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Volumn 23, Issue 6, 2006, Pages 801-808

The DNA Repair Helicases XPD and FancJ Have Essential Iron-Sulfur Domains

Author keywords

DNA

Indexed keywords

CHECKPOINT KINASE RAD3; HELICASE; IRON SULFUR PROTEIN;

EID: 33748428875     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.07.019     Document Type: Article
Times cited : (291)

References (37)
  • 2
    • 0037799262 scopus 로고    scopus 로고
    • Structural and functional characterization of the human DNA repair helicase XPD by comparative molecular modeling and site-directed mutagenesis of the bacterial repair protein UvrB
    • Bienstock R.J., Skorvaga M., Mandavilli B.S., and Van Houten B. Structural and functional characterization of the human DNA repair helicase XPD by comparative molecular modeling and site-directed mutagenesis of the bacterial repair protein UvrB. J. Biol. Chem. 278 (2003) 5309-5316
    • (2003) J. Biol. Chem. , vol.278 , pp. 5309-5316
    • Bienstock, R.J.1    Skorvaga, M.2    Mandavilli, B.S.3    Van Houten, B.4
  • 3
    • 0029038131 scopus 로고
    • A regulated MET3-GLC7 gene fusion provides evidence of a mitotic role for Saccharomyces cerevisiae protein phosphatase 1
    • Black S., Andrews P.D., Sneddon A.A., and Stark M.J. A regulated MET3-GLC7 gene fusion provides evidence of a mitotic role for Saccharomyces cerevisiae protein phosphatase 1. Yeast 11 (1995) 747-759
    • (1995) Yeast , vol.11 , pp. 747-759
    • Black, S.1    Andrews, P.D.2    Sneddon, A.A.3    Stark, M.J.4
  • 4
  • 7
    • 1442281478 scopus 로고    scopus 로고
    • The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations
    • Cantor S., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S., and Livingston D.M. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc. Natl. Acad. Sci. USA 101 (2004) 2357-2362
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2357-2362
    • Cantor, S.1    Drapkin, R.2    Zhang, F.3    Lin, Y.4    Han, J.5    Pamidi, S.6    Livingston, D.M.7
  • 12
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz R.D., and Sugino A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74 (1988) 527-534
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 14
    • 0034651623 scopus 로고    scopus 로고
    • Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase
    • Hirota Y., and Lahti J.M. Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase. Nucleic Acids Res. 28 (2000) 917-924
    • (2000) Nucleic Acids Res. , vol.28 , pp. 917-924
    • Hirota, Y.1    Lahti, J.M.2
  • 15
    • 0029151127 scopus 로고
    • Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase
    • Kowal A.T., Werth M.T., Manodori A., Cecchini G., Schroder I., Gunsalus R.P., and Johnson M.K. Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase. Biochemistry 34 (1995) 12284-12293
    • (1995) Biochemistry , vol.34 , pp. 12284-12293
    • Kowal, A.T.1    Werth, M.T.2    Manodori, A.3    Cecchini, G.4    Schroder, I.5    Gunsalus, R.P.6    Johnson, M.K.7
  • 17
    • 0035176067 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases
    • Lehmann A.R. The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases. Genes Dev. 15 (2001) 15-23
    • (2001) Genes Dev. , vol.15 , pp. 15-23
    • Lehmann, A.R.1
  • 20
    • 24944575242 scopus 로고    scopus 로고
    • BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ
    • Litman R., Peng M., Jin Z., Zhang F., Zhang J., Powell S., Andreassen P.R., and Cantor S.B. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell 8 (2005) 255-265
    • (2005) Cancer Cell , vol.8 , pp. 255-265
    • Litman, R.1    Peng, M.2    Jin, Z.3    Zhang, F.4    Zhang, J.5    Powell, S.6    Andreassen, P.R.7    Cantor, S.B.8
  • 21
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine M.S., McKenzie III A., Demarini D.J., Shah N.G., Wach A., Brachat A., Philippsen P., and Pringle J.R. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14 (1998) 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 22
    • 16344377473 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in DNA repair
    • Lukianova O.A., and David S.S. A role for iron-sulfur clusters in DNA repair. Curr. Opin. Chem. Biol. 9 (2005) 145-151
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 145-151
    • Lukianova, O.A.1    David, S.S.2
  • 23
    • 0034777015 scopus 로고    scopus 로고
    • Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration
    • Pieroni L., Khalil L., Charlotte F., Poynard T., Piton A., Hainque B., and Imbert-Bismut F. Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration. Clin. Chem. 47 (2001) 2059-2061
    • (2001) Clin. Chem. , vol.47 , pp. 2059-2061
    • Pieroni, L.1    Khalil, L.2    Charlotte, F.3    Poynard, T.4    Piton, A.5    Hainque, B.6    Imbert-Bismut, F.7
  • 24
    • 27744528421 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake by cells and the use of iron chelators for the treatment of cancer
    • Richardson D.R. Molecular mechanisms of iron uptake by cells and the use of iron chelators for the treatment of cancer. Curr. Med. Chem. 12 (2005) 2711-2729
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2711-2729
    • Richardson, D.R.1
  • 25
    • 0037772376 scopus 로고    scopus 로고
    • An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA
    • Roberts J.A., Bell S.D., and White M.F. An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA. Mol. Microbiol. 48 (2003) 361-371
    • (2003) Mol. Microbiol. , vol.48 , pp. 361-371
    • Roberts, J.A.1    Bell, S.D.2    White, M.F.3
  • 26
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast
    • Sikorski R.S., and Boeke J.D. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194 (1991) 302-318
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 27
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • Singleton M.R., and Wigley D.B. Modularity and specialization in superfamily 1 and 2 helicases. J. Bacteriol. 184 (2002) 1819-1826
    • (2002) J. Bacteriol. , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 28
    • 1642360837 scopus 로고    scopus 로고
    • Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion
    • Skibbens R.V. Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion. Genetics 166 (2004) 33-42
    • (2004) Genetics , vol.166 , pp. 33-42
    • Skibbens, R.V.1
  • 29
    • 0037059785 scopus 로고    scopus 로고
    • The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions
    • Skorvaga M., Theis K., Mandavilli B.S., Kisker C., and Van Houten B. The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J. Biol. Chem. 277 (2002) 1553-1559
    • (2002) J. Biol. Chem. , vol.277 , pp. 1553-1559
    • Skorvaga, M.1    Theis, K.2    Mandavilli, B.S.3    Kisker, C.4    Van Houten, B.5
  • 30
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism
    • Soultanas P., Dillingham M.S., Wiley P., Webb M.R., and Wigley D.B. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 19 (2000) 3799-3810
    • (2000) EMBO J. , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 31
    • 22744445013 scopus 로고    scopus 로고
    • Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase
    • Takahashi T.S., Wigley D.B., and Walter J.C. Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase. Trends Biochem. Sci. 30 (2005) 437-444
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 437-444
    • Takahashi, T.S.1    Wigley, D.B.2    Walter, J.C.3
  • 32
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer M.M., Ahern H., Xing D., Cunningham R.P., and Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14 (1995) 4108-4120
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 34
    • 0033010723 scopus 로고    scopus 로고
    • Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
    • Tirode F., Busso D., Coin F., and Egly J.M. Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Mol. Cell 3 (1999) 87-95
    • (1999) Mol. Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.M.4
  • 36
    • 0041344536 scopus 로고    scopus 로고
    • Characterization of the DNA damage-inducible helicase DinG from Escherichia coli
    • Voloshin O.N., Vanevski F., Khil P.P., and Camerini-Otero R.D. Characterization of the DNA damage-inducible helicase DinG from Escherichia coli. J. Biol. Chem. 278 (2003) 28284-28293
    • (2003) J. Biol. Chem. , vol.278 , pp. 28284-28293
    • Voloshin, O.N.1    Vanevski, F.2    Khil, P.P.3    Camerini-Otero, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.