Abstract
Temperature-resistant pseudorevertants of the temperature-sensitive Escherichia coli mutant KNS19, harboring a mutation in rplX, the gene for ribosomal protein L24, were isolated, cloned, and sequenced. The codon GAC for the amino acid Asp in the temperature-sensitive mutant corresponding to position 84 in the protein chain mutated either back to the wild type (Gly) or to codons for the amino acids Tyr and Glu. Furthermore, rplX genes from two other mutants with an altered protein L24 were cloned and sequenced. The mutations were localized at position 56 (Gly to Asp) and at position 62 (Glu to Lys) in the rplX gene. The latter two mutants lacked a conditional lethal phenotype. The results suggest that the amino acid Gly at positions 56 and 84 in the protein might be involved in loop formations.
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- Branlant C., Sri Widada J., Krol A., Ebel J. P. RNA sequences in ribonucleoprotein fragments of the complex formed from ribosomal 23-S RNA and ribosomal protein L24 of Escherichia coli. Eur J Biochem. 1977 Mar 15;74(1):155–170. doi: 10.1111/j.1432-1033.1977.tb11377.x. [DOI] [PubMed] [Google Scholar]
- Cabezón T., Herzog A., Petre J., Yaguchi M., Bollen A. Ribosomal assembly deficiency in an Escherichia coli thermosensitive mutant having an altered L24 ribosomal protein. J Mol Biol. 1977 Nov 5;116(3):361–374. doi: 10.1016/0022-2836(77)90075-4. [DOI] [PubMed] [Google Scholar]
- Dabbs E. R. A spontaneous mutant of Escherichia coli with protein L24 lacking from the ribosome. Mol Gen Genet. 1982;187(3):453–458. doi: 10.1007/BF00332627. [DOI] [PubMed] [Google Scholar]
- Dabbs E. R., Wittman H. G. A strain of Escherichia coli which gives rise to mutations in a large number of ribosomal proteins. Mol Gen Genet. 1976 Dec 22;149(3):303–309. doi: 10.1007/BF00268532. [DOI] [PubMed] [Google Scholar]
- Geyl D., Böck A., Isono K. An improved method for two-dimensional gel-electrophoresis: analysis of mutationally altered ribosomal proteins of Escherichia coli. Mol Gen Genet. 1981;181(3):309–312. doi: 10.1007/BF00425603. [DOI] [PubMed] [Google Scholar]
- Kimura M., Kimura J., Ashman K. The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus. Eur J Biochem. 1985 Aug 1;150(3):491–497. doi: 10.1111/j.1432-1033.1985.tb09049.x. [DOI] [PubMed] [Google Scholar]
- Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nishi K., Dabbs E. R., Schnier J. DNA sequence and complementation analysis of a mutation in the rplX gene from Escherichia coli leading to loss of ribosomal protein L24. J Bacteriol. 1985 Sep;163(3):890–894. doi: 10.1128/jb.163.3.890-894.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nishi K., Schnier J. A temperature-sensitive mutant in the gene rplX for ribosomal protein L24 and its suppression by spontaneous mutations in a 23S rRNA gene of Escherichia coli. EMBO J. 1986 Jun;5(6):1373–1376. doi: 10.1002/j.1460-2075.1986.tb04369.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sanger F., Coulson A. R., Hong G. F., Hill D. F., Petersen G. B. Nucleotide sequence of bacteriophage lambda DNA. J Mol Biol. 1982 Dec 25;162(4):729–773. doi: 10.1016/0022-2836(82)90546-0. [DOI] [PubMed] [Google Scholar]
- Sibanda B. L., Thornton J. M. Beta-hairpin families in globular proteins. Nature. 1985 Jul 11;316(6024):170–174. doi: 10.1038/316170a0. [DOI] [PubMed] [Google Scholar]
- Sloof P., Hunter J. B., Garrett R. A., Branlant C. RNA-RNA interactions in the binding site of protein L24 on 23S ribosomal RNA of Escherichia coli: 1. Evidence for their occurrence between widely separated sequence regions. Nucleic Acids Res. 1978 Oct;5(10):3503–3513. doi: 10.1093/nar/5.10.3503. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Venkatachalam C. M. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers. 1968 Oct;6(10):1425–1436. doi: 10.1002/bip.1968.360061006. [DOI] [PubMed] [Google Scholar]