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

Li FAN

PDF(443 KB)
PDF(443 KB)
Front. Biol. ›› 2013, Vol. 8 ›› Issue (4) : 363-368. DOI: 10.1007/s11515-013-1259-x
MINI-REVIEW
MINI-REVIEW

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

Author information +
History +

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.

Keywords

XPB / XPD / TFIIH / helicase / DNA repair / nucleotide excision repair / transcription

Cite this article

Download citation ▾
Li FAN. How two helicases work together within the TFIIH complex, a perspective from structural studies of XPB and XPD helicases. Front Biol, 2013, 8(4): 363‒368 https://doi.org/10.1007/s11515-013-1259-x

References

[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
CrossRef Pubmed Google scholar
[2]
Compe E, Egly J M (2012). TFIIH: when transcription met DNA repair. Nat Rev Mol Cell Biol, 13(6): 343–354
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[7]
Gillet L C J, Schärer O D (2006). Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem Rev, 106(2): 253–276
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[11]
Kuper J, Kisker C (2013). DNA Helicases in NER, BER, and MMR. Adv Exp Med Biol, 767: 203–224
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[14]
Min J H, Pavletich N P (2007). Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature, 449(7162): 570–575
CrossRef Pubmed Google scholar
[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
Pubmed
[16]
Naegeli H, Sugasawa K (2011). The xeroderma pigmentosum pathway: decision tree analysis of DNA quality. DNA Repair (Amst), 10(7): 673–683
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar
[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
CrossRef Pubmed Google scholar

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.

RIGHTS & PERMISSIONS

2014 Higher Education Press and Springer-Verlag Berlin Heidelberg
PDF(443 KB)

Accesses

Citations

Detail

Sections
Recommended

/