In this study, we have analyzed an ORF from Corynebacterium glutamicum, which codes for a homologue of the Streptomyces coelicolor WhiB-family of proteins known to be involved in sporulation. This ORF encoded a putative protein which harbors a helix-turn-helix DNA-binding motif and a probable redox-sensing motif, and has been designated whcE. We constructed a whcE mutant strain and analyzed the strain under a variety of growth conditions. This mutant strain exhibited a prolonged lag phase and earlier death within the stationary phase, suggesting that the relevant gene may play a role in both growth adaptation and stress responses. Further analysis determined that the mutant strain was not only sensitive with regard to survival under heat stress, but was also markedly susceptible to thiol-specific oxidant diamide and redox cycling compounds, including menadione and plumbagin. The mutant strain also exhibited reductions in thioredoxin reductase activity, which indicates that the trxB gene encoding thioredoxin reductase is under the control of WhcE. Expression of whcE was stimulated during the stationary phase of cell growth and could be modulated by diamide. We also delineated the relationship between whcE and the sigH gene, which is located downstream of whcE, and has been shown to be involved in heat stress responses, via the encoding of an ECF sigma factor. In a sigH mutant strain, the whcE gene was no longer expressed, thereby suggesting that the sigmaH sigma factor is involved in whcE expression. Our results suggest that WhcE functions as a transcription factor which can activate the trxB gene, as well as other genes, possibly by sensing redox changes during the metabolic downshifting of cells from exponential growth to the stationary phase, whereas sigmaH appears to function as the sigma factor for these genes, including whcE.