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Title: Structure and specificity of FEN-1 from Methanopyrus kandleri

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. Ultimately, we found both 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.
Authors:
 [1] ;  [2] ;  [1] ;  [1] ;  [1]
  1. Univ. of Arizona, Tucson, AZ (United States). Dept. of Chemistry and Biochemistry
  2. SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Publication Date:
OSTI Identifier:
1291006
Grant/Contract Number:
AC02-76SF00515; P41GM103393; S10OD013237
Type:
Accepted Manuscript
Journal Name:
Proteins
Additional Journal Information:
Journal Volume: 83; Journal Issue: 1; Journal ID: ISSN 0887-3585
Publisher:
Wiley
Research Org:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES protein-DNA complex; DNA nuclease; nucleotide excision repair