
doi: 10.1007/bf00268529
pmid: 799246
An isogenic pair of Escherichia coli mutants (relA+ tufB valSts and relA1 tufB valSts) has been cultured at several temperatures to establish various degrees of limitation for valyl-tRNA synthetase. The biosynthetic rate of 16 identifiable proteins, most of which are components of the transcription and translation apparatus, was measured by pulse-labelling with [35S]-methionine, followed by protein separation using two-dimensional gel electrophoresis (O'Farrell, 1975). No single pattern of response to amino acid starvation of biosynthetic rate was observed. EF-Ts, L12 and S6 were found to be under strong stringent and relaxed regulation; EF-G, EF-Tu-A and S1 are under strong stringent, but weak relaxed regulation; EF-Tu-B, alpha, VRS, IRS and ARS are under week stringent and weak relaxed regulation; beta is under weak stringent regulation and does not respond at all to relaxed conditions; the biosynthetic rate of a protein called stringent starvation protein is strongly stimulated, relative to other proteins, in the starved stringent strain.
Transcription, Genetic, Valine, Guanine Nucleotides, Peptide Fragments, Kinetics, Bacterial Proteins, Species Specificity, Leucine, Protein Biosynthesis, Escherichia coli, Amino Acids, Uracil
Transcription, Genetic, Valine, Guanine Nucleotides, Peptide Fragments, Kinetics, Bacterial Proteins, Species Specificity, Leucine, Protein Biosynthesis, Escherichia coli, Amino Acids, Uracil
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