RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations.

Abstract:

:Most genetic regulatory mechanisms involve protein-DNA interactions. In these processes, the classical Watson-Crick DNA structure sometimes is distorted severely, which in turn enables the precise recognition of the specific sites by the protein. Despite its key importance, very little is known about such deformation processes. To address this general question, we have studied a model system, namely, RecA binding to double-stranded DNA. Results from micromanipulation experiments indicate that RecA binds strongly to stretched DNA; based on this observation, we propose that spontaneous thermal stretching fluctuations may play a role in the binding of RecA to DNA. This has fundamental implications for the protein-DNA binding mechanism, which must therefore rely in part on a combination of flexibility and thermal fluctuations of the DNA structure. We also show that this mechanism is sequence sensitive. Theoretical simulations support this interpretation of our experimental results, and it is argued that this is of broad relevance to DNA-protein interactions.

authors

Leger JF,Robert J,Bourdieu L,Chatenay D,Marko JF

doi

10.1073/pnas.95.21.12295

subject

Has Abstract

pub_date

1998-10-13 00:00:00

pages

12295-9

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

95

pub_type

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