Characterization of the generimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 inEscherichia coli K12
- 1 June 1989
- journal article
- research article
- Published by Springer Nature in Molecular Genetics and Genomics
- Vol. 217 (2-3) , 281-288
- https://doi.org/10.1007/bf02464894
Abstract
Ribosomal protein S6 of wild-type strains ofEscherichia coli contains up to six glutamic acid residues at its C-terminus. The first two residues are encoded by the structural gene for this protein (rpsF) and the rest are added post-translationally. Mutants deficient in this modification were isolated and characterized genetically and biochemically. The S6 protein in these mutants appeared to contain only two glutamic acid residues at the C-terminus as expected. The mutated gene was termedrimK and was mapped at 18.7 min betweencmlA andaroA. TherimK gene was cloned into a cosmid vector and its nucleotide sequence determined. Analysis of the transcriptional and translational products of this gene indicates that it encodes a protein with an Mr of 31.5 kDa and that it forms an operon with a gene encoding a 24 kDa protein. AnrpsF mutant containing a Glu to Lys replacement in the second residue from the C-terminus of protein S6 was isolated. The S6 protein of this mutant was apparently inaccessible to the RimK modification system. This indicates that the RimK modification system requires the wild-type amino acid sequence at least in the C-terminal region of ribosomal protein S6.This publication has 51 references indexed in Scilit:
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