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Updated: Apr 21, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
Published on: March 25, 2020
Structure and specificity of FEN-1 from Methanopyrus kandleri
Santosh Shah1, Pete Dunten, Amanda Stiteler
1Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, 85721.
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.
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