PMID:2841193
| Citation |
Csonka, LN, Gelvin, SB, Goodner, BW, Orser, CS, Siemieniak, D and Slightom, JL (1988) Nucleotide sequence of a mutation in the proB gene of Escherichia coli that confers proline overproduction and enhanced tolerance to osmotic stress. Gene 64:199-205 |
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| Abstract |
We determined the nucleotide (nt) sequence of a mutation that confers proline overproduction and enhanced tolerance of osmotic stress on bacteria. The mutation, designated as proB74, is an allele of the Escherichia coli proB gene which results in a loss of allosteric regulation of the protein product, gamma-glutamyl kinase. Our sequencing indicated that the proB74 mutation is a substitution of an A for a G at nt position 319 of the coding strand of the gene, resulting in a change of an aspartate to an asparagine at amino acid (aa) residue 107 of the predicted protein product. Rushlow et al. [Gene 39 (1984) 109-112] determined that another proB mutation (designated as DHPR), that resulted in a loss of allosteric inhibition by proline of the E. coli gamma-glutamyl kinase, was due to a substitution of an alanine for a glutamate at aa residue 143. Therefore, even though both the DHPR and the proB74 mutations caused a loss of allosteric inhibition of gamma-glutamyl kinase, they are due to different amino acid substitutions. |
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| Keywords |
Alleles; Allosteric Regulation; Base Sequence; Crosses, Genetic; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Genes, Regulator; Mutation; Osmolar Concentration; Phosphotransferases/genetics; Phosphotransferases/metabolism; Phosphotransferases (Carboxyl Group Acceptor); Proline/biosynthesis |
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