XPB

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Excision repair cross-complementing rodent repair deficiency, complementation group 3
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ERCC3 ; BTF2; GTF2H; RAD25; TFIIH; XPB
External IDs OMIM133510 MGI95414 HomoloGene96 GeneCards: ERCC3 Gene
EC number 3.6.4.12
RNA expression pattern
PBB GE ERCC3 202176 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2071 13872
Ensembl ENSG00000163161 ENSMUSG00000024382
UniProt P19447 P49135
RefSeq (mRNA) NM_000122 NM_133658
RefSeq (protein) NP_000113 NP_598419
Location (UCSC) Chr 2:
128.01 – 128.05 Mb
Chr 18:
32.24 – 32.27 Mb
PubMed search [1] [2]

XPB (Xeroderma Pigmentosum B) is an ATP dependent human DNA helicase that is a part of the TFIIH transcription factor complex.

Structure[edit]

The 3D structure of the archeael homologue of XPB has been solved by X-ray crystallography by Dr. John Tainer and his group at The Scripps Research Institute.[1]

Function[edit]

XPB plays a significant role in normal basal transcription, transcription coupled repair (TCR), and nucleotide excision repair (NER). Purified XPB has been shown to unwind DNA with 3’-5’polarity.

Disorders[edit]

Mutations in XPB and other related complementation groups, XPA-XPG, leads to a number of genetic disorders such as Xeroderma Pigmentosum, Cockayne's syndrome, and Trichothiodystrophy.

Interactions[edit]

XPB has been shown to interact with XPC,[2] BCR gene,[3] ERCC2,[4][5][6][7] P53,[8] GTF2H2,[4][5] GTF2H1,[4][5][9] GTF2H5,[4] Cyclin-dependent kinase 7,[4][9][10] PSMC5[11] and GTF2H4.[4][5]

See also[edit]

References[edit]

  1. ^ Fan L, Arvai A, Cooper P, Iwai S, Hanaoka F, Tainer J (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:10.1016/j.molcel.2006.02.017. PMID 16600867. 
  2. ^ Yokoi, M; Masutani C, Maekawa T, Sugasawa K, Ohkuma Y, Hanaoka F (March 2000). "The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA". J. Biol. Chem. (UNITED STATES) 275 (13): 9870–5. doi:10.1074/jbc.275.13.9870. ISSN 0021-9258. PMID 10734143. 
  3. ^ Takeda, N; Shibuya M, Maru Y (January 1999). "The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (1): 203–7. doi:10.1073/pnas.96.1.203. ISSN 0027-8424. PMC 15117. PMID 9874796. 
  4. ^ a b c d e f Giglia-Mari, Giuseppina; Coin Frederic, Ranish Jeffrey A, Hoogstraten Deborah, Theil Arjan, Wijgers Nils, Jaspers Nicolaas G J, Raams Anja, Argentini Manuela, van der Spek P J, Botta Elena, Stefanini Miria, Egly Jean-Marc, Aebersold Ruedi, Hoeijmakers Jan H J, Vermeulen Wim (July 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nat. Genet. (United States) 36 (7): 714–9. doi:10.1038/ng1387. ISSN 1061-4036. PMID 15220921. 
  5. ^ a b c d Marinoni, J C; Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez D M, Hoeijmakers J H, Egly J M (March 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. (ENGLAND) 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. ISSN 0261-4189. PMC 1169708. PMID 9118947. 
  6. ^ Drapkin, R; Reardon J T, Ansari A, Huang J C, Zawel L, Ahn K, Sancar A, Reinberg D (April 1994). "Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II". Nature (ENGLAND) 368 (6473): 769–72. doi:10.1038/368769a0. ISSN 0028-0836. PMID 8152490. 
  7. ^ Iyer, N; Reagan M S, Wu K J, Canagarajah B, Friedberg E C (February 1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein". Biochemistry (UNITED STATES) 35 (7): 2157–67. doi:10.1021/bi9524124. ISSN 0006-2960. PMID 8652557. 
  8. ^ Wang, X W; Yeh H, Schaeffer L, Roy R, Moncollin V, Egly J M, Wang Z, Freidberg E C, Evans M K, Taffe B G (June 1995). "p53 modulation of TFIIH-associated nucleotide excision repair activity". Nat. Genet. (UNITED STATES) 10 (2): 188–95. doi:10.1038/ng0695-188. ISSN 1061-4036. PMID 7663514. 
  9. ^ a b Rossignol, M; Kolb-Cheynel I, Egly J M (April 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". EMBO J. (ENGLAND) 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. ISSN 0261-4189. PMC 1169767. PMID 9130708. 
  10. ^ Yee, A; Nichols M A, Wu L, Hall F L, Kobayashi R, Xiong Y (December 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Res. (UNITED STATES) 55 (24): 6058–62. ISSN 0008-5472. PMID 8521393. 
  11. ^ Weeda, G; Rossignol M, Fraser R A, Winkler G S, Vermeulen W, van 't Veer L J, Ma L, Hoeijmakers J H, Egly J M (June 1997). "The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor". Nucleic Acids Res. (ENGLAND) 25 (12): 2274–83. doi:10.1093/nar/25.12.2274. ISSN 0305-1048. PMC 146752. PMID 9173976. 

Further reading[edit]

External links[edit]