Journal of Bacteriology, August 1999, p. 5085-5089, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
F. A. Janssens Laboratory of Genetics, Katholieke Universiteit Leuven, B-3001 Heverlee, Belgium,1 and Laboratorio de Microbiología, Universidad Politécnica de Madrid, Escuela Técnica Superior de Ingenieros Agrónomos, 28040 Madrid, Spain2
Received 5 March 1999/Accepted 27 May 1999
The Bradyrhizobium japonicum hupT gene was sequenced, and its gene product was found to be homologous to NtrB-like histidine kinases. A hupT mutant expresses higher levels of hydrogenase activity than the wild-type strain under hydrogenase-inducing conditions (i.e., microaerobiosis plus hydrogen, or symbiosis), whereas in noninduced hupT cells, hupSL expression is derepressed but does not lead to hydrogenase activity. We conclude that HupT is involved in the repression of HupSL synthesis at the transcriptional level but that enzymatic activation requires inducing conditions.
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |