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J. Biol. Chem., Vol. 276, Issue 37, 35024-35028, September 14, 2001
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From the The Escherichia coli RuvB protein is
a motor protein that 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, that 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
Ile148 and Ile150 are in a unique
A Unique
-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*
,§¶,**,
Research Institute for Microbial Diseases,
Osaka University 3-1 Yamadaoka, Suita, Osaka 565-0871, the
§ Japan Science and Technology Corporation Precursory
Research for Embryonic Science and Technology, 3-1 Yamadaoka, Suita, Osaka 565-0871, and the ** Biomolecular
Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka
565-0874, Japan
-hairpin
that protrudes from the AAA+ ATPase domain of RuvB. We
propose that this -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.
*
This work was supported by Grants-in-aid for Scientific
Research 08280102 and 0828010 on Priority Areas from the Ministry of
Education, Science, Sports and Culture of Japan (to H. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed. Tel.: 81-6-6879-8317;
Fax: 81-6-6879-8320; E-mail:
shinagaw@biken.osaka-u.ac.jp.
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