Disassembly of Escherichia coli RecA E38K/ C17 Nucleoprotein Filaments Is Required to Complete DNA Strand Exchange*
نویسندگان
چکیده
Rachel L. Britt, Nami Haruta, Shelley L. Lusetti, Sindhu Chitteni-Pattu, Ross B. Inman, and Michael M. Cox From the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, the Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan, and the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003
منابع مشابه
Disassembly of Escherichia coli RecA E38K/DeltaC17 nucleoprotein filaments is required to complete DNA strand exchange.
Disassembly of RecA protein subunits from a RecA filament has long been known to occur during DNA strand exchange, although its importance to this process has been controversial. An Escherichia coli RecA E38K/DeltaC17 double mutant protein displays a unique and pH-dependent mutational separation of DNA pairing and extended DNA strand exchange. Single strand DNA-dependent ATP hydrolysis is catal...
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RecA protein primarily associates with and dissociates from opposite ends of nucleoprotein filaments formed on linear duplex DNA. RecA nucleoprotein filaments that are hydrolyzing ATP therefore engage in a dynamic process under some conditions that has some of the properties of treadmilling. We have also investigated whether the net polymerization of recA protein at one end of the filament and/...
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تاریخ انتشار 2010