한빛사 논문
Abstract
Sung Hyun Kim †, Kaushik Ragunathan ‡, Jeehae Park ‡, Chirlmin Joo §, Doseok Kim *†, and Taekjip Ha *‡∥
† Department of Physics and Interdisciplinary Program of Integrated Biotechnology, Sogang University, Seoul 121-742, Korea
‡ Center for Biophysics and Computational Biology and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States
§ Kavli Institute of NanoScience, Department of BioNanoScience, Delft University of Technology, 2628 CJ Delft, The Netherlands
∥ Department of Physics and Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign and Howard Hughes Medical Institute, Urbana, Illinois 61801, United States
* Corresponding authors
Abstract
The active, stretched conformation of the RecA filament bound to single-stranded DNA is required for homologous recombination. During this process, the RecA filament mediates the homology search and base pair exchange with a complementary sequence. Subsequently, the RecA filament dissociates from DNA upon reaction completion. ATP binding and hydrolysis is critical throughout these processes. Little is known about the timescale, order of conversion between different cofactor bound forms during ATP hydrolysis, and the associated changes in filament conformation. We used single-molecule fluorescence techniques to investigate how ATP hydrolysis is coupled with filament dynamics. For the first time, we observed real-time cooperative structural changes within the RecA filament. This cooperativity between neighboring monomers provides a time window for nucleotide cofactor exchange, which keeps the filament in the active conformation amidst continuous cycles of ATP hydrolysis.
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