Structure and specificity of FEN‐1 from Methanopyrus kandleri

Year: 2014

Type: article

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.

Source: Proteins Structure Function and Bioinformatics

DOI: 10.1002/prot.24704

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

Institutions: University of Arizona, Stanford Synchrotron Radiation Lightsource, Stanford University

Language: English

Topic: DNA Repair Mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: U.S. Department of Energy, National Institutes of Health, Office of Science, National Institute of General Medical Sciences, Basic Energy Sciences, Biological and Environmental Research, SLAC National Accelerator Laboratory

OpenAlex ID: W2141395036