The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription.
Sigma 54-dependent transcriptional activators such as Escherichia coli NtrC, Rhizobium meliloti NifA, and Rhizobium leguminosarum DctD share similar central and carboxy-terminal domains but differ in the structure and function of their amino-terminal domains. We have deleted the amino-terminal and carboxy-terminal domains of R. leguminosarum DctD and have demonstrated that the central domain of DctD, like that of NifA, is transcriptionally competent.
Huala
E
E
Department of Genetics, Harvard Medical School, Boston, Massachusetts.
Stigter
J
J
Ausubel
F M
FM
D001224:Aspartic Acid / Q000494:pharmacology; D004252:DNA Mutational Analysis; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D011401:Promoter Regions, Genetic / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D016961:Rhizobium leguminosarum / Q000235:genetics / Q000378:metabolism*; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism; D013386:Succinates / Q000494:pharmacology; D019802:Succinic Acid; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000235:genetics*; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D012808:Sigma Factor; D013386:Succinates; D014157:Transcription Factors; D001224:Aspartic Acid; D019802:Succinic Acid; D001616:beta-Galactosidase