Physics of RecA-mediated homologous recognition

Biophysical Journal
Kevin KlapsteinRobijn Bruinsma

Abstract

To accomplish its DNA strand exchange activities, the Escherichia coli protein RecA polymerizes onto DNA to form a stiff helical nucleoprotein filament within which the DNA is extended by 50%. Homology search and recognition occurs between ssDNA within the filament and an external dsDNA molecule. We show that stretching the internal DNA greatly enhances homology recognition by increasing the probability that the homologous regions of a stretched DNA molecule and a parallel, unstretched DNA molecule will be "in register" at some position. We also show that the stretching and stiffness of the filament act together to ensure that initiation of homologous exchange between the substrate DNA molecules at one position precludes initiation of homologous exchange at any other position. This prevents formation of multiple exchange site "topological traps" which would prevent completion of the exchange reaction and resolution of the products.

References

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Citations

Jan 18, 2007·Nature Reviews. Molecular Cell Biology·Michael M Cox
Sep 17, 2009·Nature Reviews. Microbiology·Allon WeinerAbraham Minsky
Apr 3, 2012·Nucleic Acids Research·Lumir KrejciXiaolan Zhao
Apr 13, 2011·PloS One·Judith Miné-HattabJean-Louis Viovy
Mar 17, 2007·Critical Reviews in Biochemistry and Molecular Biology·Michael M Cox
Nov 13, 2010·Molecular Cell·Yonatan Savir, Tsvi Tlusty
Mar 4, 2017·PLoS Computational Biology·Amir BitranMara Prentiss
Feb 9, 2005·Physical Review Letters·Kevin D DorfmanJean-Louis Viovy
Mar 1, 2013·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·Julea VlassakisMara Prentiss
Jul 15, 2016·Physical Review. E·Sergio Cruz LeónMaria Fyta

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