Structure and specificity of FEN-1 from Methanopyrus kandleri

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

doi:10.1002/prot.24704

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

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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.

Authors:

Shah, Santosh ^[1]; Dunten, Pete ^[2]; Stiteler, Amanda ^[1]; Park, Chad K. ^[1]; Horton, Nancy C. ^[1]

Univ. of Arizona, Tucson, AZ (United States). Dept. of Chemistry and Biochemistry
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Publication Date:: Tue Nov 18 00:00:00 EST 2014

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); USDOE Office of Science (SC), Biological and Environmental Research (BER)

OSTI Identifier:: 1291006

Alternate Identifier(s):: OSTI ID: 1400880

Grant/Contract Number:: AC02-76SF00515; P41GM103393; S10OD013237

Resource Type:: Accepted Manuscript

Journal Name:: Proteins

Additional Journal Information:: Journal Volume: 83; Journal Issue: 1; Journal ID: ISSN 0887-3585

Publisher:: Wiley

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; protein-DNA complex; DNA nuclease; nucleotide excision repair

Citation Formats


                    Shah, Santosh, Dunten, Pete, Stiteler, Amanda, Park, Chad K., and Horton, Nancy C. Structure and specificity of FEN-1 from Methanopyrus kandleri.  United States: N. p., 2014. 
Web.  doi:10.1002/prot.24704.

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                    Shah, Santosh, Dunten, Pete, Stiteler, Amanda, Park, Chad K., & Horton, Nancy C. Structure and specificity of FEN-1 from Methanopyrus kandleri.  United States.  https://doi.org/10.1002/prot.24704

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                    Shah, Santosh, Dunten, Pete, Stiteler, Amanda, Park, Chad K., and Horton, Nancy C. Tue .  
"Structure and specificity of FEN-1 from Methanopyrus kandleri".  United States.  https://doi.org/10.1002/prot.24704.  https://www.osti.gov/servlets/purl/1291006.

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@article{osti_1291006,

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

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

  abstractNote = {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.},

  doi          = {10.1002/prot.24704},

  journal      = {Proteins},

  number       = 1,

  volume       = 83,

  place        = {United States},

  year         = {Tue Nov 18 00:00:00 EST 2014},

  month        = {Tue Nov 18 00:00:00 EST 2014}

}

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