residue 86 could compete with and substitute for G83 as a catalytic base. Conserved bases in loop D specifically catalyze GTP hydrolysis, a guanine at residue 86 can compete with and substitute for G83 as a catalytic base, loop E controls the action of the distal end docking sites
additional information
P61010; P06625
analysis of binding of wild-type and mutant SRalpha and SRbeta by gel filtration and immunoprecipitation, overview. SRX2, the minimum SRbeta binding domain of SRalpha, binds to the GTPase domain of SRbeta, no other regions of SRalpha are observed to bind to SRbeta. Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex, overview
additional information
analysis of the G-loop dynamics of FtsY NG domain, overview. The combination of high-resolution and multiple solved structures of FtsYNG in different states reveals a distinct sensor-relay system of the unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsYNG in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The binding of magnesium in the nucleotide site causes the reorientation of the beta-and gamma-phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions. An alternative conformation of the P-loop senses nucleotide-binding, FtsY P-loops dynamics, mechanism, detailed overview
additional information
-
analysis of the G-loop dynamics of FtsY NG domain, overview. The combination of high-resolution and multiple solved structures of FtsYNG in different states reveals a distinct sensor-relay system of the unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsYNG in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The binding of magnesium in the nucleotide site causes the reorientation of the beta-and gamma-phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions. An alternative conformation of the P-loop senses nucleotide-binding, FtsY P-loops dynamics, mechanism, detailed overview
additional information
P08240; Q9Y5M8
binding of SR to Sec61 positions SRalpha close to Sec61beta
additional information
Q9DBG7; P47758
binding of SR to Sec61 positions SRalpha close to Sec61beta
additional information
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane, in vitro and in vivo, using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. SRP binding to the receptor occurs by heterodimerization of the highly conserved NG domains of Ffh and FtsY, respectively, resulting in the formation of the so-called targeting complex. A dimerization-induced conformational switch of the nucleotide gamma-phosphate is conserved in Escherichia coli, filling an important gap in SRP GTPase activation. Asymmetries in the catalytic center affect GTP hydrolysis
additional information
-
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane, in vitro and in vivo, using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. SRP binding to the receptor occurs by heterodimerization of the highly conserved NG domains of Ffh and FtsY, respectively, resulting in the formation of the so-called targeting complex. A dimerization-induced conformational switch of the nucleotide gamma-phosphate is conserved in Escherichia coli, filling an important gap in SRP GTPase activation. Asymmetries in the catalytic center affect GTP hydrolysis
additional information
P08240; Q9Y5M8
reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions, as well as interactions within the SRP complex, overview. SRP RNA does not bind to the ribosome, while signal recognition particle (SRP) binds with nanomolar affinity involving a two-step mechanism of the key-player SRP GTPase, SRP54. SRP54 is the major determinant of SRP-ribosome interaction. Modulation of SRP-ribosome interaction by signal recognition particle receptor (SR). As long as SRP54 is not assembled into SRP, ribosome binding is of moderate affinity at most. Separating SRP biogenesis in two parts, a nucleolar and a cytosolic one, is essential for correct SRP assembly. Affinity of the entire recombinant SRPS/SR system to RNCs exposing an SRP-targeting signal
additional information
-
reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions, as well as interactions within the SRP complex, overview. SRP RNA does not bind to the ribosome, while signal recognition particle (SRP) binds with nanomolar affinity involving a two-step mechanism of the key-player SRP GTPase, SRP54. SRP54 is the major determinant of SRP-ribosome interaction. Modulation of SRP-ribosome interaction by signal recognition particle receptor (SR). As long as SRP54 is not assembled into SRP, ribosome binding is of moderate affinity at most. Separating SRP biogenesis in two parts, a nucleolar and a cytosolic one, is essential for correct SRP assembly. Affinity of the entire recombinant SRPS/SR system to RNCs exposing an SRP-targeting signal
additional information
the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane. Determination of in silico three-dimensional model of the structure of cpSRP54 by homology modeling using cytosolic homologues, overview. Single-molecule Foerster resonance energy transfer experiments reveals the presence of at least two distinct conformations. Small angle X-ray scattering shows that the linking region among the GTPase (G-domain) and methionine-rich (M-domain) domains, an M-domain loop, and the cpSRP43 binding C-terminal extension of cpSRP54 are predominantly disordered. The linker and loop segments are observed to play an important role in organizing the domain arrangement of cpSRP54
additional information
the SRP RNAis a universally conserved component of SRP that mediates key interactions between two GTPases in SRP and its receptor, thus enabling rapid delivery of cargo to the target membrane. Notably, this essential RNA is bypassed in the chloroplast (cp) SRP of green plants. The cpSRP and cpSRP receptor GTPases (cpSRP54 and cpFtsY, respectively) interact efficiently by themselves without the SRP RNA, molecular mechanism, overview
additional information
Thermochaetoides thermophila
the structures of the SRbeta-GTPase in its GTP- and GDP-states describe a switch cycle revealing a fixed switch II region. The linker region between the N-terminal SRX domain and the C-terminal NG domain of SRalpha is crucial for ribosome binding of the SR. Analysis of the structure of the ctSRbeta-GTP/SRX complex and of ctSRbeta-GDP complex, overview. The conformation of SRbeta does not directly influence ribosome binding but rather regulates the SRX interaction during the switch cycle. ctSRbeta contains all consensus fingerprints that define the SRbeta family, which like for all GTPases cluster around the nucleotide. The fingerprints are GxxxxGKS/T64 for the P loop, TxxS107 within the switch I region (residues 99-110), DxPGHxxLR154 within the switch II region (residues 146-160), and NKxD253 for the guanine binding pocket. The catalytic residue His150 is in a resting position pointing outward of the active center, rendering the ctSRbeta-GTP/SRX complex inactive. The histidine is tied to the backbone nitrogen of Lys152 within switch II and therefore it must be available in the deprotonated form. A unique feature of SRbeta applies to the switch II fingerprint. The conserved fingerprint within Arf and Sar1 writes as DxGG(QArf/HSar1)xxxRxW, and this signature is the prerequisite for the family-specific interswitch toggle mechanism. While most of the fingerprint is conserved in the SRb family, the first glycine is replaced by the rigid proline and the terminal tryptophan is not present. CtSRX not only contacts switch I, but also interacts with the N-terminal turn of helix alpga2 (HxxL153) in the switch II region. Most importantly, the C-terminal Pi-helical turn of helix alpha1x (X1xxFFX2) sequesters the catalytic histidine His150 away from the active center
additional information
Thermochaetoides thermophila IMI 039719
-
the structures of the SRbeta-GTPase in its GTP- and GDP-states describe a switch cycle revealing a fixed switch II region. The linker region between the N-terminal SRX domain and the C-terminal NG domain of SRalpha is crucial for ribosome binding of the SR. Analysis of the structure of the ctSRbeta-GTP/SRX complex and of ctSRbeta-GDP complex, overview. The conformation of SRbeta does not directly influence ribosome binding but rather regulates the SRX interaction during the switch cycle. ctSRbeta contains all consensus fingerprints that define the SRbeta family, which like for all GTPases cluster around the nucleotide. The fingerprints are GxxxxGKS/T64 for the P loop, TxxS107 within the switch I region (residues 99-110), DxPGHxxLR154 within the switch II region (residues 146-160), and NKxD253 for the guanine binding pocket. The catalytic residue His150 is in a resting position pointing outward of the active center, rendering the ctSRbeta-GTP/SRX complex inactive. The histidine is tied to the backbone nitrogen of Lys152 within switch II and therefore it must be available in the deprotonated form. A unique feature of SRbeta applies to the switch II fingerprint. The conserved fingerprint within Arf and Sar1 writes as DxGG(QArf/HSar1)xxxRxW, and this signature is the prerequisite for the family-specific interswitch toggle mechanism. While most of the fingerprint is conserved in the SRb family, the first glycine is replaced by the rigid proline and the terminal tryptophan is not present. CtSRX not only contacts switch I, but also interacts with the N-terminal turn of helix alpga2 (HxxL153) in the switch II region. Most importantly, the C-terminal Pi-helical turn of helix alpha1x (X1xxFFX2) sequesters the catalytic histidine His150 away from the active center
-
additional information
Thermochaetoides thermophila DSM 1495
-
the structures of the SRbeta-GTPase in its GTP- and GDP-states describe a switch cycle revealing a fixed switch II region. The linker region between the N-terminal SRX domain and the C-terminal NG domain of SRalpha is crucial for ribosome binding of the SR. Analysis of the structure of the ctSRbeta-GTP/SRX complex and of ctSRbeta-GDP complex, overview. The conformation of SRbeta does not directly influence ribosome binding but rather regulates the SRX interaction during the switch cycle. ctSRbeta contains all consensus fingerprints that define the SRbeta family, which like for all GTPases cluster around the nucleotide. The fingerprints are GxxxxGKS/T64 for the P loop, TxxS107 within the switch I region (residues 99-110), DxPGHxxLR154 within the switch II region (residues 146-160), and NKxD253 for the guanine binding pocket. The catalytic residue His150 is in a resting position pointing outward of the active center, rendering the ctSRbeta-GTP/SRX complex inactive. The histidine is tied to the backbone nitrogen of Lys152 within switch II and therefore it must be available in the deprotonated form. A unique feature of SRbeta applies to the switch II fingerprint. The conserved fingerprint within Arf and Sar1 writes as DxGG(QArf/HSar1)xxxRxW, and this signature is the prerequisite for the family-specific interswitch toggle mechanism. While most of the fingerprint is conserved in the SRb family, the first glycine is replaced by the rigid proline and the terminal tryptophan is not present. CtSRX not only contacts switch I, but also interacts with the N-terminal turn of helix alpga2 (HxxL153) in the switch II region. Most importantly, the C-terminal Pi-helical turn of helix alpha1x (X1xxFFX2) sequesters the catalytic histidine His150 away from the active center
-
additional information
Thermochaetoides thermophila CBS 144.50
-
the structures of the SRbeta-GTPase in its GTP- and GDP-states describe a switch cycle revealing a fixed switch II region. The linker region between the N-terminal SRX domain and the C-terminal NG domain of SRalpha is crucial for ribosome binding of the SR. Analysis of the structure of the ctSRbeta-GTP/SRX complex and of ctSRbeta-GDP complex, overview. The conformation of SRbeta does not directly influence ribosome binding but rather regulates the SRX interaction during the switch cycle. ctSRbeta contains all consensus fingerprints that define the SRbeta family, which like for all GTPases cluster around the nucleotide. The fingerprints are GxxxxGKS/T64 for the P loop, TxxS107 within the switch I region (residues 99-110), DxPGHxxLR154 within the switch II region (residues 146-160), and NKxD253 for the guanine binding pocket. The catalytic residue His150 is in a resting position pointing outward of the active center, rendering the ctSRbeta-GTP/SRX complex inactive. The histidine is tied to the backbone nitrogen of Lys152 within switch II and therefore it must be available in the deprotonated form. A unique feature of SRbeta applies to the switch II fingerprint. The conserved fingerprint within Arf and Sar1 writes as DxGG(QArf/HSar1)xxxRxW, and this signature is the prerequisite for the family-specific interswitch toggle mechanism. While most of the fingerprint is conserved in the SRb family, the first glycine is replaced by the rigid proline and the terminal tryptophan is not present. CtSRX not only contacts switch I, but also interacts with the N-terminal turn of helix alpga2 (HxxL153) in the switch II region. Most importantly, the C-terminal Pi-helical turn of helix alpha1x (X1xxFFX2) sequesters the catalytic histidine His150 away from the active center
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). E3TF13_ICTPU
193
0
21949
TrEMBL
other Location (Reliability: 2)
E3TFY4_ICTPU
201
0
22581
TrEMBL
other Location (Reliability: 2)
E3TFX3_ICTPU
208
0
23603
TrEMBL
other Location (Reliability: 4)
A0A8M1PIP3_DANRE
86
0
10076
TrEMBL
other Location (Reliability: 2)
A0A2G9GNI6_9LAMI
119
0
13339
TrEMBL
other Location (Reliability: 2)
A0A061IEN5_CRIGR
410
0
46714
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0U1WP62_KARMI
316
8
34824
TrEMBL
Secretory Pathway (Reliability: 1)
H6N5W5_MYCHN
Mycoplasma haemocanis (strain Illinois)
445
0
50249
TrEMBL
-
E3TFG9_ICTPU
197
0
22234
TrEMBL
other Location (Reliability: 2)
E3TGM4_ICTPU
184
0
20548
TrEMBL
Secretory Pathway (Reliability: 2)
E3TDZ6_ICTPU
201
0
23030
TrEMBL
other Location (Reliability: 3)
G7KQW9_MEDTR
553
0
60843
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6RC35_ROSCH
568
0
62550
TrEMBL
Chloroplast (Reliability: 1)
A0A8M1PGX0_DANRE
141
0
15850
TrEMBL
other Location (Reliability: 2)
G8C2I4_9MOLU
460
0
52212
TrEMBL
-
F7XUX3_MIDMI
Midichloria mitochondrii (strain IricVA)
218
0
23642
TrEMBL
-
A0A1Z5K6C0_FISSO
555
0
60992
TrEMBL
other Location (Reliability: 3)
A0A072ULN5_MEDTR
391
0
43658
TrEMBL
other Location (Reliability: 5)
F6S322_XENTR
200
4
21688
TrEMBL
Secretory Pathway (Reliability: 1)
E3TC22_ICTFU
109
0
12966
TrEMBL
other Location (Reliability: 5)
A0A2G9I0V8_9LAMI
373
0
41519
TrEMBL
Chloroplast (Reliability: 2)
A0A5B7AVE5_DAVIN
332
0
37037
TrEMBL
other Location (Reliability: 2)
A0A1Z5KE64_FISSO
571
0
61488
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1Z5JT64_FISSO
556
0
61136
TrEMBL
other Location (Reliability: 2)
A0A5Q0UFY0_9ARCH
429
0
47635
TrEMBL
-
E3TF97_ICTPU
207
0
23476
TrEMBL
other Location (Reliability: 2)
E3TEI0_ICTPU
217
0
23485
TrEMBL
other Location (Reliability: 4)
A0A1Z5KQ54_FISSO
567
0
61306
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396H272_MEDTR
168
0
18558
TrEMBL
other Location (Reliability: 1)
A0A061ICH9_CRIGR
324
0
37012
TrEMBL
Secretory Pathway (Reliability: 5)
E3TC89_ICTFU
193
0
21949
TrEMBL
other Location (Reliability: 2)
A0A6J8DE17_MYTCO
959
0
112147
TrEMBL
Secretory Pathway (Reliability: 2)
A0A396H3Z9_MEDTR
171
0
19593
TrEMBL
other Location (Reliability: 2)
E3TFX5_ICTPU
221
0
24586
TrEMBL
other Location (Reliability: 1)
A0A061IHG2_CRIGR
123
1
13509
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PT06_ROSCH
372
0
40711
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6RIZ2_ROSCH
208
0
22904
TrEMBL
other Location (Reliability: 3)
E3TFG5_ICTPU
176
0
20700
TrEMBL
other Location (Reliability: 2)
E3TDR0_ICTPU
192
0
21784
TrEMBL
other Location (Reliability: 3)
A0A067XSB5_KARVE
250
4
28452
TrEMBL
Secretory Pathway (Reliability: 1)
E3TGM7_ICTPU
199
0
22243
TrEMBL
other Location (Reliability: 3)
E3TFU1_ICTPU
200
4
21397
TrEMBL
Secretory Pathway (Reliability: 1)
E3TE62_ICTPU
205
0
23233
TrEMBL
other Location (Reliability: 5)
E3TEY0_ICTPU
262
0
29680
TrEMBL
other Location (Reliability: 3)
E3TDY5_ICTPU
390
0
44002
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PDX5_ROSCH
215
0
23535
TrEMBL
other Location (Reliability: 2)
E3TFU4_ICTPU
354
0
40295
TrEMBL
other Location (Reliability: 3)
E3TG48_ICTPU
184
0
20609
TrEMBL
other Location (Reliability: 5)
B5DG80_SALSA
396
1
45077
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9GEZ5_9LAMI
300
0
33211
TrEMBL
other Location (Reliability: 2)
E3TEJ5_ICTPU
218
0
24494
TrEMBL
other Location (Reliability: 1)
E3TFH9_ICTPU
267
5
29952
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7AV75_DAVIN
194
0
21571
TrEMBL
other Location (Reliability: 4)
E3TC99_ICTFU
192
0
21416
TrEMBL
other Location (Reliability: 2)
E3TE02_ICTPU
218
0
24431
TrEMBL
other Location (Reliability: 2)
A0A396H2I8_MEDTR
314
0
35823
TrEMBL
other Location (Reliability: 5)
G0SD15_CHATD
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
514
0
55983
TrEMBL
-
SR54C_ARATH
564
0
61232
Swiss-Prot
other Location (Reliability: 2)
Q8U051_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
322
0
35813
TrEMBL
-
SRP54_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
443
0
49879
Swiss-Prot
-
SRP14_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
106
0
11718
Swiss-Prot
-
FTSY_ECOLI
Escherichia coli (strain K12)
497
0
54513
Swiss-Prot
other Location (Reliability: 2)
SRP54_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
447
0
50047
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
34900
apo-enzyme, analytical ultracentrifugation and small-angle X-ray scattering
43000
54000
43000
-
1 * 54000 + 1 * 43000, chloroplast signal recognition particle is a heterodimer consisting of a 54 kDa GTPase (cpSRP54) subunit, and a 43 kDa subunit (cpSRP43)
43000
1 * 54000 + 1 * 43000, chloroplast signal recognition particle protein is a heterodimer formed by the subunits cpSRP54 and cpSRP43, X-ray crystallography
54000
-
1 * 54000 + 1 * 43000, chloroplast signal recognition particle is a heterodimer consisting of a 54 kDa GTPase (cpSRP54) subunit, and a 43 kDa subunit (cpSRP43)
54000
1 * 54000 + 1 * 43000, chloroplast signal recognition particle protein is a heterodimer formed by the subunits cpSRP54 and cpSRP43, X-ray crystallography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 22400-25600, recombinant M-domain of subunit SRP54, SDS-PAGE and SAXS
heterodimer
homodimer
monomer
additional information
heterodimer
-
1 * 54000 + 1 * 43000, chloroplast signal recognition particle is a heterodimer consisting of a 54 kDa GTPase (cpSRP54) subunit, and a 43 kDa subunit (cpSRP43)
heterodimer
1 * 54000 + 1 * 43000, chloroplast signal recognition particle protein is a heterodimer formed by the subunits cpSRP54 and cpSRP43, X-ray crystallography
heterodimer
-
cpSRP lacks an RNA moiety and functions as a heterodimer composed of a conserved 54-kDa guanosine triphosphatase (cpSRP54) and a unique 43-kDa subunit (cpSRP43)
heterodimer
the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane. Determination of in silico three-dimensional model of the structure of cpSRP54 by homology modeling using cytosolic homologues. Single-molecule Foerster resonance energy transfer experiments reveals the presence of at least two distinct conformations. Small angle X-ray scattering shows that the linking region among the GTPase (G-domain) and methionine-rich (M-domain) domains, an M-domain loop, and the cpSRP43 binding C-terminal extension of cpSRP54 are predominantly disordered. The linker and loop segments are observed to play an important role in organizing the domain arrangement of cpSRP54. Domain structure, overview. The orientation of the M-domain varies in different SRP54s and bacterial homologues Ffhs, structure comparisons of wild-type and mutants and enzyme from other species, detailed overview. Subunit cpSRP54 exists in at least two different conformations
heterodimer
P61010; P06625
the signal recognition particle (SRP) receptor is a heterodimer of two polypeptides (SRalpha and SRbeta) that each contain a GTP binding domain. The GTP binding domain in the peripheral membrane SRalpha subunit has a well defined role in regulating targeting of SRP ribosome-nascent chain complexes to the translocon. Without bound GTP, the empty form of the SRbeta GTPase domain is unable to dimerize with SRalpha
heterodimer
-
Ffh and FtsY associate into a heterodimer upon GTP binding, upon GTP hydrolysis Ffh and FtsY dissociate
heterodimer
P08240; Q9Y5M8
1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE
heterodimer
Q9DBG7; P47758
1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE
heterodimer
Thermochaetoides thermophila
SRP GTPases are multi-domain proteins. SRalpha consists of an N-terminal SNARE-like Longin domain (SRX domain) that is connected by a long flexible linker to the NG domain, which harbors the GTPase activity. The SRX domain is responsible for interaction with the SRbeta GTPase in a GTP-dependent manner
heterodimer
Thermochaetoides thermophila CBS 144.50
-
SRP GTPases are multi-domain proteins. SRalpha consists of an N-terminal SNARE-like Longin domain (SRX domain) that is connected by a long flexible linker to the NG domain, which harbors the GTPase activity. The SRX domain is responsible for interaction with the SRbeta GTPase in a GTP-dependent manner
-
heterodimer
Thermochaetoides thermophila DSM 1495
-
SRP GTPases are multi-domain proteins. SRalpha consists of an N-terminal SNARE-like Longin domain (SRX domain) that is connected by a long flexible linker to the NG domain, which harbors the GTPase activity. The SRX domain is responsible for interaction with the SRbeta GTPase in a GTP-dependent manner
-
heterodimer
Thermochaetoides thermophila IMI 039719
-
SRP GTPases are multi-domain proteins. SRalpha consists of an N-terminal SNARE-like Longin domain (SRX domain) that is connected by a long flexible linker to the NG domain, which harbors the GTPase activity. The SRX domain is responsible for interaction with the SRbeta GTPase in a GTP-dependent manner
-
heterodimer
-
FtsY and Ffh assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex
monomer
Thermochaetoides thermophila CBS 144.50
-
SRbeta is a small monomeric GTPase
-
monomer
Thermochaetoides thermophila DSM 1495
-
SRbeta is a small monomeric GTPase
-
monomer
Thermochaetoides thermophila IMI 039719
-
SRbeta is a small monomeric GTPase
-
additional information
-
homology modeling and structure analysis, overview
additional information
P61010; P06625
determination of the crystal structure of the GTPase heterodimers, and structure comparisons, overview
additional information
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. Biochemical analysis and integrative modeling suggest that the homodimer employs the same interface as the heterodimer. Ffh does not homodimerize while FtsY is able to form a homodimer. FtsY homodimer and FtsY/Ffh heterodimer share a similar interface
additional information
-
efficient protein targeting requires heterodimerization and activation of the GTPases present in the SRP receptor FtsY and the SRP protein Ffh. FtsY also forms a homodimer at the membrane using the same interaction surface as the heterodimer. Homodimerization adds to the complex interaction landscape of protein targeting. Biochemical analysis and integrative modeling suggest that the homodimer employs the same interface as the heterodimer. Ffh does not homodimerize while FtsY is able to form a homodimer. FtsY homodimer and FtsY/Ffh heterodimer share a similar interface
additional information
P08240; Q9Y5M8
in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases
additional information
Q9DBG7; P47758
in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
PAB0955 is able to phosphorylate itself in vitro at 80°C only in the presence of GTP and Mg2+ ions
ribonucleoprotein
ribonucleoprotein
-
SRP comprises the Ffh protein and 4.5S RNA, which together recognize hydrophobic signal peptides as they emerge from translating ribosomes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit cpSRP43 in complex with a synthetic L18 peptide, hanging drop vapour diffusion method, using
the crystal structure of cpFtsY with bound malonate is solved at 1.75 A resolution
-
SRalpha and SRbeta complex, X-ray diffraction structure determination and analysis
P61010; P06625
purified recombinant isolated FtsYNG domain in the nucleotide-free (apo) form, the GDP-bound, and the non-hydrolysable GTP-bound form (including GMPPNP (5'-guanylyl imidodiphosphate) and GMPPCP (beta,gamma-methyleneguanosine 5'-triphosphate)), X-ray diffraction structure determination and analysis at 1.22-1.88 A resolution
signal recognition particle in complex with its receptor, X-ray diffraction structure determination and analysis at 3.94 A resolution
-
hanging drop vapor diffusion method, 2.45 A crystal structure of the mammalian SRbeta in its Mg2+GTP-bound state in complex with the minimal binding domain of SRalpha termed SRX
-
crystal structure of the S-domain of signal-recognition-particle RNA at 2.6 A
-
hanging drop vapor diffusion method, 2.45 A crystal structure of the mammalian SRbeta in its Mg2+GTP-bound state in complex with the minimal binding domain of SRalpha termed SRX
-
ammonium sulfate precipitation or sodium citrate precipitation, structures of the NG domain of FtsY in two different forms: an apo and a sulfate-loaded form
-
the crystal structure of PAB0955, free and in complex with six different nucleotides, is determined
-
free and GDP-magnesium-bound forms, hanging drop vapour diffusion method, the hexagonal form grows in 1.1-1.5 M ammonium phosphate and 100 mM sodium acetate pH 5.0. The monoclinic form grows in 0.9-1.2 M lithium sulfate, 0.4-0.6 M ammonium sulfate, and 100 mM sodium citrate pH 5.0. For the GDP-bound structure, best crystals grow in 14-17% (w/v) PEG 8000 and 100 mM Tris pH 8.0
GDP-bound subunit SRP54 and free subunit SRP19 are crystallized by hanging drop vapour diffusion method, crystals of SRP54 grow in 1.0-1.3 M lithium sulfate and 100 mM sodium acetate pH 5.0, crystals of SRP19 grow in 1.2-1.3 M sodium malonate and 100 mM sodium acetate pH 5.0
crystal structure of SRP54 with and without its cognate RNA binding site
-
hanging drop vapour diffusion method, at 21°C, using 50 mM cacodylic acid pH 6.5, 22% (w/v) PEG 4000, and 50 mM sodium acetate
purified recombinant SRbeta in complex with the SRX domain of SRalpha in the GTP-bound state and of GDP- and GDP-Mg2+-bound SRbeta, X-ray diffraction structure determination and analysis at 1.9-3.2 A resolution
Thermochaetoides thermophila
crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface
-
the 2.1 A X-ray structure of FtsY from Thermus aquaticus bound to GDP is reported
-
the structure of the GMPPNP-stabilized complex of Thermus aquaticus Ffh and FtsY NG domains is determined at 1.97 A resolution
-
two structures of the SRP GTPase Ffh NG-domains are determined at 1.1 A resolution providing the basis for comparative examination of the extensive water structure of the apo conformation
-
X-ray structure of a complex of the N and G domains of Ffh with the GTPase FtsY of the SRP receptor in the presence of the non-hydrolyzable GTP analogue GMPPCP
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Thr112Ala
A142W
-
site-directed mutagenesis, the mutant cpSRP54 exhibits the same GTP-dependent complex assembly kinetics as wild-type cpSRP54
A143L
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A143W
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A168W
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A169L
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A169W
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
D137A
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
D163A
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
F33L
-
mutation in the N-domain modulates the interaction kinetic between cpSRP54 and cpFtsY
F71V
-
mutation in the N-domain modulates the interaction kinetic between cpSRP54 and cpFtsY
R140A
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
R166A
-
site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
S54C/K407C
site-directed mutagenesis, mutations S54C in the N-domain and K407C in the M-domain of cpSRP54r resulting in mutant cpSRP54S54C/K407C
V339N/L370N
site-directed mutagenesis, mutant cpSRP54V339N/L370N of the mature enyme
DELTAflhF1
-
flhF fragment from bp +282 to +1071 relative to the translational initiation site
DELTAflhF2
-
flhF fragment from bp +210 to +685 relative to the translational initiation site
D181N
G118L
G118L/D181N
H119L
K75I
K75I/H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a null mutant phenotype and no binding of SRalpha
N178K
C86A
-
mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, C86 and C86G reduce GTPase activity by only 50%
C86G
-
mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, DELTAC86 and C86G reduce GTPase activity by only 50%. Despite defective GTP hydrolysis, the G83A mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
C86U
-
mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, C86 and C86G reduce GTPase activity by only 50%
C87A/C97U
-
site-directed mutagenesis, combining C97U with C87A generates a superactive SRP RNA double mutant that hydrolyzes GTP 5.5fold faster than wild-type SRP RNA
C97U
-
site-directed mutagenesis, the mutant prolongs GTPase docking at the distal end, which correlates with its faster GTP hydrolysis rate
C97U/G99A
-
site-directed mutagenesis, combining G99A with C87A generate s a superactive SRP RNA double mutant that hydrolyzes GTP 4.6fold faster than wild-type SRP RNA
F240V
-
mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
G257A
-
residue resides at the N-GTPase domain interface, mutation produces a lethal phenotype, it does not significantly affect Ffh function, but severely reduces interaction with FtsY
G455W
G83A
-
deletion or substitution of G83 by any other nucleotide completely abolishes the stimulatory effect of the SRP RNA on GTP hydrolysis. Despite defective GTP hydrolysis, the G83A mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
G99A
-
site-directed mutagenesis, the mutant prolongs GTPase docking at the distal end, which correlates with its faster GTP hydrolysis rate
L199F
-
mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
G257A
-
residue resides at the N-GTPase domain interface, mutation produces a lethal phenotype, it does not significantly affect Ffh function, but severely reduces interaction with FtsY
-
F48A
-
the cpFtsY mutant exhibits a GTP hydrolysis rate 4times greater than wild type cpFtsY in the absence of liposomes, the mutation reduces light-harvesting chlorophyll-binding protein integration efficiency by nearly 80%
F49A
-
the mutation reduces light-harvesting chlorophyll-binding protein integration efficiency by nearly 40%
A145S
-
substitution introduced into the putative GTP binding motif GXXGXGK
G141V
-
substitution introduced into the putative GTP binding motif GXXGXGK
G222V
-
substitution introduced into the putative GTP binding motif GXXGXGK
GAK-VSG
-
substitution introduced into the putative GTP binding motif GXXGXGK
GTK-VSG
-
substitution introduced into the putative GTP binding motif GXXGXGK
K147G
-
substitution introduced into the putative GTP binding motif GXXGXGK
K228G
-
substitution introduced into the putative GTP binding motif GXXGXGK
T226S
-
substitution introduced into the putative GTP binding motif GXXGXGK
additional information
D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level, but no binding in absence of GTP. SRalpha binding to D181N can be restored to some level by adding back nucleotide, i.e. GTP, GDP, XTP or XDP, but not with ATP
G118L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and binding of SRalpha at wild-type level
G118L/D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta) and weak binding of SRalpha
H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level
K75I
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and no binding of SRalpha
N178K
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and weak binding of SRalpha
G455W
-
mutant, exhibits no significant GTP hydrolysis and defective in SRP-FtsY complex formation
additional information
-
binding kinetics and competing inhibitions with several bacterial cpFtsY mutants, affinities of mutant bacterial cpFtsYs for cpSRP54, and complex formations, overview
additional information
-
flhF::cat mutant strain assembles flagella and is motile
additional information
-
flhF::cat mutant strain assembles flagella and is motile
-
additional information
-
SRbetaC1-deltaTM, hydrolysis of XTP favored over GTP
additional information
-
SRbeta-deltaloop, hydrolysis of XTP favored over GTP
additional information
-
SRbeta-deltaTM, hydrolysis of XTP favored over GTP
additional information
-
Srbeta-loop2, hydrolysis of XTP favored over GTP
additional information
P61010; P06625
construction of several deletion mutants: SRbeta-DELTATM, SRbetaDELTA4, SRbetaDELTA5, SRbeta1C1-DELTATM, SRbeta-DELTAloop, and SRbeta-loop2, phenotypes, altered SRalpha binding of the truncated mutants, overview. Deletion of the last 6 amino-acids from the carboxyl-terminus of the SRbeta GTPase domain results in a molecule (SRbetaC1) with primarily type I topology, similar to SRbeta
additional information
-
FtsY mutated in the 4th GTP-binding consensus element displays reduced GTP-binding and -hydrolysis which correlates with a reduced ability to interact with SRP
additional information
-
4.5S RNA tetraloop mutants UUCG, UUUU, CUUC, GUAA and GAAA
additional information
-
several mutants show higher GTPase activity than wild-type SRP RNA, most notably mutations at G99, U12, and C97. By modifying the GTPase docking interface, the efficiency of activation of the Ffh-FtsY GTPase complex can be specifically tuned. When G83 is mutated, substitution of C86 with guanine rescues the SRP RNA-mediated stimulation of GTPase activity to 50% of wild-type rate. Despite defective GTP hydrolysis, neither the G83A nor C86G mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
additional information
construction of the FtsYDELTAN1 mutant, and creation of a fusion construct comprising two FtsYDELTAN1 molecules linked via a 31-amino-acid GS linker, similar to the situation for the FtsY/Ffh heterodimer (FtsYDELTAN12)
additional information
-
construction of the FtsYDELTAN1 mutant, and creation of a fusion construct comprising two FtsYDELTAN1 molecules linked via a 31-amino-acid GS linker, similar to the situation for the FtsY/Ffh heterodimer (FtsYDELTAN12)
additional information
P08240; Q9Y5M8
construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct
additional information
P08240; Q9Y5M8
two-site binding analysis of the SRP54DELTAC-ribosome interaction. Having a signal sequence fused to SRP54 or presented by the ribosome does not seem to significantly change SRP binding to the ribosome
additional information
-
two-site binding analysis of the SRP54DELTAC-ribosome interaction. Having a signal sequence fused to SRP54 or presented by the ribosome does not seem to significantly change SRP binding to the ribosome
additional information
Q9DBG7; P47758
construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct
additional information
Thermochaetoides thermophila
while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
additional information
Thermochaetoides thermophila CBS 144.50
-
while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
-
additional information
Thermochaetoides thermophila DSM 1495
-
while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
-
additional information
Thermochaetoides thermophila IMI 039719
-
while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ffh NG is purified, the Ffh NG-FtsY NGd20 complex is purified using ion exchange chromatography, a Q Sepharose and a SP Sepharose column
-
FtsY NGd20 is purified, the Ffh NG-FtsY NGd20 complex is purified using ion exchange chromatography, a Q Sepharose and a SP Sepharose column
-
glutathione Sepharose column chromatography
heat selective precipitation, cobalt-chelating affinity chromatography, gel filtration, and ion-exchange chromatography
HiPrep heparin Sepharose column chromatography, SP Sepharose column chromatography, and Superdex 75 gel filtration
proteins are purified using histidine-binding magnetic agarose beads
-
recombinant C-terminally His6-tagged wild-type and mutant mature cpSRP54 (residues 76-564) from Escherichia coli strain BL21 Star
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography,anion exchange chromatography, and cation exchange chromatography, followed by gel filtration
Q9DBG7; P47758
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21(DE3)
Thermochaetoides thermophila
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21(DE3) by nickel affinity chromatography,anion exchange chromatography, and cation exchange chromatography, followed by gel filtration
P08240; Q9Y5M8
recombinant His6-tagged signal recognition particle protein cpSRP54 from Escherichia coli strain Rosetta by nickel affinity chromatography, cation exchange chromatography, and anion exchange chromatography
recombinant wild-type and mutant cpSRP54 from Escherichia coli strain Rosetta BL21 by two steps of cation exchange chromatography
-
the FtsY NGd20 protein is purified over a HiTrap Blue column, desalted, then passed over a HiTrap SP and a HiTrap Q Sepharose column
-
heat selective precipitation, cobalt-chelating affinity chromatography, gel filtration, and ion-exchange chromatography
heat selective precipitation, cobalt-chelating affinity chromatography, gel filtration, and ion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a construct of Thermus aquaticus FtsY in which the first 20 amino acids are deleted is subsequently expressed
-
expression in Escherichia coli
expression of wild-type and mutant cpSRP54 in Escherichia coli strain Rosetta BL21
-
gene CPSRP54, recombinant overexpression of His6-tagged signal recognition particle protein cpSRP54 in Escherichia coli strain Rosetta, coexpression with signal recognition particle activator protein cpFtsY forming the cpSRP54-cpFtsY complex
recombinant expression of C-terminally His6-tagged wild-type and mutant mature cpSRP54 (residues 76-564) in Escherichia coli strain BL21 Star
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21 (DE3)
Q9DBG7; P47758
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3)
recombinant large-scale production of all human SRP components and the reconstitution of homogeneous signal recognition particle (SRP) and signal recognition particle receptor (SR) complexes
P08240; Q9Y5M8
the Escherichia coli strain TOP10 is used for general cloning stategies and the strain SCS110 as an intermediary host in Bacillus cereus transformation experiments, the vectors pRN5101 and pDG148 are used
-
the NG domain of Ffh is cloned into pUCm-T, and into pET-15b for expression in Escherichia coli BL21 cells
-
the NG domain of FtsY is cloned into pUCm-T, and into pET-15b for expression in Escherichia coli BL21 cells
-
the NG domain of Thermus aquaticus Ffh is cloned and subsequently expressed
-
the vector pJGS3 expressing the protein FtsY NGd20, in which the N-terminal residues 2-20 of FtsY are deleted, is constructed by PCR-based site-directed mutagenesis of pTB88 for expression in Escherichia coli Rosetta-2DE3 pLysS cells
-
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3)
P08240; Q9Y5M8
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
protein translocation across the endoplasmic reticulum
medicine
-
protein translocation across the endoplasmic reticulum
medicine
-
protein translocation across the endoplasmic reticulum
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Conolly, T.; Gilmore, R.
The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
Cell
57
599-610
1989
Canis lupus familiaris
Conolly, T.; Rapiejko, P.J.; Gilmore, R.
Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor
Science
252
1171-1173
1991
Triticum aestivum
Samuelsson, T.; Olsson, M.
GTPase activity of a bacterial SRP-like complex
Nucleic Acids Res.
21
847-853
1993
Mycoplasma mycoides, Mycoplasma mycoides SRPM54
Miller, J.D.; Wilhelm, H.; Gierasch, L.; Gilmore, R.; Walter, P.
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
Nature
366
351-354
1993
Escherichia coli
Conolly, T.; Gilmore, R.
GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor
J. Cell Biol.
123
799-807
1993
Canis lupus familiaris
Zopf, D.; Bernstein, H.D.; Walter, P.
GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding
J. Cell Biol.
120
1113-1121
1993
Canis lupus familiaris
Miller, J.D.; Tajima, S.; Lauffer, L.; Walter, P.
The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alph subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane
J. Cell Biol.
128
273-282
1995
Canis lupus familiaris
Kusters, R.; Lentzen, G.; Eppens, E.; van Geel, A.; van der Weijden, C.C.; Wintermeyer, W.; Luirink, J.
The functioning of the SRP receptor FtsY in protein-targeting in E.coli is correlated with its ability to bind and hydrolyse GTP
FEBS Lett.
372
253-258
1995
Escherichia coli
Bacher, G.; Lutcke, H.; Jungnickel, B.; Rapoport, T.A.; Dobberstein, B.
Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
Nature
381
248-251
1996
Triticum aestivum
Macao, B.; Luirink, J.; Samuelsson, T.
Ffh and FtsY in a Mycoplasma mycoides signal-recognition particle pathway: SRP RNA and M domain of Ffh are not required for stimulation of GTPase activity in vitro
Mol. Microbiol.
24
523-534
1997
Mycoplasma mycoides, Mycoplasma mycoides MmFtsY
Freymann, D.M.; Keenan, R.J.; Stroud, R.M.; Walter, P.
Structure of the conserved GTPase domain of the signal recognition particle
Nature
385
361-364
1997
Thermus aquaticus
Moll, R.; Schmidtke, S.; Petersen, A.; Schfer, G.
The signal recognition particle receptor alpha subunit of the hyperthermophilic archaeon Acidianus ambivalens exhibits an intrinsic GTP-hydrolyzing activity
Biochim. Biophys. Acta
1335
218-230
1997
Acidianus ambivalens
Farmery, M.; Macao, B.; Larsson, T.; Samuelsson, T.
Binding of GTP and GDP induces a significant conformational change in the GTPase domain of Ffh, a bacterial homologue of the SRP 54 kDa subunit
Biochim. Biophys. Acta
1385
61-68
1998
Mycoplasma mycoides, Mycoplasma mycoides Ffh
Ogg, S.C.; Barz, W.P.; Walter, P.
A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit
J. Cell Biol.
142
341-354
1998
Saccharomyces cerevisiae
Bacher, G.; Pool, M.; Dobberstein, B.
The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor
J. Cell Biol.
146
723-730
1999
Canis lupus familiaris
Montoya, G.; te Kaat, K.; Moll, R.; Schfer, G.; Sinning, I.
Crystallization and preliminary x-ray diffraction studies on the conserved GTPase domain of the signal recognition particle from Acidianus ambivalens
Acta Crystallogr. Sect. D
55
1949-1951
1999
Acidianus ambivalens, Acidianus ambivalens Ffh
Moll, R.; Schmidtke, S.; Schfer, G.
Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens Ffh-homologous protein suggest an SRP-like complex in archaea
Eur. J. Biochem.
259
441-448
1999
Acidianus ambivalens, Acidianus ambivalens Ffh
Legate, K.R.; Falcone, D.; Andrews, D.W.
Nucleotide-dependent binding of the GTPase domain of the signal recognition particle receptor beta-subunit to the alpha-subunit
J. Biol. Chem.
275
27439-27446
2000
Canis lupus familiaris
Peluso, P.; Shan, S.O.; Nock, S.; Herschlag, D.; Walter, P.
Role of SRP RNA in the GTPase cycles of Ffh and FtsY
Biochemistry
40
15224-15233
2001
Escherichia coli
Lu, Y.; Qi, H.Y.; Hyndman, J.B.; Ulbrandt, N.D.; Teplyakov, A.; Tomasevic, N.; Bernstein, H.D.
Evidence for a novel GTPase priming step in the SRP protein targeting pathway
EMBO J.
20
6724-6734
2001
Escherichia coli, Escherichia coli WAM121
Zanen, G.; Antelmann, H.; Westers, H.; Hecker, M.; van Dijl, J.M.; Quax, W.J.
FlhF, the third signal recognition particle-GTPase of Bacillus subtilis, is dispensable for protein secretion
J. Bacteriol.
186
5956-5960
2004
Bacillus subtilis, Bacillus subtilis 168
Swain, J.F.; Gierasch, L.M.
Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle
J. Biol. Chem.
276
12222-12227
2001
Escherichia coli
Egea, P.F.; Shan, S.O.; Napetschnig, J.; Savage, D.F.; Walter, P.; Stroud, R.M.
Substrate twinning activates the signal recognition particle and its receptor
Nature
427
215-221
2004
Thermus aquaticus
Rosendal, K.R.; Wild, K.; Montoya, G.; Sinning, I.
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
Proc. Natl. Acad. Sci. USA
100
14701-14706
2003
Saccharolobus solfataricus
Shan, S.O.; Walter, P.
Induced nucleotide specificity in a GTPase
Proc. Natl. Acad. Sci. USA
100
4480-4485
2003
Escherichia coli
Shan, S.O.; Walter, P.
Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor
Biochemistry
44
6214-6222
2005
Escherichia coli
Schuenemann, D.
Structure and function of the chloroplast signal recognition particle
Curr. Genet.
44
295-304
2004
Arabidopsis thaliana, Escherichia coli
Shan, S.O.; Walter, P.
Co-translational protein targeting by the signal recognition particle
FEBS Lett.
579
921-926
2005
Thermus aquaticus
Crowley, P.J.; Svensater, G.; Snoep, J.L.; Bleiweis, A.S.; Brady, L.J.
An ffh mutant of Streptococcus mutans is viable and able to physiologically adapt to low pH in continuous culture
FEMS Microbiol. Lett.
234
315-324
2004
Streptococcus mutans
Yurist, S.; Dahan, I.; Eichler, J.
SRP19 is a dispensable component of the signal recognition particle in Archaea
J. Bacteriol.
189
276-279
2007
Haloferax volcanii
Sivaraja, V.; Kumar, T.K.; Leena, P.S.; Chang, A.N.; Vidya, C.; Goforth, R.L.; Rajalingam, D.; Arvind, K.; Ye, J.L.; Chou, J.; Henry, R.; Yu, C.
Three-dimensional solution structures of the chromodomains of cpSRP43
J. Biol. Chem.
280
41465-41471
2005
Arabidopsis thaliana
Schlenker, O.; Hendricks, A.; Sinning, I.; Wild, K.
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains
J. Biol. Chem.
281
8898-8906
2006
Homo sapiens, Mus musculus
Dani, H.M.; Singh, J.; Singh, S.
Advances in the structure and functions of signal recognition particle in protein targeting
J. Biol. Regul. Homeost. Agents
17
303-307
2004
Saccharomyces cerevisiae, Escherichia coli, Pyrococcus furiosus
Lustig, Y.; Goldshmidt, H.; Uliel, S.; Michaeli, S.
The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi
J. Cell Sci.
118
4551-4562
2005
Trypanosoma brucei
Gariani, T.; Samuelsson, T.; Sauer-Eriksson, A.E.
Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY
J. Struct. Biol.
153
85-96
2006
Mycoplasma mycoides
Wild Klemen, W.K.; Halic Mari, H.M.; Sinning Irmgar, S.I.; Beckmann Rolan, B.R.
SRP meets the ribosome
Nat. Struct. Mol. Biol.
11
1049-1053
2004
Escherichia coli, Saccharolobus solfataricus, Thermus aquaticus
Spanggord, R.J.; Siu, F.; Ke, A.; Doudna, J.A.
RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle
Nat. Struct. Mol. Biol.
12
1116-1122
2005
Escherichia coli
Rosenblad, M.A.; Samuelsson, T.
Identification of chloroplast signal recognition particle RNA genes
Plant Cell Physiol.
45
1633-1639
2004
Arabidopsis thaliana, Chlamydomonas sp., Chlorella vulgaris, Cyanidioschyzon merolae, Cyanidium caldarium, Mesostigma viride, Trieres chinensis, Pisum sativum, Thalassiosira pseudonana, Epifagus virginiana, Porphyra purpurea, Guillardia theta, Nephroselmis olivacea
Fulton, L.A.; Cordum, H.S.; Wang, C.; Elliott, G.; Edwards, J.; Mardis, E.R.; Engstrand, L.G.; Gordon, J.I.
The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression
Proc. Natl. Acad. Sci. USA
103
9999-10004
2006
Helicobacter pylori (Q1CSB4), Helicobacter pylori (Q1CTA7), Helicobacter pylori (Q1CU93), Helicobacter pylori HPAG1 (Q1CSB4), Helicobacter pylori HPAG1 (Q1CTA7), Helicobacter pylori HPAG1 (Q1CU93)
Hainzl, T.; Huang, S.; Sauer-Eriksson, A.E.
Structural insights into SRP RNA: an induced fit mechanism for SRP assembly
RNA
11
1043-1050
2005
Methanocaldococcus jannaschii
Dong, H.J.; Tao, S.M.; Li, Y.Q.; Chan, S.H.; Shen, X.L.; Wang, C.X.; Guan, W.J.
Analysis of the GTPase activity and active sites of the NG domains of FtsY and Ffh from Streptomyces coelicolor
Acta Biochim. Biophys. Sin. (Shanghai)
38
467-476
2006
Streptomyces coelicolor
Ramirez, U.D.; Freymann, D.M.
Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh
Acta Crystallogr. Sect. D
D62
1520-1534
2006
Thermus aquaticus
Bange, G.; Wild, K.; Sinning, I.
Protein translocation: checkpoint role for SRP GTPase activation
Curr. Biol.
17
R980-R982
2007
Escherichia coli, Thermus aquaticus
Gras, S.; Chaumont, V.; Fernandez, B.; Carpentier, P.; Charrier-Savournin, F.; Schmitt, S.; Pineau, C.; Flament, D.; Hecker, A.; Forterre, P.; Armengaud, J.; Housset, D.
Structural insights into a new homodimeric self-activated GTPase family
EMBO Rep.
8
569-575
2007
Pyrococcus abyssi
Stengel, K.F.; Holdermann, I.; Wild, K.; Sinning, I.
The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site
FEBS Lett.
581
5671-5676
2007
Arabidopsis thaliana
Angelini, S.; Boy, D.; Schiltz, E.; Koch, H.G.
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
J. Cell Biol.
174
715-724
2006
Escherichia coli
Shan, S.O.; Chandrasekar, S.; Walter, P.
Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
J. Cell Biol.
178
611-620
2007
Escherichia coli
Chandrasekar, S.; Chartron, J.; Jaru-Ampornpan, P.; Shan, S.O.
Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction
J. Mol. Biol.
375
425-436
2008
Arabidopsis thaliana, Escherichia coli
Gawronski-Salerno, J.; Freymann, D.M.
Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY
J. Struct. Biol.
158
122-128
2007
Thermus aquaticus
Salvetti, S.; Ghelardi, E.; Celandroni, F.; Ceragioli, M.; Giannessi, F.; Senesi, S.
FlhF, a signal recognition particle-like GTPase, is involved in the regulation of flagellar arrangement, motility behaviour and protein secretion in Bacillus cereus
Microbiology
153
2541-2552
2007
Bacillus cereus
Gawronski-Salerno, J.; Coon, J.S.; Focia, P.J.; Freymann, D.M.
X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases
Proteins
66
984-995
2007
Thermus aquaticus
Siu, F.Y.; Spanggord, R.J.; Doudna, J.A.
SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting
RNA
13
240-250
2007
Escherichia coli
Brooks, M.A.; Ravelli, R.B.; McCarthy, A.A.; Strub, K.; Cusack, S.
Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle
Acta Crystallogr. Sect. D
65
421-433
2009
Schizosaccharomyces pombe, Schizosaccharomyces pombe (Q9P372)
Abe, K.; Hattori, T.; Isobe, T.; Kitagawa, K.; Oda, T.; Uchida, C.; Kitagawa, M.
Pirh2 interacts with and ubiquitylates signal recognition particle receptor beta subunit
Biomed. Res.
29
53-60
2008
Homo sapiens
Ananthamurthy, K.; Kathir, K.M.; Kumar, T.K.; Kight, A.; Goforth, R.L.; Henry, R.
1H, 13C and 15N resonance assignments of the C-terminal domain of the 43 kDa subunit of the chloroplast signal recognition particle
Biomol. NMR Assign.
2
37-39
2008
Arabidopsis thaliana
Rosch, J.W.; Vega, L.A.; Beyer, J.M.; Lin, A.; Caparon, M.G.
The signal recognition particle pathway is required for virulence in Streptococcus pyogenes
Infect. Immun.
76
2612-2619
2008
Streptococcus pyogenes, Streptococcus pyogenes HSC5
Marty, N.J.; Rajalingam, D.; Kight, A.D.; Lewis, N.E.; Fologea, D.; Kumar, T.K.; Henry, R.L.; Goforth, R.L.
The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity
J. Biol. Chem.
284
14891-14903
2009
Pisum sativum
Kathir, K.M.; Rajalingam, D.; Sivaraja, V.; Kight, A.; Goforth, R.L.; Yu, C.; Henry, R.; Kumar, T.K.
Assembly of chloroplast signal recognition particle involves structural rearrangement in cpSRP43
J. Mol. Biol.
381
49-60
2008
Arabidopsis thaliana
Dalley, J.A.; Selkirk, A.; Pool, M.R.
Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation
Mol. Biol. Cell
19
2876-2884
2008
Saccharomyces cerevisiae
Maier, K.S.; Hubich, S.; Liebhart, H.; Krauss, S.; Kuhn, A.; Facey, S.J.
An amphiphilic region in the cytoplasmic domain of KdpD is recognized by the signal recognition particle and targeted to the Escherichia coli membrane
Mol. Microbiol.
68
1471-1484
2008
Escherichia coli, Escherichia coli MC1061
Egea, P.F.; Napetschnig, J.; Walter, P.; Stroud, R.M.
Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus
PLoS ONE
3
e3528
2008
Pyrococcus furiosus (Q8U070), Pyrococcus furiosus
Egea, P.F.; Tsuruta, H.; de Leon, G.P.; Napetschnig, J.; Walter, P.; Stroud, R.M.
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane
PLoS ONE
3
e3619
2008
Pyrococcus furiosus (Q8U051), Pyrococcus furiosus
van Nues, R.W.; Leung, E.; McDonald, J.C.; Dantuluru, I.; Brown, J.D.
Roles for Srp72p in assembly, nuclear export and function of the signal recognition particle
RNA Biol.
5
73-83
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae JDY819
Buskiewicz, I.A.; Joeckel, J.; Rodnina, M.V.; Wintermeyer, W.
Conformation of the signal recognition particle in ribosomal targeting complexes
RNA
15
44-54
2009
Escherichia coli, Escherichia coli MRE 600
Stengel, K.F.; Holdermann, I.; Cain, P.; Robinson, C.; Wild, K.; Sinning, I.
Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43
Science
321
253-256
2008
Arabidopsis thaliana (O22265)
Nguyen, T.X.; Chandrasekar, S.; Neher, S.; Walter, P.; Shan, S.O.
Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle
Biochemistry
50
7208-7217
2011
Arabidopsis thaliana
Ataide, S.; Schmitz, N.; Shen, K.; Ke, A.; Shan, S.; Doudna, J.; Ban, N.
The crystal structure of the signal recognition particle in complex with its receptor
Science
331
881-886
2011
Escherichia coli
Shen, K.; Wang, Y.; Hwang Fu, Y.H.; Zhang, Q.; Feigon, J.; Shan, S.O.
Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end
J. Biol. Chem.
288
36385-36397
2013
Escherichia coli
Henderson, R.C.; Gao, F.; Jayanthi, S.; Kight, A.; Sharma, P.; Goforth, R.L.; Heyes, C.D.; Henry, R.L.; Suresh Kumar, T.K.
Domain organization in the 54-kDa subunit of the chloroplast signal recognition particle
Biophys. J.
111
1151-1162
2016
Arabidopsis thaliana (P37107)
Chandrasekar, S.; Sweredoski, M.J.; Sohn, C.H.; Hess, S.; Shan, S.O.
Co-evolution of two GTPases enables efficient protein targeting in an RNA-less chloroplast signal recognition particle pathway
J. Biol. Chem.
292
386-396
2017
Arabidopsis thaliana (P37107)
Wild, K.; Bange, G.; Motiejunas, D.; Kribelbauer, J.; Hendricks, A.; Segnitz, B.; Wade, R.C.; Sinning, I.
Structural basis for conserved regulation and adaptation of the signal recognition particle targeting complex
J. Mol. Biol.
428
2880-2897
2016
Canis lupus familiaris (P61010 AND P06625)
Faoro, C.; Ataide, S.
Structural insights into the G-loop dynamics of E. coli FtsY NG domain
J. Struct. Biol.
208
107387
2019
Escherichia coli (P0AGD7 AND P10121), Escherichia coli
Jadhav, B.; McKenna, M.; Johnson, N.; High, S.; Sinning, I.; Pool, M.R.
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation
Nat. Commun.
6
10133
2015
Thermochaetoides thermophila (G0SD15), Homo sapiens (P08240 AND Q9Y5M8), Mus musculus (Q9DBG7 AND P47758), Thermochaetoides thermophila IMI 039719 (G0SD15), Thermochaetoides thermophila DSM 1495 (G0SD15), Thermochaetoides thermophila CBS 144.50 (G0SD15)
Wild, K.; Juaire, K.D.; Soni, K.; Shanmuganathan, V.; Hendricks, A.; Segnitz, B.; Beckmann, R.; Sinning, I.
Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions
Nucleic Acids Res.
47
3184-3196
2019
Homo sapiens (P08240 AND Q9Y5M8), Homo sapiens
Jadhav, B.; Wild, K.; Pool, M.R.; Sinning, I.
Structure and switch cycle of SRbeta as ancestral eukaryotic GTPase associated with secretory membranes
Structure
23
1838-1847
2015
Thermochaetoides thermophila (G0SD15), Thermochaetoides thermophila IMI 039719 (G0SD15), Thermochaetoides thermophila DSM 1495 (G0SD15), Thermochaetoides thermophila CBS 144.50 (G0SD15)
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