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A motor that makes its own track: helicase unwinding of DNA.

作者信息

Betterton M D, Jülicher Frank

机构信息

Insitut Curie, Physico-chimie Curie, UMR 168, 26 rue d'Ulm, 75248 Paris Cedex 05, France.

出版信息

Phys Rev Lett. 2003 Dec 19;91(25):258103. doi: 10.1103/PhysRevLett.91.258103. Epub 2003 Dec 18.

DOI:10.1103/PhysRevLett.91.258103
PMID:14754162
Abstract

We study the unwinding of DNA by helicase proteins as a representative system in which a motor protein interacts with a mobile obstacle. In our discrete model, the interaction between the helicase and the DNA fork is characterized by an interaction potential. For the case of a hard-wall potential, the helicase opens the DNA by rectifying thermal fluctuations which spontaneously open base pairs. A potential with nonzero range describes the destabilization of the double strand by the enzymatic action of the helicase. We derive solutions for the opening speed as a function of the potential shape and relate our results to experiments on helicase motion.

摘要

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