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. 1969 Oct;100(1):377–382. doi: 10.1128/jb.100.1.377-382.1969

New Methionine Structural Gene in Salmonella typhimurium

J D Childs a,1, D A Smith b
PMCID: PMC315403  PMID: 4899000

Abstract

Eight metH mutants in Salmonella typhimurium with closely linked sites of mutation which could grow only on methionine were isolated from a metE mutant deficient in N5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase; their deficiency in cobalamin-dependent N5-methyltetrahydrofolate-homocysteine transmethylase was supported by the results of enzyme studies of one of them. Cotransduction of metH and metA (homoserine O-transsuccinylase) mutants was obtained, thus revealing linkage between a second pair of the six known methionine structural genes. One metH mutant clearly differed from the rest in that it reverted at a higher frequency, was temperature sensitive, complemented all other metH mutants, and was located farthest from the metA gene.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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