PMID: 9183010May 1, 1997Paper

Thermochemical and kinetic evidence for nucleotide-sequence-dependent RecA-DNA interactions

European Journal of Biochemistry
P WittungB Nordén

Abstract

RecA catalyses homologous recombination in Escherichia coli by promoting pairing of homologous DNA molecules after formation of a helical nucleoprotein filament with single-stranded DNA. The primary reaction of RecA with DNA is generally assumed to be unspecific. We show here, by direct measurement of the interaction enthalpy by means of isothermal titration calorimetry, that the polymerisation of RecA on single-stranded DNA depends on the DNA sequence, with a high exothermic preference for thymine bases. This enthalpic sequence preference of thymines by RecA correlates with faster binding kinetics of RecA to thymine DNA. Furthermore, the enthalpy of interaction between the RecA x DNA filament and a second DNA strand is large only when the added DNA is complementary to the bound DNA in RecA. This result suggests a possibility for a rapid search mechanism by RecA x DNA filaments for homologous DNA molecules.

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Citations

Apr 14, 2010·Journal of Molecular Modeling·Claudio Carra, Francis A Cucinotta
Oct 15, 1998·Proceedings of the National Academy of Sciences of the United States of America·J F LegerJ F Marko
Nov 18, 2009·Journal of Biomolecular Structure & Dynamics·Claudio Carra, Francis A Cucinotta
May 11, 2006·Nucleic Acids Research·Rakhi RajanCharles E Bell
Jun 28, 2013·Nucleic Acids Research·Sung Hyun KimDoseok Kim
Jul 3, 2007·Analytical Biochemistry·Andrew M LeeScott F Singleton
Jan 22, 2005·Trends in Biotechnology·Alexander A VolodinR Daniel Camerini-Otero
Mar 10, 2001·Journal of Molecular Biology·K MorimatsuM Takahashi
Sep 30, 2004·Biophysical Journal·Renaud FulconisJean-Louis Viovy
Jul 2, 2003·FEBS Letters·Alexander A VolodinR Daniel Camerini-Otero
Sep 16, 2017·Science Advances·Sung Hyun KimDoseok Kim
Dec 11, 2003·Journal of the American Chemical Society·Alberto I Roca, Scott F Singleton

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