Structure and specificity of FEN-1 from Methanopyrus kandleri

Santosh Shah, Pete Dunten, Amanda Stiteler, Chad K. Park, Nancy C Horton

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)188-194
Number of pages7
JournalProteins: Structure, Function and Genetics
Volume83
Issue number1
DOIs
StatePublished - 2015

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Flap Endonucleases
DNA Repair
Repair
Nucleotides
Genomic Instability
Genes
DNA
Proteins

Keywords

  • DNA nuclease
  • Nucleotide excision repair
  • Protein-DNA complex

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Cite this

Structure and specificity of FEN-1 from Methanopyrus kandleri. / Shah, Santosh; Dunten, Pete; Stiteler, Amanda; Park, Chad K.; Horton, Nancy C.

In: Proteins: Structure, Function and Genetics, Vol. 83, No. 1, 2015, p. 188-194.

Research output: Contribution to journalArticle

Shah, Santosh ; Dunten, Pete ; Stiteler, Amanda ; Park, Chad K. ; Horton, Nancy C. / Structure and specificity of FEN-1 from Methanopyrus kandleri. In: Proteins: Structure, Function and Genetics. 2015 ; Vol. 83, No. 1. pp. 188-194.
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