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Nucleic Acids Research, 1994, Vol. 22, No. 9 1555-1561
© 1994

MOLECULAR BIOLOGY

Intramolecular signal transduction within the FixJ transcriptional activator: in vitro evidence for the inhibitory effect of the phosphorylatable regulatory domain

Sandra Da Re, Stéphane Bertagnoli+, Joëlle Fourment, Jean-Marc Reyrat and Daniel Kahn*

Laboratoire de Biologie Moléculaire des Relations Plantes–Microorganismes CNRS-INRA, BP27, F-31326 Castanet-Tolosan Cedex, France

*To whom correspondence should be addressed

Received February 18, 1994. Revised March 24, 1994. Accepted March 24, 1994.

FixJ is a phosphorylatable ‘response regulator’ controlling the transcription of the key nitrogen fixation genes nifA and fixK in Rhizobium meliloti. Sequence and genetic analyses indicated that FixJ comprises an N-terminal phosphorylatable regulatory domain, FixJN, and a C-terminal transcriptional activator domain, FixJC. We have now overexpressed and purified the FixJC protein and show that it is fully active in an in vitro transcription system with purified RNA polymerase. FixJC appeared to act synergistically with RNA polymerase at the nifA promoter. Furthermore FixJC was more active in vitro than the full-length dephosphorylated FixJ protein. Therefore activity of FixJC is inhibited by FixJN within the FixJ protein. This inhibition is relieved by phosphorylation of FixJN. Such a negative mode of intramolecular signal transduction may be generalizable to other response regulators.

+Present address: Ecole Nationale Vétérinaire, Laboratoire Associé INRA de Microbiologie Moléculaire, Toulouse, France


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