» Articles » PMID: 17120115

Helicase: Mystery of Progression

Overview
Journal Mol Biol Rep
Specialty Molecular Biology
Date 2006 Nov 23
PMID 17120115
Authors
Affiliations
Soon will be listed here.
Abstract

Helicases mode of unwinding the nucleic acids and translocation along single stranded nucleic acids is still a subject of great curiosity. Based on the energy transduction and electrophilic interactions, we present a model to explain the mode of action of active helicases. This model considers that both strand separation as well as translocation is active processes fueled by NTP hydrolysis. The model proposes that the translocation appears to involve creeping of helicase over the ssNA lattice rather than inchworm movement.

References
1.
Yarranton G, Gefter M . Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein. Proc Natl Acad Sci U S A. 1979; 76(4):1658-62. PMC: 383449. DOI: 10.1073/pnas.76.4.1658. View

2.
Soultanas P, Dillingham M, Wiley P, Webb M, Wigley D . Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 2000; 19(14):3799-810. PMC: 313991. DOI: 10.1093/emboj/19.14.3799. View

3.
Taylor A, Smith G . RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature. 2003; 423(6942):889-93. DOI: 10.1038/nature01674. View

4.
Betterton M, Julicher F . Opening of nucleic-acid double strands by helicases: active versus passive opening. Phys Rev E Stat Nonlin Soft Matter Phys. 2005; 71(1 Pt 1):011904. DOI: 10.1103/PhysRevE.71.011904. View

5.
Singleton M, Dillingham M, Gaudier M, Kowalczykowski S, Wigley D . Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks. Nature. 2004; 432(7014):187-93. DOI: 10.1038/nature02988. View