Structure and specificity of FEN-1 from Methanopyrus kandleri

Santosh Shah; Pete Dunten; Amanda Stiteler; Chad K. Park; Nancy C. Horton

doi:10.1002/prot.24704

Structure and specificity of FEN-1 from Methanopyrus kandleri

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

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	188-194
Number of pages	7
Journal	Proteins: Structure, Function and Bioinformatics
Volume	83
Issue number	1
DOIs	https://doi.org/10.1002/prot.24704
State	Published - Jan 2015

Keywords

DNA nuclease
Nucleotide excision repair
Protein-DNA complex

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.24704

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title = "Structure and specificity of FEN-1 from Methanopyrus kandleri",

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.",

keywords = "DNA nuclease, Nucleotide excision repair, Protein-DNA complex",

author = "Santosh Shah and Pete Dunten and Amanda Stiteler and Park, {Chad K.} and Horton, {Nancy C.}",

note = "Publisher Copyright: {\textcopyright} 2014 Wiley Periodicals, Inc.",

year = "2015",

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T1 - Structure and specificity of FEN-1 from Methanopyrus kandleri

AU - Shah, Santosh

AU - Dunten, Pete

AU - Stiteler, Amanda

AU - Park, Chad K.

AU - Horton, Nancy C.

PY - 2015/1

Y1 - 2015/1

N2 - 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.

AB - 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.

KW - DNA nuclease

KW - Nucleotide excision repair

KW - Protein-DNA complex

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JO - Proteins: Structure, Function and Bioinformatics

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Structure and specificity of FEN-1 from Methanopyrus kandleri

Abstract

Keywords

ASJC Scopus subject areas

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Methanopyrus Kandleri FEN-1 nuclease

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Structure and specificity of FEN-1 from Methanopyrus kandleri

Abstract

Keywords

ASJC Scopus subject areas

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Methanopyrus Kandleri FEN-1 nuclease

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