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Volumn 24, Issue , 2014, Pages 37-45

Yeast DNA ligase IV mutations reveal a nonhomologous end joining function of BRCT1 distinct from XRCC4/Lif1 binding

Author keywords

BRCT domain; DNA ligase IV; Double strand break; Nonhomologous end joining; Separation of function

Indexed keywords

BRCA1 C TERMINAL PROTEIN; LIF1 PROTEIN; PEPTIDES AND PROTEINS; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG; XRCC4 PROTEIN; DNA BINDING PROTEIN; DNA LIGASE; DNA LIGASE (ATP); LIF1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; XRCC4 PROTEIN, HUMAN;

EID: 84919730062     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.10.003     Document Type: Article
Times cited : (6)

References (51)
  • 3
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber M.R. The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway. Annu. Rev. Biochem. 2010, 79:181-211.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 4
    • 50649116450 scopus 로고    scopus 로고
    • Eukaryotic DNA ligases: structural and functional insights
    • Ellenberger T., Tomkinson A.E. Eukaryotic DNA ligases: structural and functional insights. Annu. Rev. Biochem. 2008, 77:313-338.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 313-338
    • Ellenberger, T.1    Tomkinson, A.E.2
  • 7
    • 0032537803 scopus 로고    scopus 로고
    • DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains
    • Grawunder U., Zimmer D., Leiber M.R. DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. Curr. Biol. 1998, 8:873-876.
    • (1998) Curr. Biol. , vol.8 , pp. 873-876
    • Grawunder, U.1    Zimmer, D.2    Leiber, M.R.3
  • 8
    • 0034628617 scopus 로고    scopus 로고
    • Lif1p targets the DNA ligase Lig4p to sites of DNA double-strand breaks
    • Teo S.H., Jackson S.P. Lif1p targets the DNA ligase Lig4p to sites of DNA double-strand breaks. Curr. Biol. 2000, 10:165-168.
    • (2000) Curr. Biol. , vol.10 , pp. 165-168
    • Teo, S.H.1    Jackson, S.P.2
  • 9
    • 78149459696 scopus 로고    scopus 로고
    • XLF regulates filament architecture of the XRCC4.ligase IV complex
    • Hammel M., Yu Y., Fang S., Lees-Miller S.P., Tainer J.A. XLF regulates filament architecture of the XRCC4.ligase IV complex. Structure 2010, 18:1431-1442.
    • (2010) Structure , vol.18 , pp. 1431-1442
    • Hammel, M.1    Yu, Y.2    Fang, S.3    Lees-Miller, S.P.4    Tainer, J.A.5
  • 12
    • 84874878472 scopus 로고    scopus 로고
    • XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair
    • Mahaney B.L., Hammel M., Meek K., Tainer J.A., Lees-Miller S.P. XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair. Biochim. Biol. Cell. 2013, 91:31-41.
    • (2013) Biochim. Biol. Cell. , vol.91 , pp. 31-41
    • Mahaney, B.L.1    Hammel, M.2    Meek, K.3    Tainer, J.A.4    Lees-Miller, S.P.5
  • 15
    • 0032971199 scopus 로고    scopus 로고
    • Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4
    • Bryans M., Valenzano M.C., Stamato T.D. Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4. Mutat. Res. 1999, 433:53-58.
    • (1999) Mutat. Res. , vol.433 , pp. 53-58
    • Bryans, M.1    Valenzano, M.C.2    Stamato, T.D.3
  • 16
    • 34548567192 scopus 로고    scopus 로고
    • Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4
    • Deshpande R.A., Wilson T.E. Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4. DNA Repair 2007, 6:1507-1516.
    • (2007) DNA Repair , vol.6 , pp. 1507-1516
    • Deshpande, R.A.1    Wilson, T.E.2
  • 17
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining
    • Ahnesorg P., Smith P., Jackson S.P. XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Cell 2006, 124:301-313.
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 18
    • 80955133161 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex
    • Andres S.N., Junop M.S. Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex. Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun. 2011, 67:1399-1402.
    • (2011) Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun. , vol.67 , pp. 1399-1402
    • Andres, S.N.1    Junop, M.S.2
  • 19
    • 80053358977 scopus 로고    scopus 로고
    • Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions
    • Suppl. 1382 p following 1392
    • Wu Q., Ochi T., Matak-Vinkovic D., Robinson C.V., Chirgadze D.Y., Blundell T.L. Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions. Biochem. Soc. Trans. 2011, 39:1387-1392. Suppl. 1382 p following 1392.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1387-1392
    • Wu, Q.1    Ochi, T.2    Matak-Vinkovic, D.3    Robinson, C.V.4    Chirgadze, D.Y.5    Blundell, T.L.6
  • 21
    • 84900415740 scopus 로고    scopus 로고
    • The spatial organization of non-homologous end joining: from bridging to end joining
    • Ochi T., Wu Q., Blundell T.L. The spatial organization of non-homologous end joining: from bridging to end joining. DNA Repair 2014, 17:98-109.
    • (2014) DNA Repair , vol.17 , pp. 98-109
    • Ochi, T.1    Wu, Q.2    Blundell, T.L.3
  • 24
    • 84897026324 scopus 로고    scopus 로고
    • The clinical impact of deficiency in DNA non-homologous end-joining
    • Woodbine L., Gennery A.R., Jeggo P.A. The clinical impact of deficiency in DNA non-homologous end-joining. DNA Repair 2014, 16:84-96.
    • (2014) DNA Repair , vol.16 , pp. 84-96
    • Woodbine, L.1    Gennery, A.R.2    Jeggo, P.A.3
  • 25
    • 84872865986 scopus 로고    scopus 로고
    • Identification of the DNA repair defects in a case of Dubowitz syndrome
    • Yue J., Lu H., Lan S., Liu J., Stein M.N., Haffty B.G., Shen Z. Identification of the DNA repair defects in a case of Dubowitz syndrome. PLOS ONE 2013, 8:e54389.
    • (2013) PLOS ONE , vol.8 , pp. e54389
    • Yue, J.1    Lu, H.2    Lan, S.3    Liu, J.4    Stein, M.N.5    Haffty, B.G.6    Shen, Z.7
  • 26
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann C.B., Davies A., Cost G.J., Caputo E., Li J., Hieter P., Boeke J.D. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 1998, 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 27
    • 61849109768 scopus 로고    scopus 로고
    • Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2 FHA domain
    • Palmbos P.L., Wu D., Daley J.M., Wilson T.E. Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2 FHA domain. Genetics 2008, 180:1809-1819.
    • (2008) Genetics , vol.180 , pp. 1809-1819
    • Palmbos, P.L.1    Wu, D.2    Daley, J.M.3    Wilson, T.E.4
  • 28
    • 84879650163 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae DNA ligase IV supports imprecise end joining independently of its catalytic activity
    • Chiruvella K.K., Liang Z., Birkeland S.R., Basrur V., Wilson T.E. Saccharomyces cerevisiae DNA ligase IV supports imprecise end joining independently of its catalytic activity. PLoS Genet. 2013, 9:e1003599.
    • (2013) PLoS Genet. , vol.9 , pp. e1003599
    • Chiruvella, K.K.1    Liang, Z.2    Birkeland, S.R.3    Basrur, V.4    Wilson, T.E.5
  • 29
    • 23844464546 scopus 로고    scopus 로고
    • DNA joint dependence of pol X family polymerase action in nonhomologous end joining
    • Daley J.M., Laan R.L., Suresh A., Wilson T.E. DNA joint dependence of pol X family polymerase action in nonhomologous end joining. J. Biol. Chem. 2005, 280:29030-29037.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29030-29037
    • Daley, J.M.1    Laan, R.L.2    Suresh, A.3    Wilson, T.E.4
  • 31
    • 28544447826 scopus 로고    scopus 로고
    • Mutations of the Yku80C terminus and Xrs2 FHA domain specifically block yeast nonhomologous end joining
    • Palmbos P.L., Daley J.M., Wilson T.E. Mutations of the Yku80C terminus and Xrs2 FHA domain specifically block yeast nonhomologous end joining. Mol. Cell. Biol. 2005, 25:10782-10790.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10782-10790
    • Palmbos, P.L.1    Daley, J.M.2    Wilson, T.E.3
  • 33
    • 0036021357 scopus 로고    scopus 로고
    • Enhancement of Saccharomyces cerevisiae end-joining efficiency by cell growth stage but not by impairment of recombination
    • Karathanasis E., Wilson T.E. Enhancement of Saccharomyces cerevisiae end-joining efficiency by cell growth stage but not by impairment of recombination. Genetics 2002, 161:1015-1027.
    • (2002) Genetics , vol.161 , pp. 1015-1027
    • Karathanasis, E.1    Wilson, T.E.2
  • 34
    • 45149104841 scopus 로고    scopus 로고
    • Recruitment and dissociation of nonhomologous end joining proteins at a DNA double-strand break in Saccharomyces cerevisiae
    • Wu D., Topper L.M., Wilson T.E. Recruitment and dissociation of nonhomologous end joining proteins at a DNA double-strand break in Saccharomyces cerevisiae. Genetics 2008, 178:1237-1249.
    • (2008) Genetics , vol.178 , pp. 1237-1249
    • Wu, D.1    Topper, L.M.2    Wilson, T.E.3
  • 35
    • 0029976325 scopus 로고    scopus 로고
    • Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae
    • Moore J.K., Haber J.E. Cell cycle and genetic requirements of two pathways of nonhomologous end-joining repair of double-strand breaks in Saccharomyces cerevisiae. Mol. Cell. Biol. 1996, 16:2164-2173.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2164-2173
    • Moore, J.K.1    Haber, J.E.2
  • 36
    • 0033551662 scopus 로고    scopus 로고
    • Efficient processing of DNA ends during yeast nonhomologous end joining. Evidence for a DNA polymerase beta (Pol4)-dependent pathway
    • Wilson T.E., Lieber M.R. Efficient processing of DNA ends during yeast nonhomologous end joining. Evidence for a DNA polymerase beta (Pol4)-dependent pathway. J. Biol. Chem. 1999, 274:23599-23609.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23599-23609
    • Wilson, T.E.1    Lieber, M.R.2
  • 37
    • 0036812245 scopus 로고    scopus 로고
    • A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio
    • Wilson T.E. A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio. Genetics 2002, 162:677-688.
    • (2002) Genetics , vol.162 , pp. 677-688
    • Wilson, T.E.1
  • 39
    • 48749102974 scopus 로고    scopus 로고
    • Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair
    • Kilkenny M.L., Dore A.S., Roe S.M., Nestoras K., Ho J.C., Watts F.Z., Pearl L.H. Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair. Genes Dev. 2008, 22:2034-2047.
    • (2008) Genes Dev. , vol.22 , pp. 2034-2047
    • Kilkenny, M.L.1    Dore, A.S.2    Roe, S.M.3    Nestoras, K.4    Ho, J.C.5    Watts, F.Z.6    Pearl, L.H.7
  • 40
    • 2342484423 scopus 로고    scopus 로고
    • Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling
    • Shiozaki E.N., Gu L., Yan N., Shi Y. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Mol. Cell 2004, 14:405-412.
    • (2004) Mol. Cell , vol.14 , pp. 405-412
    • Shiozaki, E.N.1    Gu, L.2    Yan, N.3    Shi, Y.4
  • 41
    • 25444465151 scopus 로고    scopus 로고
    • Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail
    • Lee M.S., Edwards R.A., Thede G.L., Glover J.N. Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail. J. Biol. Chem. 2005, 280:32053-32056.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32053-32056
    • Lee, M.S.1    Edwards, R.A.2    Thede, G.L.3    Glover, J.N.4
  • 42
    • 0034694841 scopus 로고    scopus 로고
    • The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature
    • Yamane K., Katayama E., Tsuruo T. The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature. Biochem. Biophys. Res. Commun. 2000, 279:678-684.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 678-684
    • Yamane, K.1    Katayama, E.2    Tsuruo, T.3
  • 43
    • 0033575865 scopus 로고    scopus 로고
    • Conserved BRCT regions of TopBP1 and of the tumor suppressor BRCA1 bind strand breaks and termini of DNA
    • Yamane K., Tsuruo T. Conserved BRCT regions of TopBP1 and of the tumor suppressor BRCA1 bind strand breaks and termini of DNA. Oncogene 1999, 18:5194-5203.
    • (1999) Oncogene , vol.18 , pp. 5194-5203
    • Yamane, K.1    Tsuruo, T.2
  • 44
    • 33645217822 scopus 로고    scopus 로고
    • Characterization of the DNA binding and structural properties of the BRCT region of human replication factor C p140 subunit
    • Kobayashi M., Figaroa F., Meeuwenoord N., Jansen L.E., Siegal G. Characterization of the DNA binding and structural properties of the BRCT region of human replication factor C p140 subunit. J. Biol. Chem. 2006, 281:4308-4317.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4308-4317
    • Kobayashi, M.1    Figaroa, F.2    Meeuwenoord, N.3    Jansen, L.E.4    Siegal, G.5
  • 46
    • 79958161083 scopus 로고    scopus 로고
    • Impact of BRCA1 BRCT domain missense substitutions on phosphopeptide recognition
    • Coquelle N., Green R., Glover J.N. Impact of BRCA1 BRCT domain missense substitutions on phosphopeptide recognition. Biochemistry 2011, 50:4579-4589.
    • (2011) Biochemistry , vol.50 , pp. 4579-4589
    • Coquelle, N.1    Green, R.2    Glover, J.N.3
  • 47
    • 84860840671 scopus 로고    scopus 로고
    • The alpha2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection
    • Gilson T., Greer A.E., Vindigni A., Ketner G., Hanakahi L.A. The alpha2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection. Virology 2012, 428:128-135.
    • (2012) Virology , vol.428 , pp. 128-135
    • Gilson, T.1    Greer, A.E.2    Vindigni, A.3    Ketner, G.4    Hanakahi, L.A.5
  • 49
    • 19544379326 scopus 로고    scopus 로고
    • Analysis of DNA ligase IV mutations found in LIG4 syndrome patients: the impact of two linked polymorphisms
    • Girard P.M., Kysela B., Harer C.J., Doherty A.J., Jeggo P.A. Analysis of DNA ligase IV mutations found in LIG4 syndrome patients: the impact of two linked polymorphisms. Hum. Mol. Genet. 2004, 13:2369-2376.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2369-2376
    • Girard, P.M.1    Kysela, B.2    Harer, C.J.3    Doherty, A.J.4    Jeggo, P.A.5


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