Pleiotropic phenotype of an Escherichia coli mutant lacking leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase.
نویسندگان
چکیده
A mutant of Escherichia coli that lacks leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase had diminished activities of L-phenylalanyl-transfer ribonucleic acid synthetase and tryptophanase, grew faster than its parent with aspartic acid as the sole nitrogen source, accumulated higher levels of enterochelin in the medium during iron limitation, and exhibited an abnormal morphology.
منابع مشابه
Regulation of proline dehydrogenase activity in Escherichia coli by leucyl-, phenylalanyl-tRNA:protein transferase.
We have investigated the basis for an increased level of proline dehydrogenase activity, the most prominent phenotype displayed by a mutant of Escherichia coli lacking leucyl-, phenylalanyl-tRNA:protein transferase. A dehydrogenase preparation of approximately 95% purity from the transferaseless mutant contained glycine, which is not an acceptor determinant in the transfer reaction, as the sole...
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A mutant of Escherichia coli lacking leucyl,phenylalanyl-tRNA:protein leucyltransferase, EC 2.3.2.6) exhibited several abnormal growth characteristics relative to the wild type or a revertant when grown with glycerol as a carbon source. All three strains were auxotrophic for proline. The mutant required higher levels of this amino acid than did the other strains to attain a normal growth yield ...
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Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 129 1 شماره
صفحات -
تاریخ انتشار 1977