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RNA-binding site in T7 RNA polymerase

S Sastry1, B M Ross

  • 1Laboratory of Molecular Genetics, Box 174, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. sastrys@rockvax.rockefeller.edu

Proceedings of the National Academy of Sciences of the United States of America
|August 5, 1998
PubMed
Summary

Researchers identified key interactions between T7 RNA polymerase and nascent RNA, revealing how these contacts stabilize transcription complexes. These findings shed light on the structural dynamics of phage RNA polymerase during RNA synthesis.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Enzyme-nascent RNA contacts are proposed to stabilize RNA polymerase transcription complexes.
  • Research on multisubunit Escherichia coli RNA polymerase is extensive, but single-subunit phage RNA polymerase complexes are less understood.

Purpose of the Study:

  • To investigate the structural interactions between T7 RNA polymerase and its nascent RNA.
  • To map contact sites and understand their contribution to transcription complex stability.

Main Methods:

  • Photo-cross-linking of RNA within the T7 RNA polymerase transcription complex.
  • Mapping of cross-linked sites to identify amino acid residues involved in RNA interaction.

Main Results:

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  • A major contact site was identified between T7 RNA polymerase residues 144-168 and the nascent RNA.
  • A minor contact site was suggested between residues 1-93 and the RNA.
  • Contacts were characterized as both ionic and nonionic (hydrophobic).
  • T7 lysozyme, an inhibitor, did not directly compete for RNA binding, suggesting an indirect mechanism of action.

Conclusions:

  • Specific regions of T7 RNA polymerase interact with the emerging RNA, contributing to complex stability.
  • The N-terminal region of T7 RNA polymerase likely forms a binding channel for nascent RNA.
  • T7 lysozyme may influence transcription through conformational changes in the polymerase rather than direct RNA binding.