Crystal structure of the Escherichia coli dcm very-short-patch DNA repair endonuclease bound to its reaction product-site in a DNA superhelix
AUTOR(ES)
Bunting, Karen A.
FONTE
Oxford University Press
RESUMO
Very-short-patch repair (Vsr) enzymes occur in a variety of bacteria, where they initiate nucleotide excision repair of G:T mismatches arising by deamination of 5-methyl-cytosines in specific regulatory sequences. We have now determined the structure of the archetypal dcm-Vsr endonuclease from Escherichia coli bound to the cleaved authentic hemi-deaminated/hemi-methylated dcm sequence 5′-C-OH-3′ 5′-p-T-p-A-p-G-p-G-3′/3′-G-p-G-p-T-pMe5C-p-C formed by self-assembly of a 12mer oligonucleotide into a continuous nicked DNA superhelix. The structure reveals the presence of a Hoogsteen base pair within the deaminated recognition sequence and the substantial distortions of the DNA that accompany Vsr binding to product sites.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=152875Documentos Relacionados
- Very-Short-Patch Repair in Escherichia coli Requires the dam Adenine Methylase
- Interaction of MutS and Vsr: Some Dominant-Negative mutS Mutations That Disable Methyladenine-Directed Mismatch Repair Are Active in Very-Short-Patch Repair
- A gene required for very short patch repair in Escherichia coli is adjacent to the DNA cytosine methylase gene.
- The structural basis of damaged DNA recognition and endonucleolytic cleavage for very short patch repair endonuclease
- Very short patch mismatch repair activity associated with gene dcm is not conferred by a plasmid coding for EcoRII methylase.