Prokaryotic Nucleotide Excision Repair: The UvrABC System

Truglio, James J.; Croteau, Deborah L.; Van Houten, Bennett; Kisker, Caroline

doi:10.1021/cr040471u

Cited by 340DNA Repair MechanismsDNA and Nucleic Acid ChemistryBacterial Genetics and Biotechnology

Prokaryotic Nucleotide Excision Repair: The UvrABC System

Truglio, James J., Croteau, Deborah L., Van Houten, Bennett, Kisker, Caroline·2006·Chemical Reviews

DOI 10.1021/cr040471u

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Abstract

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProkaryotic Nucleotide Excision Repair: The UvrABC SystemJames J. Truglio, Deborah L. Croteau, Bennett Van Houten, and Caroline KiskerView Author Information Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5115, Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, and Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, Versbacher Str. 9, 97078 Würzburg, Germany Cite this: Chem. Rev. 2006, 106, 2, 233–252Publication Date (Web):January 28, 2006Publication History Received13 May 2005Published online28 January 2006Published inissue 1 February 2006https://pubs.acs.org/doi/10.1021/cr040471uhttps://doi.org/10.1021/cr040471uresearch-articleACS PublicationsCopyright © 2006 American Chemical SocietyRequest reuse permissionsArticle Views4157Altmetric-Citations255LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Genetics,Lesions,Monomers,Oligomers,Peptides and proteins Get e-Alerts

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UvrA dimer is the key complex for damage recognition that scans DNA; UvrB catalyzes local dissociation of the DNA helix and provides a scaffold for UvrC.
“The UvrA dimer is the key complex for the damage recognition that scans DNA in the search of damage, while UvrB catalyzes the local dissociation of the DNA helix and provides a scaffold for UvrC protein.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [91]
Detection can also be carried out by transcriptional-repair coupling factor (TRCF, also known as Mfd).
“The detection step can also be carried out by transcriptional-repair coupling factor (TRCF, also known as Mfd).”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [91]
UvrA dimer dissociates from the complex, leaving UvrB bound to DNA waiting for UvrC engagement.
“In the next step, the UvrA dimer dissociates form the complex, leaving UvrB bound to the DNA waiting for UvrC engagement in the repair process.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [91]
Transcription-coupled repair is induced mainly by stalling of RNA polymerase at sites of damage.
“The transcription-coupled repair is induced mainly by the stalling of RNA polymerase at the sites of damage.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [91]
UvrC homolog Cho may be incorporated; Cho cleaves DNA 4 nucleotides farther away than the normal cleavage site on the 3′ side of the lesion.
“Alternatively, UvrC homolog excinuclease (Cho) may be incorporated in the DNA process; however, this nuclease cleaves DNA molecule 4 nucleotides farther away than the normal cleavage site on the 3′ side of the lesion.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [91]

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Caenorhabditis elegans: An Emerging Model in Biomedical and Environmental Toxicology
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Crystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA Binding
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Repair of mitomycin C mono- and interstrand cross-linked DNA adducts by UvrABC: a new model
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Biochemistry of Magnesium
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Escherichia coli ClbS is a colibactin resistance protein
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Surviving the Sun: Repair and bypass of DNA UV lesions
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Cycles of light and dark co‐ordinate reversible colony differentiation in L isteria monocytogenes
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Helicases: An Overview
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Molecular repertoire of Deinococcus radiodurans after 1 year of exposure outside the International Space Station within the Tanpopo mission
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Genomic and proteomic evidences unravel the UV-resistome of the poly-extremophile Acinetobacter sp. Ver3
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Structure determination of DNA methylation lesions N 1 -meA and N 3 -meC in duplex DNA using a cross-linked protein–DNA system
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The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair
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Apigenin Impacts the Growth of the Gut Microbiota and Alters the Gene Expression of Enterococcus
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Envisioning how the prototypic molecular machine TFIIH functions in transcription initiation and DNA repair
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Repair of Hydantoin Lesions and Their Amine Adducts in DNA by Base and Nucleotide Excision Repair
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<i>Starships</i> are active eukaryotic transposable elements mobilized by a new family of tyrosine recombinases
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Nucleotide excision repair genes are expressed at low levels and are not detectably inducible in Caenorhabditis elegans somatic tissues, but their function is required for normal adult life after UVC exposure
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Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes
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Authors: Truglio, J. J., Croteau, D. L., Van Houten, B., & Kisker, C.
Affiliations: National Institutes of Health (US)
Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5115, Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, and Rudolf Virchow Center for Experimental Biomedicine, Institute for Structural Biology, University of Würzburg, Versbacher Str. 9, 97078 Würzburg, Germany
Corresponding author: Kisker, Caroline
ORCID: Croteau, Deborah L.
Kisker, Caroline
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 2006-01-28
Volume: 106
Issue: 2
Pages: 233-252
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr040471u
OpenAlex: W2060583705
Cited by: 340
References: 224
Citations by year: 2026: 11 · 2025: 11 · 2024: 6 · 2023: 18 · 2022: 14 · 2021: 11 · 2020: 14 · 2019: 13 · 2018: 14 · 2017: 20 · 2016: 14 · 2015: 13 · 2014: 22 · 2013: 22 · 2012: 24
FWCI: 1.49
Type: journal article
Language: en
Open access: closed
Locations: Chemical Reviews (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: nucleotide excision repair, uvrA, UvrB, UvrC, DNA damage recognition, DNA damage tolerance, UV-induced DNA damage, translesion synthesis, DNA repair proteins, Escherichia coli, Saccharomyces cerevisiae, DNA glycosylase, DNA helicase
MeSH terms: Animals, Bacterial Proteins, DNA Damage, DNA Repair, DNA, Bacterial, Endodeoxyribonucleases, Humans, Nucleic Acid Conformation, Escherichia coli Proteins

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Prokaryotic Nucleotide Excision Repair: The UvrABC System

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