MINI-REVIEW

How two helicases work together within the TFIIH complex, a perspective from structural studies of XPB and XPD helicases

  • Li FAN
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  • Department of Biochemistry, University of California at Riverside, Riverside, CA 92521, USA

Received date: 14 Nov 2012

Accepted date: 15 Feb 2013

Published date: 01 Aug 2013

Copyright

2014 Higher Education Press and Springer-Verlag Berlin Heidelberg

Abstract

Xeroderma pigmentosum group B (XPB) and D (XPD) are two DNA helicases inside the transcription factor TFIIH complex required for both transcription and DNA repair. The importance of these helicases is underscored by the fact that mutations of XPB and XPD cause diseases with extremely high sensitivity to UV-light and high risk of cancer, premature aging, etc. This mini-review focuses on recent developments in both structural and functional characterization of these XP helicases to illustrate their distinguished biological roles within the architectural restriction of the TFIIH complex. In particular, molecular mechanisms of DNA unwinding by these helicases for promoter opening during transcription initiation and bubble-creation around the lesion during DNA repair are described based on the integration of the crystal structures of XPB and XPD helicases into the architecture of the TFIIH complex.

Cite this article

Li FAN . How two helicases work together within the TFIIH complex, a perspective from structural studies of XPB and XPD helicases[J]. Frontiers in Biology, 2013 , 8(4) : 363 -368 . DOI: 10.1007/s11515-013-1259-x

Acknowledgements

I am grateful to John Tainer, in whose laboratory at The Scripps Research Institute I have determined the structures of AfXPB and SaXPD. I would like also to thank the Department of Biochemistry and CNAS (particularly Thomas Baldwin, Richard Debus and Russ Hille) at University of California-Riverside for many supports in establishing my own laboratory. This project has been supported by grants from UCR and the Hellman Fellowship. I apologize to people whose research activities have contributed to our understandings about the topic but are not cited here due to space limitation.
1
Chang W H, Kornberg R D (2000). Electron crystal structure of the transcription factor and DNA repair complex, core TFIIH. Cell, 102(5): 609–613

DOI PMID

2
Compe E, Egly J M (2012). TFIIH: when transcription met DNA repair. Nat Rev Mol Cell Biol, 13(6): 343–354

DOI PMID

3
Egly J M, Coin F (2011). A history of TFIIH: two decades of molecular biology on a pivotal transcription/repair factor. DNA Repair (Amst), 10(7): 714–721

DOI PMID

4
Fan L, Arvai A S, Cooper P K, Iwai S, Hanaoka F, Tainer J A (2006). Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol Cell, 22(1): 27–37

DOI PMID

5
Fan L, Fuss J O, Cheng Q J, Arvai A S, Hammel M, Roberts V A, Cooper P K, Tainer J A (2008). XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell, 133(5): 789–800

DOI PMID

6
Fuss J O, Tainer J A (2011). XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase. DNA Repair (Amst), 10(7): 697–713

DOI PMID

7
Gillet L C J, Schärer O D (2006). Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem Rev, 106(2): 253–276

DOI PMID

8
Hanawalt P C, Spivak G (2008). Transcription-coupled DNA repair: two decades of progress and surprises. Nat Rev Mol Cell Biol, 9(12): 958–970

DOI PMID

9
Hilario E, Li Y, Nobumori Y, Liu X, Fan L (2013). Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE. Acta Crystallogr D Biol Crystallogr, 69(Pt 2): 237–246

DOI PMID

10
Kim T K, Ebright R H, Reinberg D (2000). Mechanism of ATP-dependent promoter melting by transcription factor IIH. Science, 288(5470): 1418–1422

DOI PMID

11
Kuper J, Kisker C (2013). DNA Helicases in NER, BER, and MMR. Adv Exp Med Biol, 767: 203–224

DOI PMID

12
Liu H, Rudolf J, Johnson K A, McMahon S A, Oke M, Carter L, McRobbie A M, Brown S E, Naismith J H, White M F (2008). Structure of the DNA repair helicase XPD. Cell, 133(5): 801–812

DOI PMID

13
Mathieu N, Kaczmarek N, Naegeli H (2010). Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase. Proc Natl Acad Sci U S A, 107(41): 17545–17550

DOI PMID

14
Min J H, Pavletich N P (2007). Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature, 449(7162): 570–575

DOI PMID

15
Naegeli H, Modrich P, Friedberg E C (1993). The DNA helicase activities of Rad3 protein of Saccharomyces cerevisiae and helicase II of Escherichia coli are differentially inhibited by covalent and noncovalent DNA modifications. J Biol Chem, 268(14): 10386–10392

PMID

16
Naegeli H, Sugasawa K (2011). The xeroderma pigmentosum pathway: decision tree analysis of DNA quality. DNA Repair (Amst), 10(7): 673–683

DOI PMID

17
Oksenych V, Bernardes de Jesus B, Zhovmer A, Egly J M, Coin F (2009). Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J, 28(19): 2971–2980

DOI PMID

18
Roth H M, Römer J, Grundler V, Van Houten B, Kisker C, Tessmer I (2012). XPB helicase regulates DNA incision by the Thermoplasma acidophilum endonuclease Bax1. DNA Repair (Amst), 11(3): 286–293

DOI PMID

19
Rouillon C, White M F (2010). The XBP-Bax1 helicase-nuclease complex unwinds and cleaves DNA: implications for eukaryal and archaeal nucleotide excision repair. J Biol Chem, 285(14): 11013–11022

DOI PMID

20
Sarker A H, Tsutakawa S E, Kostek S, Ng C, Shin D S, Peris M, Campeau E, Tainer J A, Nogales E, Cooper P K (2005). Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome. Mol Cell, 20(2): 187–198

DOI PMID

21
Schultz P, Fribourg S, Poterszman A, Mallouh V, Moras D, Egly J M (2000). Molecular structure of human TFIIH. Cell, 102(5): 599–607

DOI PMID

21a
Singleton M R, Dillingham M S, Wigley D B (2007). Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem, 76: 23–50

22
Wolski S C, Kuper J, Hänzelmann P, Truglio J J, Croteau D L, Van Houten B, Kisker C (2008). Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLoS Biol, 6(6): e149

DOI PMID

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