The signal recognition particle receptor of
            <i>Escherichia coli</i>
            (FtsY) has a nucleotide exchange factor built into the GTPase domain

Moser, C.; Mol, Olaf; Goody, Roger S.; Sinning, Irmgard

doi:10.1073/pnas.94.21.11339

Cited by 79 publications

(62 citation statements)

References 34 publications

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“…The mechanism of guanine nucleotide exchange on GTPases by their cognate GEFs varies greatly, but mainly involves either fully obstructing the nucleotide-binding site or partial hamper of the Mg 2ϩ -or ␥/␤-phosphate binding sites (15). Most GEFs constitute extrinsic biomolecules, however, some GTPases have built-in intrinsic exchange factors as described for the N terminus of the bacterial signal recognition particle FtsY (32). Structurally, the GEFs for small GTPases such as Ran, Ras, Rho, and Rab vary greatly even among specific subfamilies.…”

Section: Discussionmentioning

confidence: 99%

Defective Guanine Nucleotide Exchange in the Elongation Factor-like 1 (EFL1) GTPase by Mutations in the Shwachman-Diamond Syndrome Protein

García-Márquez

Gijsbers

Mora³

et al. 2015

Journal of Biological Chemistry

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Background: EFL1 and the protein mutated in the Shwachman-Diamond syndrome (SBDS) participate in the maturation of the 60S ribosomal subunit. Results: SBDS increases the dissociation constant of EFL1 for GDP 60-fold. SBDS S143L disease mutation disrupts the interaction with EFL1. Conclusion: SBDS favors GDP dissociation from EFL1 and disease mutations abolishe this function. Significance: SBDS disease mutations prevent the nucleotide exchange regulation on EFL1.

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Section: Discussionmentioning

confidence: 99%

Defective Guanine Nucleotide Exchange in the Elongation Factor-like 1 (EFL1) GTPase by Mutations in the Shwachman-Diamond Syndrome Protein

García-Márquez

Gijsbers

Mora³

et al. 2015

Journal of Biological Chemistry

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“…The bacterial homologues of the SRP54 protein and SRP RNA, Ffh and 4.5S RNA ("R"), comprise a minimal bacterial SRP that can target ribosome•nascent chain complexes to the plasma membrane via interaction with FtsY, the bacterial homologue of the SRP receptor. Thus, the Ffh•R complex and FtsY provide a simplified, biochemically accessible system that allows an in-depth mechanistic investigation of the core features of the targeting process (e.g., 7,[10][11][12][13].…”

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confidence: 99%

Role of SRP RNA in the GTPase Cycles of Ffh and FtsY

et al. 2001

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The bacterial homologues of the signal recognition particle (SRP) and its receptor, 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 the mutual stimulation of GTP hydrolysis by both proteins. Previous work showed that 4.5S RNA enhances the GTPase activity in the presence of both Ffh and FtsY, but it was not clear how this was accomplished. In this work, kinetic and thermodynamic analyses of the GTPase reactions of Ffh and FtsY have provided insights into the role of 4.5S RNA in the GTPase cycles of Ffh and FtsY. We found that 4.5S RNA accelerates the association between Ffh and FtsY 400-fold in their GTP-bound form, analogous to its 200-fold catalytic effect on Ffh•FtsY association previously observed with the GppNHp-bound form [Peluso, P., et al. (2000) Science 288, [1640][1641][1642][1643]. Further, Ffh-FtsY association is rate-limiting for the observed GTPase reaction with subsaturating Ffh and FtsY, thereby accounting for the apparent stimulatory effect of 4.5S RNA on the GTPase activity observed previously. An additional step, GTP hydrolysis from the Ffh•FtsY complex, is also moderately facilitated by 4.5S RNA. These results suggest that 4.5S RNA modulates the conformation of the Ffh•FtsY complex and may, in turn, regulate its GTPase activity during the SRP functional cycle.

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“…Most importantly, SRPtype GTPases bind nucleotides much weaker than signaling GTPases and release nucleotides quickly (Moser et al, 1997;Jagath et al, 1998Jagath et al, , 2000Peluso et al, 2001). Therefore, they do not use nucleotide exchange factors to facilitate the conversion from the GDP-to the GTP-bound form.…”

Section: Introductionmentioning

confidence: 99%

Efficient Interaction between Two GTPases Allows the Chloroplast SRP Pathway to Bypass the Requirement for an SRP RNA

Jaru-Ampornpan

Chandrasekar

Shan

2007

MBoC

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Cotranslational protein targeting to membranes is regulated by two GTPases in the signal recognition particle (SRP) and the SRP receptor; association between the two GTPases is slow and is accelerated 400-fold by the SRP RNA. Intriguingly, the otherwise universally conserved SRP RNA is missing in a novel chloroplast SRP pathway. We found that even in the absence of an SRP RNA, the chloroplast SRP and receptor GTPases can interact efficiently with one another; the kinetics of interaction between the chloroplast GTPases is 400-fold faster than their bacterial homologues, and matches the rate at which the bacterial SRP and receptor interact with the help of SRP RNA. Biochemical analyses further suggest that the chloroplast SRP receptor is pre-organized in a conformation that allows optimal interaction with its binding partner, so that conformational changes during complex formation are minimized. Our results highlight intriguing differences between the classical and chloroplast SRP and SRP receptor GTPases, and help explain how the chloroplast SRP pathway can mediate efficient targeting of proteins to the thylakoid membrane in the absence of the SRP RNA, which plays an indispensable role in all the other SRP pathways.

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The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain

Cited by 79 publications

References 34 publications

Defective Guanine Nucleotide Exchange in the Elongation Factor-like 1 (EFL1) GTPase by Mutations in the Shwachman-Diamond Syndrome Protein

Defective Guanine Nucleotide Exchange in the Elongation Factor-like 1 (EFL1) GTPase by Mutations in the Shwachman-Diamond Syndrome Protein

Role of SRP RNA in the GTPase Cycles of Ffh and FtsY

Efficient Interaction between Two GTPases Allows the Chloroplast SRP Pathway to Bypass the Requirement for an SRP RNA

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