TY - JOUR
T1 - A Unique β-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
AU - Han, Yong Woon
AU - Iwasaki, Hiroshi
AU - Miyata, Tomoko
AU - Mayanagi, Kouta
AU - Yamada, Kazuhiro
AU - Morikawa, Kosuke
AU - Shinagawa, Hideo
PY - 2001/9/14
Y1 - 2001/9/14
N2 - 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 β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-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.
AB - 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 β-hairpin that protrudes from the AAA+ ATPase domain of RuvB. We propose that this β-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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U2 - 10.1074/jbc.M103611200
DO - 10.1074/jbc.M103611200
M3 - Article
C2 - 11427534
AN - SCOPUS:0035860740
SN - 0021-9258
VL - 276
SP - 35024
EP - 35028
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 37
ER -