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Volumn 14, Issue 4, 2004, Pages 491-500

Interaction of human DNA polymerase η with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE;

EID: 2442417331     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00259-X     Document Type: Article
Times cited : (748)

References (29)
  • 1
    • 0030800865 scopus 로고    scopus 로고
    • Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities
    • Bailly V., Lauder S., Prakash S., Prakash L. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272:1997;23360-23365
    • (1997) J. Biol. Chem. , vol.272 , pp. 23360-23365
    • Bailly, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 2
    • 0242389787 scopus 로고    scopus 로고
    • Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp
    • Bunting K.A., Roe S.M., Pearl L.H. Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp. EMBO J. 22:2003;5883-5892
    • (2003) EMBO J. , vol.22 , pp. 5883-5892
    • Bunting, K.A.1    Roe, S.M.2    Pearl, L.H.3
  • 3
    • 0035924590 scopus 로고    scopus 로고
    • Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation
    • Campbell D.S., Holt C.E. Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation. Neuron. 32:2001;1013-1026
    • (2001) Neuron , vol.32 , pp. 1013-1026
    • Campbell, D.S.1    Holt, C.E.2
  • 4
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/C1P1) complexed with human PCNA
    • Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J. Structure of the C-terminal region of p21(WAF1/C1P1) complexed with human PCNA. Cell. 87:1996;297-306
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 6
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:2001;195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 7
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.-L., Pyrolowakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrolowakis, G.4    Jentsch, S.5
  • 8
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Noncanonical MMS2encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 96:1999;645-653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 9
    • 0033538470 scopus 로고    scopus 로고
    • HRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson R.E., Kondratick C.M., Prakash S., Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 285:1999;263-265
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 11
    • 0035862988 scopus 로고    scopus 로고
    • Domain structure, localization and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells
    • Kannouche P., Broughton B.C., Volker M., Hanaoka F., Mullenders L.H.F., Lehmann A.R. Domain structure, localization and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells. Genes Dev. 15:2001;158-172
    • (2001) Genes Dev. , vol.15 , pp. 158-172
    • Kannouche, P.1    Broughton, B.C.2    Volker, M.3    Hanaoka, F.4    Mullenders, L.H.F.5    Lehmann, A.R.6
  • 13
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell. 79:1994;1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 14
    • 0037122004 scopus 로고    scopus 로고
    • Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
    • Mallery D.L., Vandenberg C.J., Hiom K. Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J. 21:2002;6755-6762
    • (2002) EMBO J. , vol.21 , pp. 6755-6762
    • Mallery, D.L.1    Vandenberg, C.J.2    Hiom, K.3
  • 16
    • 0034660259 scopus 로고    scopus 로고
    • Accurate translesion synthesis by human DNA polymerase η
    • Masutani C., Kusumoto R., Iwai S., Hanaoka F. Accurate translesion synthesis by human DNA polymerase η EMBO J. 19:2000;3100-3109
    • (2000) EMBO J. , vol.19 , pp. 3100-3109
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 17
    • 1542287220 scopus 로고    scopus 로고
    • Preferential cis-eyn thymine dimer bypass by DNA polymerase eta occurs with biased fidelity
    • McCulloch S.D., Kokoska R.J., Masutani C., Iwai S., Hanaoka F., Kunkel T.A. Preferential cis-eyn thymine dimer bypass by DNA polymerase eta occurs with biased fidelity. Nature. 428:2004;97-100
    • (2004) Nature , vol.428 , pp. 97-100
    • McCulloch, S.D.1    Kokoska, R.J.2    Masutani, C.3    Iwai, S.4    Hanaoka, F.5    Kunkel, T.A.6
  • 20
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science. 287:2000;501-504
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 21
    • 0033061841 scopus 로고    scopus 로고
    • The effects of ionizing radiation on DNA synthesis in eukaryotic cells
    • Rowley R., Phillips E.N., Schroeder A.L. The effects of ionizing radiation on DNA synthesis in eukaryotic cells. Int. J. Radiat. Biol. 75:1999;267-283
    • (1999) Int. J. Radiat. Biol. , vol.75 , pp. 267-283
    • Rowley, R.1    Phillips, E.N.2    Schroeder, A.L.3
  • 22
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L. A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J. 22:2003;1273-1281
    • (2003) EMBO J. , vol.22 , pp. 1273-1281
    • Shih, S.C.1    Prag, G.2    Francis, S.A.3    Sutanto, M.A.4    Hurley, J.H.5    Hicke, L.6
  • 23
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P., Ulrich H.D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature. 425:2003;188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 24
    • 0034608876 scopus 로고    scopus 로고
    • Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens
    • Tateishi S., Sakuraba Y., Masuyama S., Inoue H., Yamaizumi M. Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. Proc. Natl. Acad. Sci. USA. 97:2000;7927-7932
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7927-7932
    • Tateishi, S.1    Sakuraba, Y.2    Masuyama, S.3    Inoue, H.4    Yamaizumi, M.5
  • 26
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase η: Implications for translesion DNA synthesis
    • Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K. Structure of the catalytic core of S. cerevisiae DNA polymerase η implications for translesion DNA synthesis Mol. Cell. 8:2001;417-426
    • (2001) Mol. Cell , vol.8 , pp. 417-426
    • Trincao, J.1    Johnson, R.E.2    Escalante, C.R.3    Prakash, S.4    Prakash, L.5    Aggarwal, A.K.6
  • 27
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin- conjugating enzymes in DNA repair
    • Ulrich H.D., Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19:2000;3388-3397
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 29
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick E. The puzzle of PCNA's many partners. Bioessays. 22:2000;997-1006
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.