Kinetic gating mechanism of DNA damage recognition by Rad4/XPC
Abstract
The xeroderma pigmentosum C (XPC) complex initiates nucleotide excision repair by recognizing DNA lesions before recruiting downstream factors. How XPC detects structurally diverse lesions embedded within normal DNA is unknown. Here we present a crystal structure that captures the yeast XPC orthologue (Rad4) on a single register of undamaged DNA. The structure shows that a disulphide-tethered Rad4 flips out normal nucleotides and adopts a conformation similar to that seen with damaged DNA. Contrary to many DNA repair enzymes that can directly reject non-target sites as structural misfits, our results suggest that Rad4/XPC uses a kinetic gating mechanism whereby lesion selectivity arises from the kinetic competition between DNA opening and the residence time of Rad4/XPC per site. This mechanism is further supported by measurements of Rad4-induced lesion-opening times using temperature-jump perturbation spectroscopy. Lastly, kinetic gating may be a general mechanism used by site-specific DNA-binding proteins to minimize time-consuming interrogations of non-target sites.
- Authors:
-
- Univ. of Illinois at Chicago, Chicago, IL (United States)
- The Univ. of Chicago, Chicago, IL (United States)
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Univ. of Pittsburgh, Pittsburgh, PA (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1225230
- Alternate Identifier(s):
- OSTI ID: 1253601
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 6; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; biological sciences; biophysics; biochemistry
Citation Formats
Chen, Xuejing, Velmurugu, Yogambigai, Zheng, Guanqun, Park, Beomseok, Shim, Yoonjung, Kim, Youngchang, Liu, Lili, Van Houten, Bennett, He, Chuan, Ansari, Anjum, and Min, Jung -Hyun. Kinetic gating mechanism of DNA damage recognition by Rad4/XPC. United States: N. p., 2015.
Web. doi:10.1038/ncomms6849.
Chen, Xuejing, Velmurugu, Yogambigai, Zheng, Guanqun, Park, Beomseok, Shim, Yoonjung, Kim, Youngchang, Liu, Lili, Van Houten, Bennett, He, Chuan, Ansari, Anjum, & Min, Jung -Hyun. Kinetic gating mechanism of DNA damage recognition by Rad4/XPC. United States. https://doi.org/10.1038/ncomms6849
Chen, Xuejing, Velmurugu, Yogambigai, Zheng, Guanqun, Park, Beomseok, Shim, Yoonjung, Kim, Youngchang, Liu, Lili, Van Houten, Bennett, He, Chuan, Ansari, Anjum, and Min, Jung -Hyun. Tue .
"Kinetic gating mechanism of DNA damage recognition by Rad4/XPC". United States. https://doi.org/10.1038/ncomms6849. https://www.osti.gov/servlets/purl/1225230.
@article{osti_1225230,
title = {Kinetic gating mechanism of DNA damage recognition by Rad4/XPC},
author = {Chen, Xuejing and Velmurugu, Yogambigai and Zheng, Guanqun and Park, Beomseok and Shim, Yoonjung and Kim, Youngchang and Liu, Lili and Van Houten, Bennett and He, Chuan and Ansari, Anjum and Min, Jung -Hyun},
abstractNote = {The xeroderma pigmentosum C (XPC) complex initiates nucleotide excision repair by recognizing DNA lesions before recruiting downstream factors. How XPC detects structurally diverse lesions embedded within normal DNA is unknown. Here we present a crystal structure that captures the yeast XPC orthologue (Rad4) on a single register of undamaged DNA. The structure shows that a disulphide-tethered Rad4 flips out normal nucleotides and adopts a conformation similar to that seen with damaged DNA. Contrary to many DNA repair enzymes that can directly reject non-target sites as structural misfits, our results suggest that Rad4/XPC uses a kinetic gating mechanism whereby lesion selectivity arises from the kinetic competition between DNA opening and the residence time of Rad4/XPC per site. This mechanism is further supported by measurements of Rad4-induced lesion-opening times using temperature-jump perturbation spectroscopy. Lastly, kinetic gating may be a general mechanism used by site-specific DNA-binding proteins to minimize time-consuming interrogations of non-target sites.},
doi = {10.1038/ncomms6849},
journal = {Nature Communications},
number = ,
volume = 6,
place = {United States},
year = {Tue Jan 06 00:00:00 EST 2015},
month = {Tue Jan 06 00:00:00 EST 2015}
}
Web of Science
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