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PMID: 2768236 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

DNA ring closure mediated by protein HU.

The Journal of biological chemistry ·Vol. 264 ·No. 25 ·1989-09-05 ·Pages 14621-3

Hodges-Garcia Y, Hagerman PJ, Pettijohn DE

Abstract

The histone-like protein HU serves as an accessory factor that can facilitate the interaction of certain proteins with their specific DNA binding sites. Examples occur in different systems for prokaryotic DNA replication, transcription, and gene regulation. The protein-DNA interactions that are stimulated by HU generally involve coiling or looping of the DNA, and the possibility has been considered that HU exerts its effect by contributing flexibility to different DNA binding sites, but there has been no direct demonstration of this. To explore the possibility that HU can mediate tight DNA curvatures, we studied its effect on the formation of DNA circles when DNA ligase cyclizes short linear DNA fragments. It is demonstrated that HU greatly increases the cyclization rates of all fragments that were examined having lengths greater than 98 base pairs. Fragments of 99, 108, 120, or 126 base pairs could not cyclize in the absence of HU, but cyclization went rapidly with HU, showing that HU can mediate very tight DNA curvatures.

MeSH Terms
Bacterial Proteins/physiology Cyclization DNA/metabolism DNA Ligases/physiology DNA-Binding Proteins/physiology Kinetics Nucleic Acid Conformation Nucleic Acid Heteroduplexes/metabolism
Chemicals
Bacterial Proteins DNA-Binding Proteins Nucleic Acid Heteroduplexes histone-like protein HU, bacteria DNA DNA Ligases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hodges-Garcia Y
Department of Biochemistry, Biophysics/Genetics, University of Colorado Health Sciences Center, Denver 80262.
Hagerman P J
Pettijohn D E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1989-09-05
Pages
14621-3
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM 18243 · United States
NIGMS NIH HHS · GM 35305 · United States
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