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. 1982 May;79(10):3171–3175. doi: 10.1073/pnas.79.10.3171

Recombinational bypass of pyrimidine dimers promoted by the recA protein of Escherichia coli.

Z Livneh, I R Lehman
PMCID: PMC346376  PMID: 6954468

Abstract

recA protein, in the presence of single-stranded DNA binding protein and ATP, promotes the complete exchange of strands between circular single-stranded DNA containing pyrimidine dimers and a homologous linear duplex, converting the pyrimidine dimer-containing single-stranded DNA to a circular duplex. Bypass of a pyrimidine dimer during the branch-migration phase of the reaction requires approximately 20 seconds, a rate 1/50th of that in the absence of the dimer. The circular duplex product is specifically incised by the pyrimidine dimer-specific T4 endonuclease V, and the resulting 3' hydroxyl termini can serve as primers for deoxynucleotide polymerization by DNA polymerase I. These findings indicate that recA protein serves a direct role in recombinational repair and demonstrate that the pyrimidine dimers that have been bypassed can be processed by enzymes of the excision-repair pathway.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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