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M103611200v1
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Papers In Press, published online ahead of print June 26, 2001
J. Biol. Chem, 10.1074/jbc.M103611200
Submitted on April 23, 2001
Revised on June 19, 2001
Accepted on June 25, 2001

A unique beta-hairpin protruding from AAA+ ATPase domain of RuvB motor protein is involved in the interaction with RuvA DNA recognition protein for branch migration of Holliday junctions

Yoon-Woon Han, Hiroshi Iwasaki, Tomoko Miyata, Kouta Mayanagi, Kazuhiro Yamada, Kosuke Morikawa, and Hideo Shinagawa

Molecular and Cellular Biology, Graduate School of Integrated Science, Yokohama City University, Yokohama 230-0045

Corresponding Author: iwasaki{at}tsurumi.yokohama-cu.ac.jp

The Escherichia coli RuvB protein is a motor protein which forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, which do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that I148 and I150 are in a unique b-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this b-hairpin interacts with hydrophobic residues in the mobile third domain of RuvA, and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.


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