Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

ABSTRACT: A strain of Escherichia coli missing three members of the thioredoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed to be due to the inability of cells to reduce the essential enzyme ribonucleotide reductase. Two classes of mutations can restore growth to such a strain. First, we have isolated a collection of mutations in the gene for the protein glutaredoxin 3 that suppress the growth defect. Remarkably, all eight independent mutations alter the same amino acid, methionine-43, changing it to valine, isoleucine, or leucine. From the position of the amino acid changes and their effects, we propose that these alterations change the protein so that its properties are closer to those of glutaredoxin 1. The second means of suppressing the growth d

SUBMITTER: Ortenberg R 

PROVIDER: S-EPMC409937 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature