Sulfur-Deficient Transfer Ribonucleic Acid in a Cysteine-Requiring, “Relaxed” Mutant of Escherichia coli1
AUTOR(ES)
Harris, Charles L.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=250326Documentos Relacionados
- Increased isoleucine acceptance by sulfur-deficient transfer RNA from Escherichia coli.
- Unusual Valyl-Transfer Ribonucleic Acid Synthetase Mutant of Escherichia coli1
- Growth-Linked Instability of a Mutant Valyl-Transfer Ribonucleic Acid Synthetase in Escherichia coli1
- Role of Aminoacyl-Transfer Ribonucleic Acid in the Regulation of Ribonucleic Acid Synthesis in Escherichia coli1
- Transcriptional and post-transcriptional regulation of storage protein gene expression in sulfur-deficient pea seeds.