A Structural Model for the Damage-sensing Complex in Bacterial Nucleotide Excision Repair*

AUTOR(ES)

Pakotiprapha, Danaya

FONTE

American Society for Biochemistry and Molecular Biology

RESUMO

Nucleotide excision repair is distinguished from other DNA repair pathways by its ability to process a wide range of structurally unrelated DNA lesions. In bacteria, damage recognition is achieved by the UvrA·UvrB ensemble. Here, we report the structure of the complex between the interaction domains of UvrA and UvrB. These domains are necessary and sufficient for full-length UvrA and UvrB to associate and thereby form the DNA damage-sensing complex of bacterial nucleotide excision repair. The crystal structure and accompanying biochemical analyses suggest a model for the complete damage-sensing complex.

Documentos Relacionados

• Bax1 Is a Novel Endonuclease: IMPLICATIONS FOR ARCHAEAL NUCLEOTIDE EXCISION REPAIR*
• A p53-independent damage-sensing mechanism that functions as a checkpoint at the G1/S transition in Chinese hamster ovary cells
• A multistep damage recognition mechanism for global genomic nucleotide excision repair
• Overlapping Specificities of Base Excision Repair, Nucleotide Excision Repair, Recombination, and Translesion Synthesis Pathways for DNA Base Damage in Saccharomyces cerevisiae
• p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage