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Molecular and Cellular Biology, December 2006, p. 8868-8879, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00695-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Recruitment of the Nucleotide Excision Repair Endonuclease XPG to Sites of UV-Induced DNA Damage Depends on Functional TFIIH{triangledown}

Angelika Zotter,1,{dagger} Martijn S. Luijsterburg,2,{dagger} Daniël O. Warmerdam,2 Shehu Ibrahim,1,3 Alex Nigg,3 Wiggert A. van Cappellen,4 Jan H. J. Hoeijmakers,1 Roel van Driel,2 Wim Vermeulen,1* and Adriaan B. Houtsmuller3

Department of Cell Biology and Genetics, Erasmus MC Rotterdam, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands,1 Swammerdam Institute for Life Sciences, BioCentrum Amsterdam, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands,2 Department of Pathology, Josephine Nefkens Institute, Erasmus MC Rotterdam, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands,3 Department of Endocrinology and Reproduction, Erasmus MC Rotterdam, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands4

Received 21 April 2006/ Returned for modification 1 September 2006/ Accepted 14 September 2006

The structure-specific endonuclease XPG is an indispensable core protein of the nucleotide excision repair (NER) machinery. XPG cleaves the DNA strand at the 3' side of the DNA damage. XPG binding stabilizes the NER preincision complex and is essential for the 5' incision by the ERCC1/XPF endonuclease. We have studied the dynamic role of XPG in its different cellular functions in living cells. We have created mammalian cell lines that lack functional endogenous XPG and stably express enhanced green fluorescent protein (eGFP)-tagged XPG. Life cell imaging shows that in undamaged cells XPG-eGFP is uniformly distributed throughout the cell nucleus, diffuses freely, and is not stably associated with other nuclear proteins. XPG is recruited to UV-damaged DNA with a half-life of 200 s and is bound for 4 min in NER complexes. Recruitment requires functional TFIIH, although some TFIIH mutants allow slow XPG recruitment. Remarkably, binding of XPG to damaged DNA does not require the DDB2 protein, which is thought to enhance damage recognition by NER factor XPC. Together, our data present a comprehensive view of the in vivo behavior of a protein that is involved in a complex chromatin-associated process.

* Corresponding author. Mailing address: Department of Cell Biology and Genetics, Erasmus Medical Center, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands. Phone: (31) 10 4087194. Fax: (31) 10 4089468. E-mail: w.vermeulen{at}erasmusmc.nl.

{triangledown} Published ahead of print on 25 September 2006.

{dagger} A.Z. and M.S.L. contributed equally to this work.

Molecular and Cellular Biology, December 2006, p. 8868-8879, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00695-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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