A motor that makes its own track:: Helicase unwinding of DNA -: art. no. 258103

被引：48

作者：

Betterton, MD

Jülicher, F

机构：

[1] Inst Curie, Physicochim Curie, UMR 168, F-75248 Paris 05, France

[2] NYU, Courant Inst, New York, NY 10012 USA

[3] Max Planck Inst Phys Komplexer Syst, D-01187 Dresden, Germany

来源：

PHYSICAL REVIEW LETTERS | 2003年 / 91卷 / 25期

关键词：

D O I：

10.1103/PhysRevLett.91.258103

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

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.

引用

收藏

页数：4

相关论文

共 18 条

[1]

Alberts B., 2008, MOL BIOL CELL

[2] Kinetics of conformational fluctuations in DNA hairpin-loops [J].

Bonnet, G ;

Krichevsky, O ;

Libchaber, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (15) :8602-8606

[3] Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed [J].

Dillingham, MS ;

Wigley, DB ;

Webb, MR .

BIOCHEMISTRY, 2000, 39 (01) :205-212

[4] Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine [J].

Dillingham, MS ;

Wigley, DB ;

Webb, MR .

BIOCHEMISTRY, 2002, 41 (02) :643-651

[5]

Howard J., 2001, MECH MOTOR PROTEINS

[6] The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends [J].

Hunter, AW ;

Caplow, M ;

Coy, DL ;

Hancock, WO ;

Diez, S ;

Wordeman, L ;

Howard, J .

MOLECULAR CELL, 2003, 11 (02) :445-457

[7] Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding [J].

Kim, JL ;

Morgenstern, KA ;

Griffith, JP ;

Dwyer, MD ;

Thomson, JA ;

Murcko, MA ;

Lin, C ;

Caron, PR .

STRUCTURE, 1998, 6 (01) :89-100

[8] Major domain swiveling revealed by the crystal structures of complexes of E-coli Rep helicase bound to single-stranded DNA and ADP [J].

Korolev, S ;

Hsieh, J ;

Gauss, GH ;

Lohman, TM ;

Waksman, G .

CELL, 1997, 90 (04) :635-647

[9] Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases [J].

Korolev, S ;

Yao, NH ;

Lohman, TM ;

Weber, PC ;

Waksman, G .

PROTEIN SCIENCE, 1998, 7 (03) :605-610

[10] Mechanisms of helicase-catalyzed DNA unwinding [J].

Lohman, TM ;

Bjornson, KP .

ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :169-214