Recombinational Bypass of Pyrimidine Dimers Promoted by the RecA Protein of Escherichia Coli

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1982 May 1

PMID 6954468

Citations 18

Authors

Z Livneh

I R Lehman

Affiliations

Soon will be listed here.

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.

Citing Articles

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Gene 4 helicase of bacteriophage T7 mediates strand transfer through pyrimidine dimers, mismatches, and nonhomologous regions.

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Inducibility of the SOS response in a recA730 or recA441 strain is restored by transformation with a new recA allele.

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Biochemistry of homologous recombination in Escherichia coli.

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