Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair
Abstract
Global genome nucleotide excision repair (GG-NER) is the main pathway for the removal of bulky lesions from DNA and is characterized by an extraordinarily wide substrate specificity. Remarkably, the efficiency of lesion removal varies dramatically and certain lesions escape repair altogether and are therefore associated with high levels of mutagenicity. Central to the multistep mechanism of damage recognition in NER is the sensing of lesion-induced thermodynamic and structural alterations of DNA by the XPC-RAD23B protein and the verification of the damage by the transcription/repair factor TFIIH. Additional factors contribute to the process: UV-DDB, for the recognition of certain UV-induced lesions in particular in the context of chromatin, while the XPA protein is believed to have a role in damage verification and NER complex assembly. In this paper, we consider the molecular mechanisms that determine repair efficiency in GG-NER based on recent structural, computational, biochemical, cellular and single molecule studies of XPC-RAD23B and its yeast ortholog Rad4. We discuss how the actions of XPC-RAD23B are integrated with those of other NER proteins and, based on recent high-resolution structures of TFIIH, present a structural model of how XPC-RAD23B and TFIIH cooperate in damage recognition and verification.
- Authors:
-
- New York Univ. (NYU), NY (United States)
- Inst. for Basic Science, Ulsan (Korea, Republic of)
- Inst. for Basic Science, Ulsan (Korea, Republic of); Ulsan National Institute of Science and Technology, Ulsan (Korea, Republic of)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)
- Sponsoring Org.:
- USDOE; National Cancer Institute (NCI); National Institutes of Health (NIH); National Science Foundation (NSF); Institute for Basic Science, Daejeon (South Korea)
- OSTI Identifier:
- 1543540
- Grant/Contract Number:
- AC02-05CH11231; IBS-R022-A1-2017; P01-CA092584; R01-CA218315; R01-CA75449; R01-ES025987; R01-ES024050; MCB060037
- Resource Type:
- Accepted Manuscript
- Journal Name:
- DNA Repair
- Additional Journal Information:
- Journal Volume: 71; Journal Issue: C; Journal ID: ISSN 1568-7864
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Genetics and Heredity; Toxicology
Citation Formats
Mu, Hong, Geacintov, Nicholas E., Broyde, Suse, Yeo, Jung-Eun, and Schärer, Orlando D. Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair. United States: N. p., 2018.
Web. doi:10.1016/j.dnarep.2018.08.005.
Mu, Hong, Geacintov, Nicholas E., Broyde, Suse, Yeo, Jung-Eun, & Schärer, Orlando D. Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair. United States. https://doi.org/10.1016/j.dnarep.2018.08.005
Mu, Hong, Geacintov, Nicholas E., Broyde, Suse, Yeo, Jung-Eun, and Schärer, Orlando D. Thu .
"Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair". United States. https://doi.org/10.1016/j.dnarep.2018.08.005. https://www.osti.gov/servlets/purl/1543540.
@article{osti_1543540,
title = {Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair},
author = {Mu, Hong and Geacintov, Nicholas E. and Broyde, Suse and Yeo, Jung-Eun and Schärer, Orlando D.},
abstractNote = {Global genome nucleotide excision repair (GG-NER) is the main pathway for the removal of bulky lesions from DNA and is characterized by an extraordinarily wide substrate specificity. Remarkably, the efficiency of lesion removal varies dramatically and certain lesions escape repair altogether and are therefore associated with high levels of mutagenicity. Central to the multistep mechanism of damage recognition in NER is the sensing of lesion-induced thermodynamic and structural alterations of DNA by the XPC-RAD23B protein and the verification of the damage by the transcription/repair factor TFIIH. Additional factors contribute to the process: UV-DDB, for the recognition of certain UV-induced lesions in particular in the context of chromatin, while the XPA protein is believed to have a role in damage verification and NER complex assembly. In this paper, we consider the molecular mechanisms that determine repair efficiency in GG-NER based on recent structural, computational, biochemical, cellular and single molecule studies of XPC-RAD23B and its yeast ortholog Rad4. We discuss how the actions of XPC-RAD23B are integrated with those of other NER proteins and, based on recent high-resolution structures of TFIIH, present a structural model of how XPC-RAD23B and TFIIH cooperate in damage recognition and verification.},
doi = {10.1016/j.dnarep.2018.08.005},
journal = {DNA Repair},
number = C,
volume = 71,
place = {United States},
year = {Thu Aug 23 00:00:00 EDT 2018},
month = {Thu Aug 23 00:00:00 EDT 2018}
}
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