Functional significance of octameric RuvA for a branch migration complex from Thermus thermophilus
- Graduate School of Engineering Science, Osaka University, 1-3, Machikaneyama, Toyonaka, Osaka 560-8531 (Japan)
- Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga 526-0829 (Japan)
- Japan
- The Takara-Bio Endowed Division, Institute for Protein Research, Osaka University, 6-2-3, Furuedai, Suita, Osaka 565-0874 (Japan)
The RuvAB complex promotes migration of Holliday junction at the late stage of homologous recombination. The RuvA tetramer specifically recognizes Holliday junction to form two types of complexes. A single tetramer is bound to the open configuration of the junction DNA in complex I, while the octameric RuvA core structure sandwiches the same junction in complex II. The hexameric RuvB rings, symmetrically bound to both sides of RuvA on Holliday junction, pump out DNA duplexes, depending upon ATP hydrolysis. We investigated functional differences between the wild-type RuvA from Thermus thermophilus and mutants impaired the ability of complex II formation. These mutant RuvA, exclusively forming complex I, reduced activities of branch migration and ATP hydrolysis, suggesting that the octameric RuvA is essential for efficient branch migration. Together with our recent electron microscopic analysis, this finding provides important insights into functional roles of complex II in the coordinated branch migration mechanism.
- OSTI ID:
- 21043614
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 366, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2007.11.149; PII: S0006-291X(07)02562-4; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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