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PMID: 2834718 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Electrostatic calculations and model-building suggest that DNA bound to CAP is sharply bent.

Proteins ·Vol. 2 ·No. 4 ·1987-00-00 ·Pages 283-9

Warwicker J, Engelman BP, Steitz TA

Abstract

Two observations suggest that DNA, upon binding to E. coli catabolite gene activator protein (CAP), is sharply bent by a total angle of at least 100-150 degrees: (1) The electrostatic potential field of CAP shows regions of positive potential that form a ramp on 3 sides of the protein. (2) The DNA binding site size as determined by DNA ethylation interference with binding, (Majors: "Control of the E. coli Lac Operon at the Molecular Level." Ph.D. Thesis, Harvard University, Cambridge, 1977) and by relative affinities of DNA fragments of various lengths (Liu-Johnson et al.: Cell 47:995-1005, 1986) requires severe bending of the DNA to maintain its favorable electrostatic contact with the protein.

MeSH Terms
Bacterial Proteins/metabolism Chemical Phenomena Chemistry, Physical Cyclic AMP Receptor Protein/metabolism DNA, Bacterial/metabolism Models, Molecular Nucleic Acid Conformation RNA Polymerase I/metabolism
Chemicals
Bacterial Proteins Cyclic AMP Receptor Protein DNA, Bacterial RNA Polymerase I
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Warwicker J
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
Engelman B P
Steitz T A
Article Info
Journal
Proteins
Abbr.
Proteins
ISSN
0887-3585
Published
1987-00-00
Pages
283-9
Language
English
Region
United States
NLM ID
8700181
Subset
IM
Grants
NIGMS NIH HHS · GM 22778 · United States
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