title: Active displacement of RecA filaments by UvrD translocase activity.
abstract: The UvrD helicase has been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro. We demonstrate that UvrD utilizes an active mechanism to remove RecA from the DNA. Efficient RecA removal depends on the availability of DNA binding sites for UvrD and/or the accessibility of the RecA filament ends. The removal of RecA from DNA also requires ATP hydrolysis by the UvrD helicase but not by RecA protein. The RecA-removal activity of UvrD is slowed by RecA variants with enhanced DNA-binding properties. The ATPase rate of UvrD during RecA removal is much slower than the ATPase activity of UvrD when it is functioning either as a translocase or a helicase on DNA in the absence of RecA. Thus, in this context UvrD may operate in a specialized disassembly mode.
authors.affiliation: Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Vessela
authors.initials: V
authors.lastname: Petrova
authors.affiliation: Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Stefanie H
authors.initials: SH
authors.lastname: Chen
authors.affiliation: Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Eileen T
authors.initials: ET
authors.lastname: Molzberger
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
authors.forename: Eric
authors.initials: E
authors.lastname: Tomko
authors.affiliation: Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Sindhu
authors.initials: S
authors.lastname: Chitteni-Pattu
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
authors.forename: Haifeng
authors.initials: H
authors.lastname: Jia
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
authors.forename: Yerdos
authors.initials: Y
authors.lastname: Ordabayev
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA.
authors.forename: Timothy M
authors.initials: TM
authors.lastname: Lohman
authors.affiliation: Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706, USA Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA cox@biochem.wisc.edu.
authors.forename: Michael M
authors.initials: MM
authors.lastname: Cox
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D004265:DNA Helicases / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism*; D011938:Rec A Recombinases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D017384:Sequence Deletion
chemical_list: D004277:DNA, Single-Stranded; D029968:Escherichia coli Proteins; D000255:Adenosine Triphosphate; D004247:DNA; D011938:Rec A Recombinases; D000251:Adenosine Triphosphatases; C506746:UvrD protein, E coli; D004265:DNA Helicases
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