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Journal of Bacteriology, January 2004, p. 580-587, Vol. 186, No. 2
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.2.580-587.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Molecular Biology and Microbiology, University of Central Florida, Orlando, Florida 32816 ,1 Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 326112
Received 24 June 2003/ Accepted 20 October 2003
On the basis of hyf-lacZ fusion studies, the hyf operon of Escherichia coli, noted for encoding the fourth hydrogenase isoenzyme (HYD4), is not expressed at a significant level in a wild-type strain. However, mutant FhlA proteins (constitutive activators of the hyc-encoded hydrogenase 3 isoenzyme) activated hyf-lacZ. HyfR, an FhlA homolog encoded by the hyfR gene present at the end of the hyf operon, also activated transcription of hyf-lacZ but did so only when hyfR was expressed from a heterologous promoter. The HYD4 isoenzyme did not substitute for HYD3 in H2 production. Optimum expression of hyf-lacZ required the presence of cyclic AMP receptor protein-cyclic AMP complex and anaerobic conditions when HyfR was the activator.
Florida Agricultural Experiment Station Journal Series no. R-09737.
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