Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism
- PMID: 10275
- PMCID: PMC232829
- DOI: 10.1128/jb.128.1.86-98.1976
Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism
Abstract
We have isolated mutant strains (nit) of Salmonella typhimurium that are defective in nitrogen metabolism. They have a reduced ability to use a variety of compounds including glutamate, proline, arginine, N-acetyl-glucosamine, alanine, and adenosine as sole nitrogen source. In addition, although they grow normally on high concentrations of ammonium chloride (greater than 1 mM) as nitrogen source, they grow substantially more slowly than wild type at low concentrations (less than 1 mM). We postulated that the inability of these strains to utilize low concentrations of ammonium chloride accounts for their poor growth on other nitrogen sources. The specific biochemical lesion in strains with a nit mutation is not known; however, mutant strains have no detectable alteration in the activities of glutamine synthetase, glutamate synthetase, or glutamate dehydrogenase, the enzymes known to be involved in assimilation of ammonia. A nit mutation is suppressed by second-site mutations in the structural gene for glutamine synthetase (glnA) that decrease glutamine synthetase activity.
Similar articles
-
Regulation of ammonium ion assimilation enzymes in Neurospora crassa nit-2 and ms-5 mutant strains.Biochem Genet. 1993 Oct;31(9-10):425-39. doi: 10.1007/BF02396227. Biochem Genet. 1993. PMID: 7907211
-
Salmonella typhimurium mutants with altered glutamate dehydrogenase and glutamate synthase activities.J Bacteriol. 1980 Jan;141(1):190-8. doi: 10.1128/jb.141.1.190-198.1980. J Bacteriol. 1980. PMID: 6986357 Free PMC article.
-
Salmonella typhimurium LT-2 mutants with altered glutamine synthetase levels and amino acid uptake activities.J Bacteriol. 1978 Nov;136(2):588-96. doi: 10.1128/jb.136.2.588-596.1978. J Bacteriol. 1978. PMID: 30754 Free PMC article.
-
Regulation of the assimilation of nitrogen compounds.Annu Rev Biochem. 1978;47:1127-62. doi: 10.1146/annurev.bi.47.070178.005403. Annu Rev Biochem. 1978. PMID: 28074 Review. No abstract available.
-
An Overview of Important Enzymes Involved in Nitrogen Assimilation of Plants.Methods Mol Biol. 2020;2057:1-13. doi: 10.1007/978-1-4939-9790-9_1. Methods Mol Biol. 2020. PMID: 31595465 Review.
Cited by
-
Complementation of nitrogen-regulatory (ntr-like) mutations in Rhodobacter capsulatus by an Escherichia coli gene: cloning and sequencing of the gene and characterization of the gene product.J Bacteriol. 1987 Jan;169(1):260-71. doi: 10.1128/jb.169.1.260-271.1987. J Bacteriol. 1987. PMID: 3025172 Free PMC article.
-
OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio parahaemolyticus.J Bacteriol. 1998 Jun;180(12):3166-73. doi: 10.1128/JB.180.12.3166-3173.1998. J Bacteriol. 1998. PMID: 9620967 Free PMC article.
-
Regulation of transcription of glnA, the structural gene encoding glutamine synthetase, in glnA::Mu d1 (ApR, lac) fusion strains of Salmonella typhimurium.Mol Gen Genet. 1983;192(1-2):187-97. doi: 10.1007/BF00327665. Mol Gen Genet. 1983. PMID: 6139739
-
Organic nitrogen metabolism of phototrophic bacteria.Antonie Van Leeuwenhoek. 1989 Mar;55(3):197-219. doi: 10.1007/BF00393850. Antonie Van Leeuwenhoek. 1989. PMID: 2569291 Review.
-
NAD+ Synthetase is Required for Free-living and Symbiotic Nitrogen Fixation in the Actinobacterium Frankia casuarinae.Microbes Environ. 2023;38(1):ME22093. doi: 10.1264/jsme2.ME22093. Microbes Environ. 2023. PMID: 36858533 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources