4wa8

Publication Abstract from PubMed

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) homologues, and those present often contain significant differences compared to their eukaryotic homologues. 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. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.

Structure and Specificity of FEN-1 from Methanopyrus kandleri.,Shah S, Dunten P, Stiteler A, Park CK, Horton NC Proteins. 2014 Oct 30. doi: 10.1002/prot.24704. PMID:25354467^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.