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J. Biol. Chem., Vol. 281, Issue 52, 40144-40153, December 29, 2006

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Right-handed DNA Supercoiling by an Octameric Form of Histone-like Protein HU

MODULATION OF CELLULAR TRANSCRIPTION^*

Sudeshna Kar, Eugene J. Choi, Fusheng Guo, Emilios K. Dimitriadis, Svetlana L. Kotova, and Sankar Adhya¹

From the Laboratory of Molecular Biology, NCI, National Institutes of Health and Instrumentation Research and Development Resource, Division of Bioengineering and Physical Science, Office of Research Services, National Institutes of Health, Bethesda, Maryland 20892

In bacteria, the contribution of global nucleoid organization in determining cellular transcription programs is unclear. Using a mutant form of the most abundant nucleoid-associated protein HU, HU^E38K,V42L, we previously showed that nucleoid remodeling by the mutant protein re-organizes the global transcription pattern. Here, we demonstrate that, unlike the dimeric wild-type HU, HU^E38K,V42L is an octamer and wraps DNA around its surface. The formation of wrapped nucleoprotein complexes by HU^E38K,V42L leads to a high degree of DNA condensation. The DNA wrapping is right-handed, which restrains positive supercoils. In vivo, HU^E38K,V42L shows altered association and distribution patterns with the genetic loci whose transcription are differentially affected in the mutant strain.

Received for publication, June 9, 2006 , and in revised form, October 20, 2006.

^* This work was supported by the Intramural Research Program of the National Institutes of Health, NCI, Center for Cancer Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: 37 Convent Dr., Rm. 5138, Bethesda, MD 20892-4264. Tel.: 301-496-2495; Fax: 301-402-1455; E-mail: sadhya{at}helix.nih.gov.

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