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. 1969 Dec;100(3):1322–1327. doi: 10.1128/jb.100.3.1322-1327.1969

Sulfur-Deficient Transfer Ribonucleic Acid in a Cysteine-Requiring, “Relaxed” Mutant of Escherichia coli1

Charles L Harris a, Edward B Titchener a, Athol L Cline a,2
PMCID: PMC250326  PMID: 4902813

Abstract

A cysteine-requiring mutant of the parent strain Escherichia coli Hfr Cavalli (RCrel, Met−, λ) has been isolated. The mutant was selected by using replica plating after mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine. The mutation appears to be in the gene for sulfite reductase, since the mutant could utilize sulfide but not sulfite as a sulfur source. The mutant was found to be RCrel with respect to both methionine and cysteine. During cysteine starvation, transfer ribonucleic acid (tRNA) deficient in 4-thiouracil was produced, and in vivo studies indicate that this tRNA can accept sulfur groups to a greater extent than normal tRNA. Further, there were differences both in the rate and extent of amino acid acceptance between normal and sulfur-deficient tRNA. This suggests that thionucleotides are involved in at least one of the biological functions of the tRNA molecule.

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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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