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GDP + H2O
GMP + phosphate
GTP + H2O
GDP + phosphate
guanylyl-5'-imidodiphosphate + H2O
?
-
-
-
?
additional information
?
-
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
P61010; P06625
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
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 to the plasma membrane
-
-
?
GTP + H2O
GDP + phosphate
-
Ffh has a high specificity for GTP over noncognate nucleotides, domain structure
-
-
?
GTP + H2O
GDP + phosphate
-
GTPase reaction cycle
-
-
?
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
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
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
P08240; Q9Y5M8
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
Q9DBG7; P47758
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
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
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
Thermochaetoides thermophila
-
-
-
?
GTP + H2O
GDP + phosphate
Thermochaetoides thermophila CBS 144.50
-
-
-
?
GTP + H2O
GDP + phosphate
Thermochaetoides thermophila DSM 1495
-
-
-
?
GTP + H2O
GDP + phosphate
Thermochaetoides thermophila IMI 039719
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
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
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
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
?
-
-
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
?
-
-
not: GMPPCP
-
-
?
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
-
-
?
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Abortion, Spontaneous
Maternal serum levels of interferon-gamma and interleukin-2 soluble receptor-alpha predict the outcome of early IVF pregnancies.
Adenomatous Polyposis Coli
Identification and characterization of the familial adenomatous polyposis coli gene.
Adenoviridae Infections
Monomeric scAlu and nascent dimeric Alu RNAs induced by adenovirus are assembled into SRP9/14-containing RNPs in HeLa cells.
Colitis
Interleukin 7 transgenic mice develop chronic colitis with decreased interleukin 7 protein accumulation in the colonic mucosa.
Colitis
Naked gene therapy of hepatocyte growth factor for dextran sulfate sodium-induced colitis in mice.
Colorectal Neoplasms
The presence of interleukin-2 receptor alpha in the serum of colorectal cancer patients is unlikely to result only from T cell up-regulation.
Congenital Bone Marrow Failure Syndromes
Mutations in signal recognition particle SRP54 cause syndromic neutropenia with Shwachman-Diamond-like features.
Connective Tissue Diseases
Clinical and histopathological features of myopathies in Japanese patients with anti-SRP autoantibodies.
Connective Tissue Diseases
Clinical Features and Treatment Outcomes of Necrotizing Autoimmune Myopathy.
Connective Tissue Diseases
Treatment and outcomes in necrotising autoimmune myopathy: An Australian perspective.
Cryptogenic Organizing Pneumonia
Signal recognition particle (SRP) positive myositis in a patient with cryptogenic organizing pneumonia (COP).
Dehydration
Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584.
Dermatomyositis
The 72-kDa component of signal recognition particle is cleaved during apoptosis.
DiGeorge Syndrome
Severe Congenital Neutropenia associated with SRP54 mutation in 22q11.2 Deletion Syndrome: Hematopoietic Stem Cell Transplantation Results in Correction of Neutropenia with Adequate Immune Reconstitution.
Gingival Overgrowth
Signal recognition particle receptor (SRPR) is downregulated in a rat model of cyclosporin A-induced gingival overgrowth.
Hepatitis C
Automated RNA tertiary structure prediction from secondary structure and low-resolution restraints.
Hypercholesterolemia
Inhibition of protein translocation across the endoplasmic reticulum membrane by sterols.
Infections
Cellular microRNA miR-10a-5p inhibits replication of porcine reproductive and respiratory syndrome virus by targeting the host factor signal recognition particle 14.
Infections
Mechanism of down-regulation of RNA polymerase III-transcribed non-coding RNA genes in macrophages by Leishmania.
Infections
SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses.
Infections
What is in the Myopathy Literature?
Kidney Failure, Chronic
Serum concentration of IL-2, IL-6, TNF-alpha and their soluble receptors in children on maintenance hemodialysis.
Latent Infection
The RNA-Binding Proteins SRP14 and HMGB3 Control HIV-1 Tat mRNA Processing and Translation During HIV-1 Latency.
Leukemia
Green fluorescent protein as a selectable marker of retrovirally transduced hematopoietic progenitors.
Leukemia, Myeloid, Acute
Identification and validation of signal recognition particle 14 as a prognostic biomarker predicting overall survival in patients with acute myeloid leukemia.
Lupus Erythematosus, Systemic
Autoantibodies in the diagnosis of systemic rheumatic diseases.
Lupus Erythematosus, Systemic
The 72-kDa component of signal recognition particle is cleaved during apoptosis.
Lupus Nephritis
Immune-mediated necrotizing myopathy, associated with antibodies to signal recognition particle, together with lupus nephritis: case presentation and management.
Lymphopenia
Immune checkpoint inhibitor-associated myopathy: a clinicoseropathologically distinct myopathy.
Muscular Diseases
A pediatric patient with myopathy associated with antibodies to a signal recognition particle.
Muscular Diseases
Anti-signal recognition particle antibody in patients without inflammatory myopathy: a survey of 6180 patients with connective tissue diseases.
Muscular Diseases
Anti-signal recognition particle myopathy in the first decade of life.
Muscular Diseases
Clinical features and prognosis in anti-SRP and anti-HMGCR necrotising myopathy.
Muscular Diseases
Complement-mediated muscle cell lysis: A possible mechanism of myonecrosis in anti-SRP associated necrotizing myopathy (ASANM).
Muscular Diseases
Effective induction therapy for anti-SRP associated myositis in childhood: A small case series and review of the literature.
Muscular Diseases
Immune checkpoint inhibitor-associated myopathy: a clinicoseropathologically distinct myopathy.
Muscular Diseases
Immune-mediated necrotising myopathy associated with antibodies to the signal recognition particle treated with a combination of rituximab and cyclophosphamide.
Muscular Diseases
Immune-mediated necrotizing myopathy associated with antibodies to the signal recognition particle: A rare cause of hyperCKaemia.
Muscular Diseases
Immune-mediated necrotizing myopathy, associated with antibodies to signal recognition particle, together with lupus nephritis: case presentation and management.
Muscular Diseases
Longitudinal course of disease in a large cohort of myositis patients with autoantibodies recognizing the signal recognition particle.
Muscular Diseases
Magnetic resonance imaging changes of thigh muscles in myopathy with antibodies to signal recognition particle.
Muscular Diseases
Marked efficacy of a therapeutic strategy associating prednisone and plasma exchange followed by rituximab in two patients with refractory myopathy associated with antibodies to the signal recognition particle (SRP).
Muscular Diseases
Myopathy Associated With Antibodies to Signal Recognition Particle: Disease Progression and Neurological Outcome.
Muscular Diseases
Myopathy with antibodies to the signal recognition particle: clinical and pathological features.
Muscular Diseases
Myositis autoantibodies.
Muscular Diseases
Necrotizing myopathies: beyond statins.
Muscular Diseases
Necrotizing myopathy: clinicoserologic associations.
Muscular Diseases
Rituximab in the treatment of immune-mediated necrotizing myopathy: a review of case reports and case series.
Muscular Diseases
Treatment experience of Taiwanese patients with anti-3-hydroxy-3-methylglutaryl-coenzyme A reductase myopathy.
Muscular Diseases
What is in the Myopathy Literature?
Muscular Diseases
[A case of an anti-SRP myopathy with enlargement of the thymus].
Muscular Diseases
[A case of chronic myopathy associated with an antibody to signal recognition particle (SRP) following long-term asymptomatic hypercreatinekinasemia].
Muscular Diseases
[Acquired necrotizing myopathies.]
Muscular Diseases
[Diagnosis of Idiopathic Inflammatory Myopathy: A Muscle Pathology Perspective].
Muscular Diseases
[Histological and molecular alterations in inflammatory myopathies].
Myositis
Anti-signal recognition particle antibody in patients without inflammatory myopathy: a survey of 6180 patients with connective tissue diseases.
Myositis
Autoantibodies in polymyositis and dermatomyositis.
Myositis
Cutting Edge Issues in Polymyositis.
Myositis
Effective induction therapy for anti-SRP associated myositis in childhood: A small case series and review of the literature.
Myositis
Longitudinal course of disease in a large cohort of myositis patients with autoantibodies recognizing the signal recognition particle.
Myositis
Myopathy with antibodies to the signal recognition particle: clinical and pathological features.
Myositis
Myositis specific autoantibodies.
Myositis
Necrotizing myopathy: clinicoserologic associations.
Myositis
Signal recognition particle (SRP) positive myositis in a patient with cryptogenic organizing pneumonia (COP).
Myositis
Spectrum of immune-mediated necrotizing myopathies and their treatments.
Myositis
Treatment experience of Taiwanese patients with anti-3-hydroxy-3-methylglutaryl-coenzyme A reductase myopathy.
Myositis
What is in the Myopathy Literature?
Myositis
What's in the Literature?
Myositis
[Autoantibodies specifically detected in patients with polymyositis/dermatomyositis]
Myositis
[Diagnosis of Idiopathic Inflammatory Myopathy: A Muscle Pathology Perspective].
Myositis
[Diagnostic significance of scleroderma and myositis-associated autoantibodies]
Myositis
[Histological and molecular alterations in inflammatory myopathies].
Myositis, Inclusion Body
What is in the Myopathy Literature?
Neoplasms
Atorvastatin-induced necrotizing autoimmune myositis: An emerging dominant entity in patients with autoimmune myositis presenting with a pure polymyositis phenotype.
Neoplasms
Clinical Features and Treatment Outcomes of Necrotizing Autoimmune Myopathy.
Neoplasms
Genomic selection of reference genes for real-time PCR in human myocardium.
Neoplasms
Identification and validation of signal recognition particle 14 as a prognostic biomarker predicting overall survival in patients with acute myeloid leukemia.
Neoplasms
Identification of proteomic signatures of mantle cell lymphoma, small lymphocytic lymphoma, and marginal zone lymphoma biopsies by surface enhanced laser desorption/ionization-time of flight mass spectrometry.
Neoplasms
The moving parts of the nucleolus.
Neoplasms
The presence of interleukin-2 receptor alpha in the serum of colorectal cancer patients is unlikely to result only from T cell up-regulation.
Neoplasms
Treatment and outcomes in necrotising autoimmune myopathy: An Australian perspective.
Neoplasms
[Detection of gene expression alteration of myeloma cells treated with arsenic trioxide]
Neutropenia
A Filipino infant with severe neutropenia owing to SRP54 mutations was successfully treated with ethnically mismatched cord blood transplantation from a Japanese cord blood bank.
Neutropenia
Cellular Traffic Jam and Disease Due to Mutations in SRP54.
Neutropenia
Congenital neutropenia with variable clinical presentation in novel mutation of the SRP54 gene.
Neutropenia
Mutations in signal recognition particle SRP54 cause syndromic neutropenia with Shwachman-Diamond-like features.
Neutropenia
Mutations in the SRP54 gene cause severe congenital neutropenia as well as Shwachman-Diamond-like syndrome.
Neutropenia
Severe Congenital Neutropenia associated with SRP54 mutation in 22q11.2 Deletion Syndrome: Hematopoietic Stem Cell Transplantation Results in Correction of Neutropenia with Adequate Immune Reconstitution.
Neutropenia
SRP54 and a need for a new neutropenia nosology.
Neutropenia
SRP54 mutations induce congenital neutropenia via dominant-negative effects on XBP1 splicing.
Neutropenia
Structural and Functional Impact of SRP54 Mutations Causing Severe Congenital Neutropenia.
Neutropenia
Three patients with glucose-6 phosphatase catalytic subunit 3 deficiency.
Pneumonia
Signal recognition particle (SRP) positive myositis in a patient with cryptogenic organizing pneumonia (COP).
Polymyositis
Antibody to signal recognition particle in polymyositis.
Polymyositis
Autoantibody to signal recognition particle in African American girls with juvenile polymyositis.
Polymyositis
Coexistence of anti-Jo1 and anti-signal recognition particle antibodies in a polymyositis patient.
Polymyositis
[Diagnosis of Idiopathic Inflammatory Myopathy: A Muscle Pathology Perspective].
Porcine Reproductive and Respiratory Syndrome
Cellular microRNA miR-10a-5p inhibits replication of porcine reproductive and respiratory syndrome virus by targeting the host factor signal recognition particle 14.
Scleroderma, Systemic
Autoantibodies in the diagnosis of systemic rheumatic diseases.
Shwachman-Diamond Syndrome
SRP54 mutations induce congenital neutropenia via dominant-negative effects on XBP1 splicing.
Shwachman-Diamond Syndrome
Structural and Functional Impact of SRP54 Mutations Causing Severe Congenital Neutropenia.
Shwachman-Diamond Syndrome
Whole exome sequencing discloses heterozygous variants in the DNAJC21 and EFL1 genes but not in SRP54 in 6 out of 16 patients with Shwachman-Diamond Syndrome carrying biallelic SBDS mutations.
signal-recognition-particle gtpase deficiency
SRP54 mutations induce congenital neutropenia via dominant-negative effects on XBP1 splicing.
Spina Bifida Cystica
Proteomic analysis of amniotic fluid of pregnant rats with spina bifida aperta.
Tuberculosis
Characterization of FtsY, its interaction with Ffh, and proteomic identification of their potential substrates in Mycobacterium tuberculosis.
Tuberculosis
Essential biochemical, biophysical and computational inputs on efficient functioning of Mycobacterium tuberculosis H37Rv FtsY.
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evolution
co-evolution of two GTPases enables efficient protein targeting in an RNA-less chloroplast signal recognition particle pathway
evolution
P08240; Q9Y5M8
SR ribosome binding is evolutionarily conserved
evolution
Q9DBG7; P47758
SR ribosome binding is evolutionarily conserved
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
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D329A
-
diminished GTPase activity
T326N
-
diminished GTPase activity
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
L164Y
the mutant shows no interaction with synthetic L18 peptide
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
Y204A
the mutant shows no interaction with synthetic L18 peptide
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
K751/H119L
-
hydrolysis of XTP favored over GTP
K75I/H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a null mutant phenotype and no binding of SRalpha
A143W
-
mutant, GTPase activation defective
A144W
-
mutant, GTPase activation defective
A192D
-
reduced GTP hydrolysis, no effect on the interaction with FtsY
A334W
-
mutant, exhibits no significant GTP hydrolysis
A335W
-
mutant, GTPase activation defective
A336W
-
mutant, GTPase activation defective
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
E475K
-
mutant, complex formation defective
F240V
-
mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
G110S
-
reduced GTP hydrolysis, no effect on the interaction with 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
G455V
-
mutant, defective in SRP-FtsY complex formation
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
K399A
-
mutant, complex formation defective
L195P
-
reduced GTP hydrolysis, no effect on the interaction with FtsY
L199F
-
mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
N302A
-
mutant, GTPase activation defective
P142L
-
reduced GTP hydrolysis, no effect on the interaction with FtsY
Q109A
-
mutant, GTPase activation defective
R141A
-
mutant, GTPase activation defective
R194A
-
mutant, GTPase activation defective
R333A
-
mutant, GTPase activation defective
R386A
-
mutant, GTPase activation defective
T307A
-
mutant, complex formation and GTPase activation defective
A254L
-
no growth defect
-
D253N
-
no growth defect
-
G256A
-
no growth defect
-
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
-
R255N
-
no growth defect
-
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%
E157Q
-
reduced affinity for GTP
H91L
-
reduced GTPase activity
H91L/N154A/E157A
-
mutant
K51I
-
reduced nucleotide affinity
N154I
-
impaired nucleotide exchange
P46A/Q47A/N48A/DELTAS49
-
mutant
S220A
-
bypass requirement for GEF
S49A
-
reduced GTP hydrolysis
T52N
-
increased affinity for GEF, reduced affinity for GTP
T66A
-
prevents GTP-dependent interaction with GAP
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
Thr112Ala
-
deficient in GTP hydrolysis
Thr112Ala
-
deficient in GTP hydrolysis
-
D181N
-
hydrolysis of XTP favored over GTP
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
-
hydrolysis of XTP favored over GTP
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
-
hydrolysis of XTP favored over GTP
G118L/D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta) and weak binding of SRalpha
H119L
-
hydrolysis of XTP favored over GTP
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
-
hydrolysis of XTP favored over GTP
K75I
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and no binding of SRalpha
N178K
-
hydrolysis of XTP favored over GTP
N178K
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and weak binding of SRalpha
G455W
-
mutant, complex formation defective
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
-
SRbetaD4, hydrolysis of XTP favored over GTP
additional information
-
SRbetaD5, 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
-
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Escherichia coli
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Escherichia coli, Escherichia coli WAM121
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2001
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2003
Saccharolobus solfataricus
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2003
Escherichia coli
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An ffh mutant of Streptococcus mutans is viable and able to physiologically adapt to low pH in continuous culture
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Streptococcus mutans
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Haloferax volcanii
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Saccharomyces cerevisiae, Escherichia coli, Pyrococcus furiosus
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Escherichia coli, Saccharolobus solfataricus, Thermus aquaticus
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Bacillus cereus
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2007
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2007
Escherichia coli
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Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle
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65
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2009
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2008
Homo sapiens
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37-39
2008
Arabidopsis thaliana
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2008
Streptococcus pyogenes, Streptococcus pyogenes HSC5
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Arabidopsis thaliana
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2008
Saccharomyces cerevisiae
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2008
Escherichia coli, Escherichia coli MC1061
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2008
Pyrococcus furiosus (Q8U070), Pyrococcus furiosus
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2008
Pyrococcus furiosus (Q8U051), Pyrococcus furiosus
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2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae JDY819
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Conformation of the signal recognition particle in ribosomal targeting complexes
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15
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2009
Escherichia coli, Escherichia coli MRE 600
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Escherichia coli (P0AGD7 AND P10121), Escherichia coli
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