2000
DOI: 10.1126/science.288.5471.1640
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Role of 4.5 S RNA in Assembly of the Bacterial Signal Recognition Particle with Its Receptor

Abstract: The mechanism by which a signal recognition particle (SRP) and its receptor mediate protein targeting to the endoplasmic reticulum or to the bacterial plasma membrane is evolutionarily conserved. In Escherichia coli, this reaction is mediated by the Ffh/4.5S RNA ribonucleoprotein complex (Ffh/4.5S RNP; the SRP) and the FtsY protein (the SRP receptor). We have quantified the effects of 4.5S RNA on Ffh-FtsY complex formation by monitoring changes in tryptophan fluorescence. Surprisingly, 4.5S RNA facilitates bot… Show more

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Cited by 137 publications
(175 citation statements)
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“…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.…”
supporting
confidence: 69%
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“…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.…”
supporting
confidence: 69%
“…The results herein describe differences in the presence and absence of 4.5S RNA. In vivo, however, 4.5S RNA would be bound to Ffh throughout the targeting cycle because of the tight Ffh-RNA association and because the affinity of Ffh for 4.5S RNA does not appear to be altered by additional components in the targeting pathway such as nucleotides, the SRP receptor, or the ribosome•nascent chain complex (12,35; results herein and Johnson, A. E., personal communication). Nevertheless, the function of this RNA could be regulated by additional components in the targeting pathway.…”
Section: Discussionmentioning
confidence: 78%
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“…The formation of the Ffh-FtsY complex strongly depends on the presence of 4+5S RNA (Kusters et al+, 1995;Powers & Walter, 1995;Jagath et al+, 2000), although the binary complex was reported to be formed, albeit slowly, in the absence of 4+5S RNA when an N-terminally truncated form of FtsY was used (Peluso et al+, 2000)+ In the mammalian system, the SRP54-7S RNA complex is required for membrane targeting of ribosome-nascent chain complexes (Hauser et al+, 1995)+ Mutations in the tetranucleotide loop and in the adjoining stem of Schizosaccharomyces pombe 7S RNA did not abolish function in vivo (Selinger et al+, 1993)+ Here we report that similar base exchanges in the tetraloop and the adjoining stem in E. coli 4+5S RNA, which do not affect the affinity for Ffh, strongly influence the binding of SRP to its receptor FtsY, indicating that the structure of SRP RNA modulates the interaction of SRP with its receptor+…”
Section: Introductionmentioning
confidence: 99%