Properties of a mutant form of the prokaryotic enhancer binding protein, NTRC, which hydrolyses ATP in the absence of effectors

FEBS Letters

Dixon, Ray¹  Austin, Sara¹  Widdick, David¹  Farez-Vidal, Esther¹ 

[1] Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, UK

关键词: Transcription factor;    ATP hydrolysis;    Phosphorylation;    Enhancer binding protein;   

DOI  :  10.1016/S0014-5793(98)01206-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The mutation S170A in the proposed nucleotide binding site of the transcriptional activator protein NTRC abolishes its ability to catalyse open promoter complex formation by the σ^N-RNA polymerase holoenzyme. NTRC^S170A has significant ATPase activity, which, in contrast to the wild-type protein, is unaffected by phosphorylation or binding to enhancer sites on DNA. The mutant protein appears to oligomerise normally on DNA in response to phosphorylation but the ATPase activity is apparently not responsive to changes in oligomerisation state. The defect in transcriptional activation is discussed in relation to mutations in other σ^N-dependent activators.

【 授权许可】

Unknown