
Biological and Biomedical Sciences
Microbiology and Molecular Genetics
Harvard Medical School (Boston, MA)
In the cytoplasm of E. coli, enzymes form disulfide bonds as a part of their catalytic cycles. The reducing environment of the cytoplasm is however maintained by the thioredoxin and glutaredoxin pathways. One substrate of these pathways, ribonucleotide reductase (RNR), is essential for cell viability, and we can therefore perform suppressor analysis, selecting for growth of mutants that lack both pathways. My work has identified mutations in lipoamide dehydrogenase that suppress the cytoplasmic redox defect, and I am currently trying to further characterize these mutants.

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