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Structure and specificity of FEN-1 from Methanopyrus kandleri.

Authors :
Shah, Santosh
Dunten, Pete
Stiteler, Amanda
Park, Chad K.
Horton, Nancy C.
Source :
Proteins; Jan2015, Vol. 83 Issue 1, p188-194, 7p
Publication Year :
2015

Abstract

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. Proteins 2015; 83:188-194. © 2014 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
08873585
Volume :
83
Issue :
1
Database :
Complementary Index
Journal :
Proteins
Publication Type :
Academic Journal
Accession number :
100010791
Full Text :
https://doi.org/10.1002/prot.24704