Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor - PubMed (original) (raw)
Comparative Study
. 1994 Feb 17;367(6464):657-9.
doi: 10.1038/367657a0.
Affiliations
- PMID: 8107852
- DOI: 10.1038/367657a0
Comparative Study
Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
J D Miller et al. Nature. 1994.
Abstract
The mechanism of protein translocation across the endoplasmic reticulum membrane of eukaryotic cells and the plasma membrane of prokaryotic cells are thought to be evolutionarily related. Protein targeting to the eukaryotic translocation apparatus is mediated by the signal recognition particle (SRP), a cytosolic ribonucleoprotein, and the SRP receptor, an endoplasmic reticulum membrane protein. During targeting, the 54K SRP subunit (M(r) 54,000; SRP54), a GTP-binding protein, binds to signal sequences and then interacts with the alpha-subunit of the SRP receptor (SR alpha), another GTP-binding protein. Two proteins from Escherichia coli, Ffh and FTsY, structurally resemble SRP54 and SR alpha. Like SRP54, Ffh is a subunit of a cytosolic ribonucleoprotein that also contains the E. coli 4.5S RNA. Although there is genetic and biochemical evidence that the E. coli Ffh/4.5S ribonucleoprotein has an SRP-like function, there is no evidence for an SR alpha-like role for FtsY. Here we show that the Ffh/4.5S ribonucleoprotein binds tightly to FtsY in a GTP-dependent manner. This interaction results in the stimulation of GTP hydrolysis which can be inhibited by synthetic signal peptides. These properties mimic those of mammalian SRP and its receptor, suggesting that the E. coli Ffh/4.5S ribonucleoprotein and FtsY have functions in protein targeting that are similar to those of their mammalian counterparts.
Comment in
- Protein transport. On the beaten pathway.
Dobberstein B. Dobberstein B. Nature. 1994 Feb 17;367(6464):599-600. doi: 10.1038/367599a0. Nature. 1994. PMID: 8107844 No abstract available.
Similar articles
- GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation.
Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. Miller JD, et al. Nature. 1993 Nov 25;366(6453):351-4. doi: 10.1038/366351a0. Nature. 1993. PMID: 8247130 - Evidence for a novel GTPase priming step in the SRP protein targeting pathway.
Lu Y, Qi HY, Hyndman JB, Ulbrandt ND, Teplyakov A, Tomasevic N, Bernstein HD. Lu Y, et al. EMBO J. 2001 Dec 3;20(23):6724-34. doi: 10.1093/emboj/20.23.6724. EMBO J. 2001. PMID: 11726508 Free PMC article. - Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY.
Buskiewicz I, Kubarenko A, Peske F, Rodnina MV, Wintermeyer W. Buskiewicz I, et al. RNA. 2005 Jun;11(6):947-57. doi: 10.1261/rna.7242305. RNA. 2005. PMID: 15923378 Free PMC article. - Targeting proteins to membranes: structure of the signal recognition particle.
Egea PF, Stroud RM, Walter P. Egea PF, et al. Curr Opin Struct Biol. 2005 Apr;15(2):213-20. doi: 10.1016/j.sbi.2005.03.007. Curr Opin Struct Biol. 2005. PMID: 15837181 Review. - A structural step into the SRP cycle.
Wild K, Rosendal KR, Sinning I. Wild K, et al. Mol Microbiol. 2004 Jul;53(2):357-63. doi: 10.1111/j.1365-2958.2004.04139.x. Mol Microbiol. 2004. PMID: 15228518 Review.
Cited by
- Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase.
Kleinbeck F, Kuhn A. Kleinbeck F, et al. Viruses. 2021 Jul 20;13(7):1414. doi: 10.3390/v13071414. Viruses. 2021. PMID: 34372619 Free PMC article. - Noncanonical Functions and Cellular Dynamics of the Mammalian Signal Recognition Particle Components.
Faoro C, Ataide SF. Faoro C, et al. Front Mol Biosci. 2021 May 25;8:679584. doi: 10.3389/fmolb.2021.679584. eCollection 2021. Front Mol Biosci. 2021. PMID: 34113652 Free PMC article. Review. - Translational Control of Secretory Proteins in Health and Disease.
Karamyshev AL, Tikhonova EB, Karamysheva ZN. Karamyshev AL, et al. Int J Mol Sci. 2020 Apr 6;21(7):2538. doi: 10.3390/ijms21072538. Int J Mol Sci. 2020. PMID: 32268488 Free PMC article. Review. - Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio.
Kondo S, Imura Y, Mizuno A, Homma M, Kojima S. Kondo S, et al. Sci Rep. 2018 Aug 14;8(1):12115. doi: 10.1038/s41598-018-30531-5. Sci Rep. 2018. PMID: 30108243 Free PMC article. - Archaeal cell surface biogenesis.
Pohlschroder M, Pfeiffer F, Schulze S, Abdul Halim MF. Pohlschroder M, et al. FEMS Microbiol Rev. 2018 Sep 1;42(5):694-717. doi: 10.1093/femsre/fuy027. FEMS Microbiol Rev. 2018. PMID: 29912330 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials