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J. Biol. Chem., Vol. 264, Issue 25, 14621-14623, Sep, 1989
Y Hodges-Garcia, PJ Hagerman and DE Pettijohn
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.
DNA ring closure mediated by protein HU
Department of Biochemistry, Biophysics/Genetics, University of Colorado Health Sciences Center, Denver 80262.
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