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. Kinetic gating may be a general mechanism used by site-specific DNA-binding proteins to minimize time-consuming interrogations of non-target sites.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Chen X,Velmurugu Y,Zheng G,Park B,Shim Y,Kim Y,Liu L,Van Houten B,He C,Ansari A,Min JHdoi
10.1038/ncomms6849subject
Has Abstractpub_date
2015-01-06 00:00:00pages
5849issn
2041-1723pii
ncomms6849journal_volume
6pub_type
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