XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair

HUMANS with a defect in the XPG protein suffer from xeroderma pigmentosum (XP) resulting from an inability to perform DNA nucleotide excision repair properly 1–4 . Here we show that XPG makes a structure-specific endonucleolytic incision in a synthetic DNA substrate containing a duplex region and si...

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Published in:Nature (London) 1994-09, Vol.371 (6496), p.432-435
Main Authors: O'Donovan, Anne, Davies, Adelina A, Moggs, Jonathan G, West, Stephen C, Wood, Richard D
Format: Article
Language:English
Subjects:
3'-terminus
Base Sequence
Biological and medical sciences
Cellular biology
deoxyribonuclease
Deoxyribonucleic acid
DNA
DNA Repair
DNA, Single-Stranded - metabolism
DNA-Binding Proteins
Endodeoxyribonucleases
Endonucleases - metabolism
Escherichia coli
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
HeLa Cells
Humanities and Social Sciences
Humans
letter
man
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
multidisciplinary
Mutagenesis. Repair
Nucleic Acid Conformation
nucleotide excision repair
Proteins
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae Proteins
Science
Science (multidisciplinary)
Xeroderma Pigmentosum - enzymology
Xeroderma Pigmentosum - genetics
XPG protein
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description HUMANS with a defect in the XPG protein suffer from xeroderma pigmentosum (XP) resulting from an inability to perform DNA nucleotide excision repair properly 1–4 . Here we show that XPG makes a structure-specific endonucleolytic incision in a synthetic DNA substrate containing a duplex region and single-stranded arms. One strand of the duplex is cleaved at the border with single-stranded DNA. A cut with the same polarity is also made in a bubble structure, at the 3′ side of the centrally unpaired region. Normal cell extracts introduce a nick 3′ to a platinum – DNA lesion, but an XP-G cell extract is defective in making this incision. These data show that XPG has a direct role in making one of the incisions required to excise a damaged oligonucleotide, by cleaving 3' to DNA damage during nucleotide excision repair.
doi_str_mv 10.1038/371432a0
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subjects 3'-terminus
Base Sequence
Biological and medical sciences
Cellular biology
deoxyribonuclease
Deoxyribonucleic acid
DNA
DNA Repair
DNA, Single-Stranded - metabolism
DNA-Binding Proteins
Endodeoxyribonucleases
Endonucleases - metabolism
Escherichia coli
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
HeLa Cells
Humanities and Social Sciences
Humans
letter
man
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
multidisciplinary
Mutagenesis. Repair
Nucleic Acid Conformation
nucleotide excision repair
Proteins
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae Proteins
Science
Science (multidisciplinary)
Xeroderma Pigmentosum - enzymology
Xeroderma Pigmentosum - genetics
XPG protein
title XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair
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