Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA - PubMed (original) (raw)
Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA
J Schnier et al. Proc Natl Acad Sci U S A. 1982 Feb.
Abstract
The primary structure of proteins S1, the largest protein component of the Escherichia coli ribosome, has been elucidated by determining the amino acid sequence of the protein (from E. coli MRE600) and the nucleotide sequence of the S1 gene (rpsA, of a K-12 strain). The two methods gave results in perfect agreement except of two positions where possible strain specific differences were found. Protein S1 (MRE600) is composed of 557 amino acid residues (no modified amino acids were detected) and has Mr 61,159. The DNA sequence for protein S1 (K-12) suggests 556 amino acid residues. A computer survey of the sequence revealed three regions in S1 with a high degree of internal homology. The ribosome binding domain of S1 (NH2 terminus) does not show any preponderance of basic amino acids. The two cysteine and the majority of tryptophan residues of S1 as well as two od the three homologous regions were located in its middle region which contains the nucleic acid binding domain. The pattern of degenerate codon usage in the S1 gene is nonrandom and similar to that reported for other ribosomal protein genes.
Similar articles
- Primary structure of Escherichia coli ribosomal protein S1 and features of its functional domains.
Kimura M, Foulaki K, Subramanian AR, Wittmann-Liebold B. Kimura M, et al. Eur J Biochem. 1982 Mar;123(1):37-53. doi: 10.1111/j.1432-1033.1982.tb06495.x. Eur J Biochem. 1982. PMID: 7040075 - The Bacillus subtilis chromosome region encoding homologues of the Escherichia coli mssA and rpsA gene products.
Sorokin A, Serror P, Pujic P, Azevedo V, Ehrlich SD. Sorokin A, et al. Microbiology (Reading). 1995 Feb;141 ( Pt 2):311-9. doi: 10.1099/13500872-141-2-311. Microbiology (Reading). 1995. PMID: 7704259 - The last RNA-binding repeat of the Escherichia coli ribosomal protein S1 is specifically involved in autogenous control.
Boni IV, Artamonova VS, Dreyfus M. Boni IV, et al. J Bacteriol. 2000 Oct;182(20):5872-9. doi: 10.1128/JB.182.20.5872-5879.2000. J Bacteriol. 2000. PMID: 11004188 Free PMC article. - Variation in base composition, structure-function relationships, and origins of structural repetition in bacterial rpsA gene.
Machulin AV, Deryusheva EI, Galzitskaya OV. Machulin AV, et al. Biosystems. 2024 Apr;238:105196. doi: 10.1016/j.biosystems.2024.105196. Epub 2024 Mar 25. Biosystems. 2024. PMID: 38537772 - Ribosomal protein S1 (RpsA) of Buchnera aphidicola, the endosymbiont of aphids: characterization of the gene and detection of the product.
Clark MA, Baumann L, Baumann P, Rouhbakhsh D. Clark MA, et al. Curr Microbiol. 1996 Feb;32(2):89-94. doi: 10.1007/s002849900016. Curr Microbiol. 1996. PMID: 8574133
Cited by
- Inhibitory protein-protein interactions of the SIRT1 deacetylase are choreographed by post-translational modification.
Krzysiak TC, Choi YJ, Kim YJ, Yang Y, DeHaven C, Thompson L, Ponticelli R, Mermigos MM, Thomas L, Marquez A, Sipula I, Kemper JK, Jurczak M, Thomas G, Gronenborn AM. Krzysiak TC, et al. Protein Sci. 2024 Apr;33(4):e4938. doi: 10.1002/pro.4938. Protein Sci. 2024. PMID: 38533551 - Function of the RNA Coliphage Qβ Proteins in Medical In Vitro Evolution.
Singleton RL, Sanders CA, Jones K, Thorington B, Egbo T, Coats MT, Waffo AB. Singleton RL, et al. Methods Protoc. 2018 May 31;1(2):18. doi: 10.3390/mps1020018. Methods Protoc. 2018. PMID: 31164561 Free PMC article. Review. - A segment of cold shock protein directs the folding of a combinatorial protein.
de Bono S, Riechmann L, Girard E, Williams RL, Winter G. de Bono S, et al. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1396-401. doi: 10.1073/pnas.0407298102. Epub 2005 Jan 25. Proc Natl Acad Sci U S A. 2005. PMID: 15671167 Free PMC article. - Origin and diversity of alginate lyases of families PL-5 and -7 in Sphingomonas sp. strain A1.
Miyake O, Ochiai A, Hashimoto W, Murata K. Miyake O, et al. J Bacteriol. 2004 May;186(9):2891-6. doi: 10.1128/JB.186.9.2891-2896.2004. J Bacteriol. 2004. PMID: 15090531 Free PMC article. - Overexpression, purification, and partial characterization of ADP-ribosyltransferases modA and modB of bacteriophage T4.
Tiemann B, Depping R, Rüger W. Tiemann B, et al. Gene Expr. 1999;8(3):187-96. Gene Expr. 1999. PMID: 10634320 Free PMC article.
References
- J Biol Chem. 1974 May 25;249(10):3314-6 - PubMed
- FEBS Lett. 1974 May 1;41(2):323-6 - PubMed
- Proc Natl Acad Sci U S A. 1975 Jun;72(6):2325-9 - PubMed
- Eur J Biochem. 1976 May 1;64(2):511-8 - PubMed
- Proc Natl Acad Sci U S A. 1976 Jun;73(6):1824-8 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous