Versatility of the carboxy-terminal domain of the alpha subunit of RNA polymerase in transcriptional activation: use of the DNA contact site as a protein contact site for MarA.
作者： Bindi Dangi , Angela M. Gronenborn , Judah L. Rosner , Robert G. Martin
DOI: 10.1111/J.1365-2958.2004.04250.X
关键词:
摘要: The transcriptional activator, MarA, interacts with RNA polymerase (RNAP) to activate promoters of the mar regulon. Here, we identify interacting surfaces MarA and carboxy-terminal domain alpha subunit RNAP (alpha-CTD) by NMR-based chemical shift mapping. Spectral changes were monitored for a MarA-DNA complex upon titration alpha-CTD, alpha-CTD MarA-DNA. mapping results confirmed mutational studies retention chromatography. A model ternary shows that uses '265-like determinant' contact at surface distant from DNA. This is unlike interaction CRP or Fis activators where '265 contacts DNA while another same molecule activator. These reveal new versatility in activation.
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