Mammalian and Escherichia coli signal recognition particles - PubMed (original) (raw)
Review
Mammalian and Escherichia coli signal recognition particles
J Luirink et al. Mol Microbiol. 1994 Jan.
Free article
Abstract
Recent evidence from both biochemical and genetic studies indicates that protein targeting to the prokaryotic cytoplasmic membrane and the eukaryotic endoplasmic reticulum membrane may have more in common than previously thought. A ribonucleoprotein particle was identified in Escherichia coli that consists of at least one protein (P48 or Ffh) and one RNA molecule (4.5S RNA), both of which exhibit strong sequence similarity with constituents of the mammalian signal recognition particle (SRP). Like the mammalian SRP, the E. coli SRP binds specifically to the signal sequence of presecretory proteins. Depletion of either P48 or 4.5S RNA affects translation and results in the accumulation of precursors of several secreted proteins. This review discusses the recent studies and speculates on the position of the SRP in the complex network of protein interactions involved in translation and membrane targeting in E. coli.
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 - Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex.
Luirink J, High S, Wood H, Giner A, Tollervey D, Dobberstein B. Luirink J, et al. Nature. 1992 Oct 22;359(6397):741-3. doi: 10.1038/359741a0. Nature. 1992. PMID: 1279430 - Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor.
Powers T, Walter P. Powers T, et al. EMBO J. 1997 Aug 15;16(16):4880-6. doi: 10.1093/emboj/16.16.4880. EMBO J. 1997. PMID: 9305630 Free PMC article. - The E. coli SRP: preferences of a targeting factor.
De Gier JW, Valent QA, Von Heijne G, Luirink J. De Gier JW, et al. FEBS Lett. 1997 May 12;408(1):1-4. doi: 10.1016/s0014-5793(97)00402-x. FEBS Lett. 1997. PMID: 9180256 Review. - Structure, function and evolution of the signal recognition particle.
Nagai K, Oubridge C, Kuglstatter A, Menichelli E, Isel C, Jovine L. Nagai K, et al. EMBO J. 2003 Jul 15;22(14):3479-85. doi: 10.1093/emboj/cdg337. EMBO J. 2003. PMID: 12853463 Free PMC article. Review.
Cited by
- Increasing the Efficiency of the Accumulation of Recombinant Proteins in Plant Cells: The Role of Transport Signal Peptides.
Rozov SM, Deineko EV. Rozov SM, et al. Plants (Basel). 2022 Sep 28;11(19):2561. doi: 10.3390/plants11192561. Plants (Basel). 2022. PMID: 36235427 Free PMC article. Review. - Diversity and Versatility in Small RNA-Mediated Regulation in Bacterial Pathogens.
Felden B, Augagneur Y. Felden B, et al. Front Microbiol. 2021 Aug 10;12:719977. doi: 10.3389/fmicb.2021.719977. eCollection 2021. Front Microbiol. 2021. PMID: 34447363 Free PMC article. Review. - A cell engineering approach to enzyme-based fed-batch fermentation.
Sibley M, Ward JM. Sibley M, et al. Microb Cell Fact. 2021 Jul 24;20(1):146. doi: 10.1186/s12934-021-01634-y. Microb Cell Fact. 2021. PMID: 34303374 Free PMC article. - TISIGNER.com: web services for improving recombinant protein production.
Bhandari BK, Lim CS, Gardner PP. Bhandari BK, et al. Nucleic Acids Res. 2021 Jul 2;49(W1):W654-W661. doi: 10.1093/nar/gkab175. Nucleic Acids Res. 2021. PMID: 33744969 Free PMC article. - Altered Fecal Small RNA Profiles in Colorectal Cancer Reflect Gut Microbiome Composition in Stool Samples.
Tarallo S, Ferrero G, Gallo G, Francavilla A, Clerico G, Realis Luc A, Manghi P, Thomas AM, Vineis P, Segata N, Pardini B, Naccarati A, Cordero F. Tarallo S, et al. mSystems. 2019 Sep 17;4(5):e00289-19. doi: 10.1128/mSystems.00289-19. mSystems. 2019. PMID: 31530647 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases