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Literature summary for 3.6.5.4 extracted from

  • 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 (2015), Nat. Commun., 6, 10133 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21 (DE3) Mus musculus
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3) Homo sapiens
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3) Thermochaetoides thermophila

Protein Variants

Protein Variants Comment Organism
additional information 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 Homo sapiens
additional information 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 Mus musculus
additional information 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 Thermochaetoides thermophila

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane
-
Homo sapiens 5789
-
endoplasmic reticulum membrane
-
Mus musculus 5789
-
endoplasmic reticulum membrane
-
Thermochaetoides thermophila 5789
-
membrane 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 Homo sapiens 16020
-
membrane 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 Mus musculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens
Mg2+ required Mus musculus
Mg2+ required Thermochaetoides thermophila

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Homo sapiens
-
GDP + phosphate
-
?
GTP + H2O Mus musculus
-
GDP + phosphate
-
?
GTP + H2O Thermochaetoides thermophila
-
GDP + phosphate
-
?
GTP + H2O Thermochaetoides thermophila IMI 039719
-
GDP + phosphate
-
?
GTP + H2O Thermochaetoides thermophila DSM 1495
-
GDP + phosphate
-
?
GTP + H2O Thermochaetoides thermophila CBS 144.50
-
GDP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P08240 AND Q9Y5M8 subunits SRalpha and SRbeta
-
Mus musculus Q9DBG7 AND P47758 subunits SRalpha and SRbeta
-
Thermochaetoides thermophila G0SD15 signal recognition particle 54 kDa protein subunit with GTPase activity
-
Thermochaetoides thermophila CBS 144.50 G0SD15 signal recognition particle 54 kDa protein subunit with GTPase activity
-
Thermochaetoides thermophila DSM 1495 G0SD15 signal recognition particle 54 kDa protein subunit with GTPase activity
-
Thermochaetoides thermophila IMI 039719 G0SD15 signal recognition particle 54 kDa protein subunit with GTPase activity
-

Purification (Commentary)

Purification (Comment) Organism
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 Mus musculus
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Homo sapiens GDP + phosphate
-
?
GTP + H2O
-
Mus musculus GDP + phosphate
-
?
GTP + H2O
-
Thermochaetoides thermophila GDP + phosphate
-
?
GTP + H2O
-
Thermochaetoides thermophila IMI 039719 GDP + phosphate
-
?
GTP + H2O
-
Thermochaetoides thermophila DSM 1495 GDP + phosphate
-
?
GTP + H2O
-
Thermochaetoides thermophila CBS 144.50 GDP + phosphate
-
?
additional information both SRalpha and SRbeta are GTPases Homo sapiens ?
-
-
additional information both SRalpha and SRbeta are GTPases Mus musculus ?
-
-
additional information both SRalpha and SRbeta are GTPases Thermochaetoides thermophila ?
-
-
additional information both SRalpha and SRbeta are GTPases Thermochaetoides thermophila IMI 039719 ?
-
-
additional information both SRalpha and SRbeta are GTPases Thermochaetoides thermophila DSM 1495 ?
-
-
additional information both SRalpha and SRbeta are GTPases Thermochaetoides thermophila CBS 144.50 ?
-
-

Subunits

Subunits Comment Organism
heterodimer 1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE Homo sapiens
heterodimer 1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE Mus musculus
More 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 Homo sapiens
More 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 Mus musculus

Synonyms

Synonyms Comment Organism
CtSR
-
Thermochaetoides thermophila
GTPase
-
Homo sapiens
GTPase
-
Mus musculus
GTPase
-
Thermochaetoides thermophila
signal recognition particle receptor subunit alpha
-
Homo sapiens
signal recognition particle receptor subunit alpha
-
Mus musculus
signal recognition particle receptor subunit beta
-
Homo sapiens
signal recognition particle receptor subunit beta
-
Mus musculus
SRalpha
-
Homo sapiens
SRalpha
-
Mus musculus
SRPRA gene name, subunit SRalpha Homo sapiens
SRPRA gene name, subunit SRalpha Mus musculus
SRPRB gene name, subunit SRbeta Homo sapiens
SRPRB gene name, subunit SRbeta Mus musculus

General Information

General Information Comment Organism
evolution SR ribosome binding is evolutionarily conserved Homo sapiens
evolution SR ribosome binding is evolutionarily conserved Mus musculus
evolution 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 Thermochaetoides thermophila
malfunction 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 Homo sapiens
malfunction 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 Mus musculus
metabolism 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 Homo sapiens
metabolism 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 Mus musculus
additional information binding of SR to Sec61 positions SRalpha close to Sec61beta Homo sapiens
additional information binding of SR to Sec61 positions SRalpha close to Sec61beta Mus musculus
physiological function 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 Homo sapiens
physiological function 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 Mus musculus