Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination

Muniyappa, K. ; Shaner, S. L. ; Tsang, S. S. ; Radding, C. M. (1984) Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination Proceedings of the National Academy of Sciences of the United States of America, 81 (9). pp. 2757-2761. ISSN 0027-8424

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Official URL: http://www.pnas.org/content/81/9/2757.abstract

Abstract

Secondary structure in single-stranded DNA impedes the presynaptic association of recA protein and consequently blocks the formation of joint molecules as evidenced by effects of temperature, nucleotide sequence, and ionic conditions. Escherichia coli single-strand-binding protein eliminates sequence-specific "cold spots" by removing folds even from sites of strong secondary structure. Thus, destabilization of secondary structure in single-stranded DNA is critical for the action of recA protein, whereas specific interactions directly between helix-destabilizing proteins and recA protein are unimportant.

Item Type:Article
Source:Copyright of this article belongs to National Academy of Sciences, USA.
ID Code:22460
Deposited On:25 Nov 2010 14:00
Last Modified:17 May 2016 06:29

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