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PMID: 2523702 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Footprint of the sigma protein.

Biochemical and biophysical research communications ·Vol. 160 ·No. 1 ·1989-04-14 ·Pages 121-5

Ramesh U, Meares CF

Abstract

Escherichia coli RNA Polymerase is a multi-subunit enzyme that catalyzes RNA synthesis, using DNA as a template. The sigma subunit of this enzyme plays an important role in the recognition of promoter sites on DNA. Using DNase I footprinting, we have found that in the absence of the other subunits, sigma binds specifically to the bacteriophage lambda PR promoter DNA sequence. In the presence of the sigma subunit alone, a protective footprint encompassing the region between residue positions -41 and +17 was observed (where +1 is the transcription start site). The holoenzyme gave a footprint covering the same region. Thus not only does the sigma subunit interact with the DNA promoter site in the absence of the other components of RNA polymerase, but also the footprint of sigma is indistinguishable from that of the holoenzyme.

MeSH Terms
Bacteriophage lambda/genetics Base Sequence Binding Sites DNA, Viral/metabolism DNA-Directed RNA Polymerases/metabolism Escherichia coli/enzymology Molecular Sequence Data Promoter Regions, Genetic Sigma Factor/metabolism Transcription Factors/metabolism Transcription, Genetic
Chemicals
DNA, Viral Sigma Factor Transcription Factors DNA-Directed RNA Polymerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ramesh U
Chemistry Department, University of California, Davis 95616.
Meares C F
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-04-14
Pages
121-5
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIGMS NIH HHS · GM 25909 · United States
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