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Nucleic Acids Research 2005 33(7):2166-2175; doi:10.1093/nar/gki510
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Published online 14 April 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Eukaryotic RNases H1 act processively by interactions through the duplex RNA-binding domain

Sergei A. Gaidamakov1, Inna I. Gorshkova1,2, Peter Schuck2, Peter J. Steinbach3, Hirofumi Yamada1, Robert J. Crouch1,* and Susana M. Cerritelli1

1Laboratory of Molecular Genetics, National Institute of Child Health and Human Development Bethesda, MD 20892, USA 2Protein Biophysics Resource, Division of Bioengineering and Physical Science, Office of Research Services, Office of the Director Bethesda, MD 20892, USA 3Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Department of Health and Human Services Bethesda, MD 20892, USA

*To whom correspondence should be addressed. Tel: +1 301 496 4082; Fax: +1 301 496 0243; Email: robert_crouch{at}nih.gov

Received February 17, 2005. Revised March 25, 2005. Accepted March 25, 2005.

Ribonucleases H have mostly been implicated in eliminating short RNA primers used for initiation of lagging strand DNA synthesis. Escherichia coli RNase HI cleaves these RNA–DNA hybrids in a distributive manner. We report here that eukaryotic RNases H1 have evolved to be processive enzymes by attaching a duplex RNA-binding domain to the RNase H region. Highly conserved amino acids of the duplex RNA-binding domain are required for processivity and nucleic acid binding, which leads to dimerization of the protein. The need for a processive enzyme underscores the importance in eukaryotic cells of processing long hybrids, most of which remain to be identified. However, long RNA–DNA hybrids formed during immunoglobulin class-switch recombination are potential targets for RNase H1 in the nucleus. In mitochondria, where RNase H1 is essential for DNA formation during embryogenesis, long hybrids may be involved in DNA replication.

The authors wish it to be known that, in their opinion, the first two authors should be considered as joint First Authors


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