Direct Evidence of the Role of ATPγS in the Binding of Single-Stranded Binding Protein (Escherichia coli) and RecA to Single-Stranded DNA
Author:
Affiliation:
1. Department of Chemistry and Institute for Optical Sciences, University of Toronto, Toronto, Ontario, M5S 3H6 Canada
2. Department of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen 518060, Guangdong Province, China
Publisher
American Chemical Society (ACS)
Subject
Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science
Link
https://pubs.acs.org/doi/pdf/10.1021/la102347b
Reference33 articles.
1. recA protein-promoted DNA strand exchange. Stable complexes of recA protein and single-stranded DNA formed in the presence of ATP and single-stranded DNA binding protein.
2. HOMOLOGOUS PAIRING AND DNA STRAND-EXCHANGE PROTEINS
3. The Bacterial RecA Protein as a Motor Protein
4. Binding of the recA protein of Escherichia coli to single- and double-stranded DNA.
5. The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange.
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