The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP - PubMed (original) (raw)
The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP
R Kusters et al. FEBS Lett. 1995.
Free article
Abstract
In this study, we have established that FtsY, the E. coli homolog of the mammalian signal recognition particle (SRP) receptor, is a GTP-binding protein which displays intrinsic GTPase activity. GTP was found to influence the protease sensitivity of FtsY indicative of a conformational change. FtsY mutated in the 4th GTP-binding consensus element displayed reduced GTP-binding and -hydrolysis which correlated with a reduced ability to interact with SRP. Overexpression of the mutant proteins had a stronger inhibitory effect on protein translocation than overexpression of wild-type FtsY. These observations suggest that in E. coli GTP is important for proper functioning of FtsY in protein-targeting.
Similar articles
- Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor.
Miller JD, Bernstein HD, Walter P. Miller JD, et al. Nature. 1994 Feb 17;367(6464):657-9. doi: 10.1038/367657a0. Nature. 1994. PMID: 8107852 - A GTP-binding protein of Mycoplasma hominis: a small sized homolog to the signal recognition particle receptor FtsY.
Ladefoged SA, Christiansen G. Ladefoged SA, et al. Gene. 1997 Nov 12;201(1-2):37-44. doi: 10.1016/s0378-1119(97)00425-3. Gene. 1997. PMID: 9409769 - Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP.
Jagath JR, Rodnina MV, Wintermeyer W. Jagath JR, et al. J Mol Biol. 2000 Jan 28;295(4):745-53. doi: 10.1006/jmbi.1999.3427. J Mol Biol. 2000. PMID: 10656787 - 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 - From the elephant to E. coli: SRP-dependent protein targeting.
Wolin SL. Wolin SL. Cell. 1994 Jun 17;77(6):787-90. doi: 10.1016/0092-8674(94)90124-4. Cell. 1994. PMID: 8004667 Review. No abstract available.
Cited by
- In vitro membrane protein synthesis inside Sec translocon-reconstituted cell-sized liposomes.
Ohta N, Kato Y, Watanabe H, Mori H, Matsuura T. Ohta N, et al. Sci Rep. 2016 Nov 3;6:36466. doi: 10.1038/srep36466. Sci Rep. 2016. PMID: 27808179 Free PMC article. - Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.
Kuhn P, Draycheva A, Vogt A, Petriman NA, Sturm L, Drepper F, Warscheid B, Wintermeyer W, Koch HG. Kuhn P, et al. J Cell Biol. 2015 Oct 12;211(1):91-104. doi: 10.1083/jcb.201502103. J Cell Biol. 2015. PMID: 26459600 Free PMC article. - Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites.
Angelini S, Boy D, Schiltz E, Koch HG. Angelini S, et al. J Cell Biol. 2006 Aug 28;174(5):715-24. doi: 10.1083/jcb.200606093. Epub 2006 Aug 21. J Cell Biol. 2006. PMID: 16923832 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. - Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.
Buskiewicz I, Deuerling E, Gu SQ, Jöckel J, Rodnina MV, Bukau B, Wintermeyer W. Buskiewicz I, et al. Proc Natl Acad Sci U S A. 2004 May 25;101(21):7902-6. doi: 10.1073/pnas.0402231101. Epub 2004 May 17. Proc Natl Acad Sci U S A. 2004. PMID: 15148364 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases