Display Settings:

Format

Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
J Biol Chem. 1999 Aug 13;274(33):23378-86.

Mapping interactions of Escherichia coli GreB with RNA polymerase and ternary elongation complexes.

Author information

  • 1The Rockefeller University, New York, New York 10021, USA.

Abstract

Escherichia coli GreA and GreB modulate transcription elongation by interacting with the ternary elongation complex (containing RNA polymerase, DNA template, and RNA transcript) to induce hydrolytic cleavage of the transcript and release of the 3'-terminal fragment. Hydroxyl radical protein footprinting and alanine-scanning mutagenesis were used to investigate the interactions of GreB with RNA polymerase alone and in a ternary elongation complex. A major determinant for binding GreB to both RNA polymerase and the ternary elongation complex was identified. In addition, the hydroxyl radical footprinting indicated major conformational changes of GreB, in terms of reorientations of the N- and C-terminal domains with respect to each other, particularly upon interactions with the ternary elongation complex.

PMID:
10438515
[PubMed - indexed for MEDLINE]
Free full text

LinkOut - more resources

Full Text Sources

Other Literature Sources

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk