한빛사
>
한빛사논문
한빛사논문
- 조회121
Nucleic Acids Res., Jan 24 2025, 53 (3) gkaf034 | https://doi.org/10.1093/nar/gkaf034
A novel ADP-directed chaperone function facilitates the ATP-driven motor activity of SARS-CoV helicase
Jeongmin Yu1,2, Hyeryeon Im1,2, HyeokJin Cho1,3, Yongmoon Jeon4, Jong-Bong Lee4, Gwangrog Lee1,2,*
1Single-Molecule and Cell Mechanobiology Laboratory, Daejeon, 34141, South Korea
1Single-Molecule and Cell Mechanobiology Laboratory, Daejeon, 34141, South Korea
2Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea
3School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, 61005, South Korea
3School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, 61005, South Korea
4Department of Physics, Pohang University of Science and Technology, Pohang, 37673, South Korea
*To whom correspondence should be addressed. : Gwangrog Lee
*To whom correspondence should be addressed. : Gwangrog Lee
Abstract
Helicase is a nucleic acid motor that catalyses the unwinding of double-stranded (ds) RNA and DNA via ATP hydrolysis. Helicases can act either as a nucleic acid motor that unwinds its ds substrates or as a chaperone that alters the stability of its substrates, but the two activities have not yet been reported to act simultaneously. Here, we used single-molecule techniques to unravel the synergistic coordination of helicase and chaperone activities, and found that the severe acute respiratory syndrome coronavirus helicase (nsp13) is capable of two modes of action: (i) binding of nsp13 in tandem with the fork junction of the substrate mechanically unwinds the substrate by an ATP-driven synchronous power stroke; and (ii) free nsp13, which is not bound to the substrate but complexed with ADP in solution, destabilizes the substrate through collisions between transient binding and unbinding events with unprecedented melting capability. Our findings provide new insights into how the same enzyme works via two modes on different parts of the substrate and synergistically catalyses the unwinding reaction, utilizing ATP and recycling its by-product ADP as an energy source.
논문정보
- Research article
- 2025년 01월 (BRIC 등록일 2025-02-03)
- 국내 연구진
- 생명과학 > 구조생물 및 생물물리학
댓글 작성 로그인
팝업 닫기관련 링크
연구자 키워드
관련분야 연구자보기
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기
