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RISS 인기검색어
- 검색키워드
- 저자 : Jergic, Slobodan (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
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Loading Dynamics of a Sliding DNA Clamp
Cho, Won-Ki,Jergic, Slobodan,Kim, Daehyung,Dixon, Nicholas E,Lee, Jong-Bong WILEY-VCH Verlag 2014 Angewandte Chemie Vol.53 No.26
<P>Sliding DNA clamps are loaded at a ss/dsDNA junction by a clamp loader that depends on ATP binding for clamp opening. Sequential ATP hydrolysis results in closure of the clamp so that it completely encircles and diffuses on dsDNA. We followed events during loading of an <I>E. coli</I> β clamp in real time by using single-molecule FRET (smFRET). Three successive FRET states were retained for 0.3 s, 0.7 s, and 9 min: Hydrolysis of the first ATP molecule by the γ clamp loader resulted in closure of the clamp in 0.3 s, and after 0.7 s in the closed conformation, the clamp was released to diffuse on the dsDNA for at least 9 min. An additional single-molecule polarization study revealed that the interfacial domain of the clamp rotated in plane by approximately 8° during clamp closure. The single-molecule polarization and FRET studies thus revealed the real-time dynamics of the ATP-hydrolysis-dependent 3D conformational change of the β clamp during loading at a ss/dsDNA junction.</P>
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Loading Dynamics of a Sliding DNA Clamp
Cho, Won‐,Ki,Jergic, Slobodan,Kim, Daehyung,Dixon, Nicholas E.,Lee, Jong‐,Bong WILEY‐VCH Verlag 2014 Angewandte Chemie Vol.126 No.26
<P><B>Abstract</B></P><P>Sliding DNA clamps are loaded at a ss/dsDNA junction by a clamp loader that depends on ATP binding for clamp opening. Sequential ATP hydrolysis results in closure of the clamp so that it completely encircles and diffuses on dsDNA. We followed events during loading of an <I>E. coli</I> β clamp in real time by using single‐molecule FRET (smFRET). Three successive FRET states were retained for 0.3 s, 0.7 s, and 9 min: Hydrolysis of the first ATP molecule by the γ clamp loader resulted in closure of the clamp in 0.3 s, and after 0.7 s in the closed conformation, the clamp was released to diffuse on the dsDNA for at least 9 min. An additional single‐molecule polarization study revealed that the interfacial domain of the clamp rotated in plane by approximately 8° during clamp closure. The single‐molecule polarization and FRET studies thus revealed the real‐time dynamics of the ATP‐hydrolysis‐dependent 3D conformational change of the β clamp during loading at a ss/dsDNA junction.</P>
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