Osmosensitivity associated with insertions in argP (iciA) or glnE in glutamate synthase-deficient mutants of Escherichia coli

Journal of Bacteriology
Madhusudan R NandineniJ Gowrishankar

Abstract

An ampicillin enrichment strategy following transposon insertion mutagenesis was employed to obtain NaCl-sensitive mutants of a gltBD (glutamate synthase [GOGAT]-deficient) strain of Escherichia coli. It was reasoned that the gltBD mutation would sensitize the parental strain even to small perturbations affecting osmotolerance. Insertions conferring an osmosensitive phenotype were identified in the proU, argP (formerly iciA), and glnE genes encoding a glycine betaine/proline transporter, a LysR-type transcriptional regulator, and the adenylyltransferase for glutamine synthetase, respectively. The gltBD+ derivatives of the strains were not osmosensitive. The argP mutation, but not the glnE mutation, was associated with reduced glutamate dehydrogenase activity and a concomitant NH4+ assimilation defect in the gltBD strain. Supplementation of the medium with lysine or a lysine-containing dipeptide phenocopied the argP null mutation for both osmosensitivity and NH4+ assimilation deficiency in a gltBD background, and a dominant gain-of-function mutation in argP was associated with suppression of these lysine inhibitory effects. Osmosensitivity in the gltBD strains, elicited either by lysine supplementation or by introduction of the ...Continue Reading

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Citations

May 17, 2007·Genes & Development·Rakesh S Laishram, Jayaraman Gowrishankar
Sep 6, 2011·Journal of Bacteriology·Carmelita N Marbaniang, J Gowrishankar
May 23, 2007·Proceedings of the National Academy of Sciences of the United States of America·Dalai Yan
Jul 6, 2016·International Journal of Food Microbiology·Aline MétrisDelphine Ropers
Jul 4, 2019·Amino Acids·Daniel Charlier, Indra Bervoets

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