High-Fidelity DNA Sensing by Protein Binding Fluctuations

Details High-Fidelity DNA Sensing by Protein Binding Fluctuations High-Fidelity DNA Sensing by Protein Binding Fluctuations

2010-08-04

arxiv.org/abs/1008.0743v1

Phys Rev Lett. 2004 Dec 17;93(25):258103

Physics

Biological Physics

PACS numbers: 87.15.Ya, 87.14.Ee, 87.14.Gg http://www.ncbi.nlm.nih.gov/pubmed/15697950

Scientific paper

10.1103/PhysRevLett.93.258103

One of the major functions of RecA protein in the cell is to bind single-stranded DNA exposed upon damage, thereby triggering the SOS repair response.We present fluorescence anisotropy measurements at the binding onset, showing enhanced DNA length discrimination induced by adenosine triphosphate consumption. Our model explains the observed DNA length sensing as an outcome of out-of equilibrium binding fluctuations, reminiscent of microtubule dynamic instability. The cascade architecture of the binding fluctuations is a generalization of the kinetic proofreading mechanism. Enhancement of precision by an irreversible multistage pathway is a possible design principle in the noisy biological environment.

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