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Structure and specificity of FEN-1 from Methanopyrus kandleri.

ABSTRACT: DNA repair is fundamental to genome stability and is found in all three domains of life. However many archaeal species, such as Methanopyrus kandleri, contain only a subset of the eukaryotic nucleotide excision repair (NER) homologs, and those present often contain significant differences compared to their eukaryotic homologs. To clarify the role of the NER XPG-like protein Mk0566 from M. kandleri, its biochemical activity and three-dimensional structure were investigated. Both were found to be more similar to human FEN-1 than human XPG, suggesting a biological role in replication and long-patch base excision repair rather than in NER.

SUBMITTER: Shah S

PROVIDER: S-EPMC4270939 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

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Structure and specificity of FEN-1 from Methanopyrus kandleri.

Shah Santosh S Dunten Pete P Stiteler Amanda A Park Chad K CK Horton Nancy C NC

Proteins 20141118 1

DNA repair is fundamental to genome stability and is found in all three domains of life. However many archaeal species, such as Methanopyrus kandleri, contain only a subset of the eukaryotic nucleotide excision repair (NER) homologs, and those present often contain significant differences compared to their eukaryotic homologs. To clarify the role of the NER XPG-like protein Mk0566 from M. kandleri, its biochemical activity and three-dimensional structure were investigated. Both were found to be ...[more]

PMID: 25354467

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