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      The carboxy-terminal coiled-coil of the RNA polymerase beta'-subunit is the main binding site for Gre factors.

      EMBO Reports

      Amino Acid Sequence, Binding Sites, DNA-Directed RNA Polymerases, chemistry, genetics, metabolism, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Sequence Alignment, Transcriptional Elongation Factors

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          Abstract

          Bacterial Gre transcript cleavage factors stimulate the intrinsic endonucleolytic activity of RNA polymerase (RNAP) to rescue stalled transcription complexes. They bind to RNAP and extend their coiled-coil (CC) domains to the catalytic centre through the secondary channel. Three existing models for the Gre-RNAP complex postulate congruent mechanisms of Gre-assisted catalysis, while offering conflicting views of the Gre-RNAP interactions. Here, we report the GreB structure of Escherichia coli. The GreB monomers form a triangle with the tip of the amino-terminal CC of one molecule trapped within the hydrophobic cavity of the carboxy-terminal domain of a second molecule. This arrangement suggests an analogous model for recruitment to RNAP. Indeed, the beta'-subunit CC located at the rim of the secondary channel has conserved hydrophobic residues at its tip. We show that substitutions of these residues and those in the GreB C-terminal domain cavity confer defects in GreB activity and binding to RNAP, and present a plausible model for the RNAP-GreB complex.

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          Author and article information

          Journal
          10.1038/sj.embor.7401079
          2247394
          17917675

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