The Full-length Saccharomyces cerevisiae Sgs1 Protein Is a Vigorous DNA Helicase That Preferentially Unwinds Holliday Junctions
Open Access
- 1 March 2010
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 285 (11) , 8290-8301
- https://doi.org/10.1074/jbc.m109.083196
Abstract
No abstract availableKeywords
This publication has 64 references indexed in Scilit:
- Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coliGenes & Development, 2009
- Human exonuclease 1 and BLM helicase interact to resect DNA and initiate DNA repairProceedings of the National Academy of Sciences, 2008
- DNA helicases Sgs1 and BLM promote DNA double-strand break resectionGenes & Development, 2008
- Sgs1 Helicase and Two Nucleases Dna2 and Exo1 Resect DNA Double-Strand Break EndsCell, 2008
- Resolution of Converging Replication Forks by RecQ and Topoisomerase IIIMolecular Cell, 2008
- Saccharomyces cerevisiae Replication Protein A Binds to Single-Stranded DNA in Multiple Salt-Dependent ModesBiochemistry, 2006
- Topoisomerase IIIα and Bloom’s helicase can resolve a mobile double Holliday junction substrate through convergent branch migrationProceedings of the National Academy of Sciences, 2006
- Sgs1 Regulates Gene Conversion Tract Lengths and Crossovers Independently of Its Helicase ActivityMolecular and Cellular Biology, 2006
- Structural dynamics of individual Holliday junctionsNature Structural & Molecular Biology, 2002
- Binding specificity determines polarity of DNA unwinding by the Sgs1 protein of S. cerevisiaeJournal of Molecular Biology, 1999