Mutational analysis of the phosphate-binding loop of Rhizobium meliloti DctD, a sigma54-dependent activator.
The phosphate-binding loop of sigma54-dependent activators is thought to participate in ATP binding and/or hydrolysis. Alanine substitutions at positions 3, 4, 6, 7, and 8 of this motif in Rhizobium meliloti DctD disrupted transcriptional activation and ATP hydrolysis. Interestingly, substitution of alanine at position 7 also affected DNA binding.
Gao
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Y
Department of Microbiology, University of Georgia, Athens, Georgia 30602, USA.
Wang
Y K
YK
Hoover
T R
TR
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012321:DNA-Directed RNA Polymerases / Q000235:genetics* / Q000378:metabolism; D006868:Hydrolysis; D009154:Mutation; D011487:Protein Conformation; D051877:RNA Polymerase Sigma 54; D012808:Sigma Factor / Q000235:genetics* / Q000378:metabolism; D016962:Sinorhizobium meliloti / Q000235:genetics* / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C073788:dctD protein, Rhizobium meliloti; D000255:Adenosine Triphosphate; D012321:DNA-Directed RNA Polymerases; D051877:RNA Polymerase Sigma 54