한빛사 논문
울산대학교
Seoyun Choi1, Seung-Won Lee2, Hajin Kim2,3,* and Byungchan Ahn1,*
1 Department of Life Sciences, University of Ulsan, Ulsan 44610, Republic of Korea, 2 School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44610, Republic of Korea and 3 Center for Genomic Integrity, Institute for Basic Science, Ulsan 44610, Republic of Korea
*To whom correspondence should be addressed.
Correspondence may also be addressed to Hajin Kim.
Abstract
The RecQ family of helicases is highly conserved both structurally and functionally from bacteria to humans. Defects in human RecQ helicases are associated with genetic diseases that are characterized by cancer predisposition and/or premature aging. RecQ proteins exhibit 3′-5′ helicase activity and play critical roles in genome maintenance. Recent advances in single-molecule techniques have revealed the reiterative unwinding behavior of RecQ helicases. However, the molecular mechanisms involved in this process remain unclear, with contradicting reports. Here, we characterized the unwinding dynamics of the Caenorhabditis elegans RecQ helicase HIM-6 using single-molecule fluorescence resonance energy transfer measurements. We found that HIM-6 exhibits reiterative DNA unwinding and the length of DNA unwound by the helicase is sharply defined at 25–31 bp. Experiments using various DNA substrates revealed that HIM-6 utilizes the mode of ‘sliding back’ on the translocated strand, without strand-switching for rewinding. Furthermore, we found that Caenorhabditis elegans replication protein A, a single-stranded DNA binding protein, suppresses the reiterative behavior of HIM-6 and induces unidirectional, processive unwinding, possibly through a direct interaction between the proteins. Our findings shed new light on the mechanism of DNA unwinding by RecQ family helicases and their co-operation with RPA in processing DNA.
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