GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and G
- PMID: 2999765
- PMCID: PMC390844
- DOI: 10.1073/pnas.82.22.7500
GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and G
Abstract
The amino acid sequence of LepA protein, which has been shown to be cotranscribed with signal peptidase I in Escherichia coli, was compared with greater than 2000 known protein sequences. It was revealed that, of the 598 amino acid residues contained in LepA, an amino-terminal domain of 112 residues is homologous to a domain of similar size found in initiation factor 2, elongation factor Tu, and elongation factor G (IF2, EF-Tu, and EF-G), factors required for translation in E. coli. In this domain, 46 and 34 residues align perfectly with the corresponding regions of EF-G and EF-Tu, respectively. If functionally conserved residues within this domain (19 for EF-G and 17 for EF-Tu) are included, the overall resemblance is 58% and 46%, respectively, for EF-G and EF-Tu. A similar domain exists internally in IF2, where there is 42% overall resemblance with the domain of LepA. Immediately adjacent to this region is a small sequence of limited similarity that exists not only in EF-G, EF-Tu, and IF2 but also in the protooncogene c-Ha-ras-1 (from human bladder) and other GTP-binding proteins. Given these homologies, GTP-photoaffinity labeling and subcellular fractionation experiments were undertaken, and it was found that LepA is indeed a membrane-bound GTP-binding protein.
Similar articles
-
Small clusters of divergent amino acids surrounding the effector domain mediate the varied phenotypes of EF-G and LepA expression.Mol Microbiol. 1995 Mar;15(5):943-53. doi: 10.1111/j.1365-2958.1995.tb02363.x. Mol Microbiol. 1995. PMID: 7596295
-
The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain.J Mol Biol. 2007 Jan 12;365(2):468-79. doi: 10.1016/j.jmb.2006.10.025. Epub 2006 Oct 27. J Mol Biol. 2007. PMID: 17070545
-
Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors.Proc Natl Acad Sci U S A. 1984 Dec;81(24):7787-91. doi: 10.1073/pnas.81.24.7787. Proc Natl Acad Sci U S A. 1984. PMID: 6096856 Free PMC article.
-
Messenger RNA translation in prokaryotes: GTPase centers associated with translational factors.Biochimie. 1996;78(7):577-89. doi: 10.1016/s0300-9084(96)80004-6. Biochimie. 1996. PMID: 8955901 Review.
-
Crystallographic studies of elongation factor G.Biochem Cell Biol. 1995 Nov-Dec;73(11-12):1209-16. doi: 10.1139/o95-130. Biochem Cell Biol. 1995. PMID: 8722038 Review.
Cited by
-
Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.Int J Mol Sci. 2023 Apr 7;24(8):6878. doi: 10.3390/ijms24086878. Int J Mol Sci. 2023. PMID: 37108045 Free PMC article.
-
Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.Mol Cell Biol. 2017 May 31;37(12):e00653-16. doi: 10.1128/MCB.00653-16. Print 2017 Jun 15. Mol Cell Biol. 2017. PMID: 28320876 Free PMC article. Review.
-
Identification of two structural elements important for ribosome-dependent GTPase activity of elongation factor 4 (EF4/LepA).Sci Rep. 2015 Feb 25;5:8573. doi: 10.1038/srep08573. Sci Rep. 2015. PMID: 25712150 Free PMC article.
-
Ribosomal elongation factor 4 promotes cell death associated with lethal stress.mBio. 2014 Dec 9;5(6):e01708. doi: 10.1128/mBio.01708-14. mBio. 2014. PMID: 25491353 Free PMC article.
-
The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli.Nucleic Acids Res. 2014 Dec 1;42(21):13370-83. doi: 10.1093/nar/gku1098. Epub 2014 Nov 6. Nucleic Acids Res. 2014. PMID: 25378333 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials