Intramolecular signal transduction within the FixJ transcriptional activator: in vitro evidence for the inhibitory effect of the phosphorylatable regulatory domain
Identifieur interne : 004945 ( Main/Exploration ); précédent : 004944; suivant : 004946Intramolecular signal transduction within the FixJ transcriptional activator: in vitro evidence for the inhibitory effect of the phosphorylatable regulatory domain
Auteurs : Sandra Da Re [France] ; Stéphane Bertagnoli [France] ; Joëlle Fourment [France] ; Jean-Marc Reyrat [France] ; Daniel Kahn [France]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 1994-05-11.
Abstract
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.
Url:
DOI: 10.1093/nar/22.9.1555
Affiliations:
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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.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Midi-Pyrénées</li><li>Occitanie (région administrative)</li></region><settlement><li>Castanet-Tolosan</li></settlement></list><tree><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Re, Sandra Da" sort="Re, Sandra Da" uniqKey="Re S" first="Sandra Da" last="Re">Sandra Da Re</name></region><name sortKey="Bertagnoli, Stephane" sort="Bertagnoli, Stephane" uniqKey="Bertagnoli S" first="Stéphane" last="Bertagnoli">Stéphane Bertagnoli</name><name sortKey="Fourment, Joelle" sort="Fourment, Joelle" uniqKey="Fourment J" first="Joëlle" last="Fourment">Joëlle Fourment</name><name sortKey="Kahn, Daniel" sort="Kahn, Daniel" uniqKey="Kahn D" first="Daniel" last="Kahn">Daniel Kahn</name><name sortKey="Reyrat, Jean Marc" sort="Reyrat, Jean Marc" uniqKey="Reyrat J" first="Jean-Marc" last="Reyrat">Jean-Marc Reyrat</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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