메뉴 건너뛰기




Volumn 4, Issue 11, 2006, Pages 1947-1956

A role for PCNA ubiquitination in immunoglobulin hypermutation

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DEAMINASE; IMMUNOGLOBULIN LIGHT CHAIN; PROTEIN DERIVATIVE; PROTEIN RAD18; UNCLASSIFIED DRUG; IMMUNOGLOBULIN LAMBDA CHAIN; MUTAGENIC AGENT; SUMO PROTEIN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

EID: 33751050806     PISSN: 15457885     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0040366     Document Type: Article
Times cited : (137)

References (34)
  • 1
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419: 135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 2
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P, Ulrich HD (2003) Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425: 188-191.
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 3
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche PL, Wing J, Lehmann AR (2004) Interaction of human DNA polymerase eta with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage. Mol Cell 14: 491-500.
    • (2004) Mol Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 4
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe K, Tateishi S, Kawasuji M, Tsurimoto T, Inoue H, et al. (2004) Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J 23: 3886-3896.
    • (2004) EMBO J , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5
  • 5
    • 29444454665 scopus 로고    scopus 로고
    • Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1
    • Garg P, Burgers PM (2005) Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1. Proc Natl Acad Sci U S A 102: 18361-18366.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18361-18366
    • Garg, P.1    Burgers, P.M.2
  • 6
    • 0034268780 scopus 로고    scopus 로고
    • Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme
    • Muramatsu M, Kinoshita K, Fagarasan S, Yamada S, Shinkai Y, et al. (2000) Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme. Cell 102: 553-563.
    • (2000) Cell , vol.102 , pp. 553-563
    • Muramatsu, M.1    Kinoshita, K.2    Fagarasan, S.3    Yamada, S.4    Shinkai, Y.5
  • 7
    • 0037026482 scopus 로고    scopus 로고
    • Altering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase
    • Di Noia J, Neuberger MS (2002) Altering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase. Nature 419: 43-48.
    • (2002) Nature , vol.419 , pp. 43-48
    • Di Noia, J.1    Neuberger, M.S.2
  • 8
    • 29644440411 scopus 로고    scopus 로고
    • Uracil DNA glycosylase disruption blocks Ig gene conversion and induces transition mutations
    • Saribasak H, Saribasak NN, Ipek FM, Ellwart JW, Arakawa H, et al. (2006) Uracil DNA glycosylase disruption blocks Ig gene conversion and induces transition mutations. J Immunol 176: 365-371.
    • (2006) J Immunol , vol.176 , pp. 365-371
    • Saribasak, H.1    Saribasak, N.N.2    Ipek, F.M.3    Ellwart, J.W.4    Arakawa, H.5
  • 9
    • 6344256944 scopus 로고    scopus 로고
    • Mismatch recognition and uracil excision provide complementary paths to both Ig switching and the A/T-focused phase of somatic mutation
    • Rada C, Di Noia JM, Neuberger MS (2004) Mismatch recognition and uracil excision provide complementary paths to both Ig switching and the A/T-focused phase of somatic mutation. Mol Cell 16: 163-171.
    • (2004) Mol Cell , vol.16 , pp. 163-171
    • Rada, C.1    Di Noia, J.M.2    Neuberger, M.S.3
  • 10
    • 0035377269 scopus 로고    scopus 로고
    • DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes
    • Zeng X, Winter DB, Kasmer C, Kraemer KH, Lehmann AR, et al. (2001). DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes. Nat Immunol 2: 537-541.
    • (2001) Nat Immunol , vol.2 , pp. 537-541
    • Zeng, X.1    Winter, D.B.2    Kasmer, C.3    Kraemer, K.H.4    Lehmann, A.R.5
  • 11
    • 18244401095 scopus 로고    scopus 로고
    • Contribution of DNA polymerase eta to immunoglobulin gene hypermutation in the mouse
    • Delbos F, De Smet A, Faili A, Aoufouchi S, Weill JC, et al. (2005) Contribution of DNA polymerase eta to immunoglobulin gene hypermutation in the mouse. J Exp Med 201: 1191-1196.
    • (2005) J Exp Med , vol.201 , pp. 1191-1196
    • Delbos, F.1    De Smet, A.2    Faili, A.3    Aoufouchi, S.4    Weill, J.C.5
  • 12
    • 20844452399 scopus 로고    scopus 로고
    • Different mutation signatures in DNA polymerase eta- and MSH6-deficient mice suggest separate roles in antibody diversification
    • Martomo SA, Yang WW, Wersto RP, Ohkumo T, Kondo Y, et al. (2005) Different mutation signatures in DNA polymerase eta- and MSH6-deficient mice suggest separate roles in antibody diversification. Proc Natl Acad Sci USA 102: 8656-8661.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8656-8661
    • Martomo, S.A.1    Yang, W.W.2    Wersto, R.P.3    Ohkumo, T.4    Kondo, Y.5
  • 13
    • 33344468484 scopus 로고    scopus 로고
    • Strand-biased defect in C/G transversions in hypermutating immunoglobulin genes in Rev1-deficient mice
    • Jansen JG, Langerak P, Tsaalbi-Shtylik A, van den Berk P, Jacobs H, et al. (2006) Strand-biased defect in C/G transversions in hypermutating immunoglobulin genes in Rev1-deficient mice. J Exp Med 203: 319-323.
    • (2006) J Exp Med , vol.203 , pp. 319-323
    • Jansen, J.G.1    Langerak, P.2    Tsaalbi-Shtylik, A.3    Van Den Berk, P.4    Jacobs, H.5
  • 14
    • 0037388452 scopus 로고    scopus 로고
    • Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line
    • Simpson LJ, Sale JE (2003) Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line. EMBO J 22: 1654-1664.
    • (2003) EMBO J , vol.22 , pp. 1654-1664
    • Simpson, L.J.1    Sale, J.E.2
  • 15
    • 20044379457 scopus 로고    scopus 로고
    • An update on the role of translesion synthesis DNA polymerases in Ig hypermutation
    • Diaz M, Lawrence C (2005) An update on the role of translesion synthesis DNA polymerases in Ig hypermutation. Trends Immunol 26: 215-220.
    • (2005) Trends Immunol , vol.26 , pp. 215-220
    • Diaz, M.1    Lawrence, C.2
  • 16
    • 0025936509 scopus 로고
    • Increased ratio of targeted to random integration after transfection of chicken B cell lines
    • Buerstedde JM, Takeda S (1991) Increased ratio of targeted to random integration after transfection of chicken B cell lines. Cell 67: 179-188.
    • (1991) Cell , vol.67 , pp. 179-188
    • Buerstedde, J.M.1    Takeda, S.2
  • 17
    • 3242886111 scopus 로고    scopus 로고
    • Reverse genetic studies of the DNA damage response in the chicken B lymphocyte line DT40
    • Yamazoe M, Sonoda E, Hochegger H, Takeda S (2004) Reverse genetic studies of the DNA damage response in the chicken B lymphocyte line DT40. DNA Repair 3: 1175-1185.
    • (2004) DNA Repair , vol.3 , pp. 1175-1185
    • Yamazoe, M.1    Sonoda, E.2    Hochegger, H.3    Takeda, S.4
  • 18
    • 19344367559 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase initiates immunoglobulin gene conversion and hypermutation by a common intermediate
    • DOI: 10.1371/journal.pbio.0020179
    • Arakawa H, Saribasak H, Buerstedde JM (2004) Activation-induced cytidine deaminase initiates immunoglobulin gene conversion and hypermutation by a common intermediate. PLoS Biol. 2: e179. DOI: 10.1371/journal.pbio.0020179
    • (2004) PLoS Biol , vol.2
    • Arakawa, H.1    Saribasak, H.2    Buerstedde, J.M.3
  • 19
    • 1542348470 scopus 로고    scopus 로고
    • Immunoglobulin gene conversion: Insights from bursal B cells and the DT40 cell line
    • Arakawa H, Buerstedde JM (2004) Immunoglobulin gene conversion: insights from bursal B cells and the DT40 cell line. Dev Dyn 229: 458-464.
    • (2004) Dev Dyn , vol.229 , pp. 458-464
    • Arakawa, H.1    Buerstedde, J.M.2
  • 20
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S (2005) SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436: 428-433.
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 21
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and Ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E, Chen S, Davies AA, Huttner D, Krejci L, et al. (2005) Crosstalk between SUMO and Ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 19: 123-133.
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5
  • 22
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson JR, Lawrence CW, Hinkle DC (1996) Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382: 729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 23
    • 33644543730 scopus 로고    scopus 로고
    • The catalytic activity of REV1 is employed during immunoglobulin gene diversification in DT40
    • Ross AL, Sale JE (2006) The catalytic activity of REV1 is employed during immunoglobulin gene diversification in DT40. Mol Immunol 43: 1587-1594.
    • (2006) Mol Immunol , vol.43 , pp. 1587-1594
    • Ross, A.L.1    Sale, J.E.2
  • 25
    • 0037107370 scopus 로고    scopus 로고
    • RAD18 and RAD54 cooperatively contribute to maintenance of genomic stability in vertebrate cells
    • Yamashita YM, Okada T, Matsusaka T, Sonoda E, Zhao GY, et al. (2002) RAD18 and RAD54 cooperatively contribute to maintenance of genomic stability in vertebrate cells. EMBO J 21: 5558-5566.
    • (2002) EMBO J , vol.21 , pp. 5558-5566
    • Yamashita, Y.M.1    Okada, T.2    Matsusaka, T.3    Sonoda, E.4    Zhao, G.Y.5
  • 26
    • 33744958660 scopus 로고    scopus 로고
    • The WD40-repeats of FANCL are required for Fanconi anemia core complex assembly
    • In press
    • Gurtan AM, Stuckert P, D'Andrea AD (2006) The WD40-repeats of FANCL are required for Fanconi anemia core complex assembly. J Biol Chem: In press.
    • (2006) J Biol Chem
    • Gurtan, A.M.1    Stuckert, P.2    D'Andrea, A.D.3
  • 27
    • 13844308526 scopus 로고    scopus 로고
    • UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40
    • Simpson LJ, Sale JE (2005) UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40. DNA Repair 4: 503-510.
    • (2005) DNA Repair , vol.4 , pp. 503-510
    • Simpson, L.J.1    Sale, J.E.2
  • 28
    • 33749510488 scopus 로고    scopus 로고
    • RAD18-independent ubiquitination of proliferating-cell nuclear antigen in the avian cell line DT40
    • [E-pub 4 August 2006]
    • Simpson LJ, Ross AL, Szuts D, Alviani CA, Oestergaard VH, et al. (2006) RAD18-independent ubiquitination of proliferating-cell nuclear antigen in the avian cell line DT40. EMBO Rep [E-pub 4 August 2006].
    • (2006) EMBO Rep
    • Simpson, L.J.1    Ross, A.L.2    Szuts, D.3    Alviani, C.A.4    Oestergaard, V.H.5
  • 29
  • 30
    • 10644283823 scopus 로고    scopus 로고
    • Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution
    • International Chicken Genome Sequencing Consortium
    • International Chicken Genome Sequencing Consortium (2004) Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature 432: 695-716.
    • (2004) Nature , vol.432 , pp. 695-716
  • 31
    • 3042559648 scopus 로고    scopus 로고
    • Mutant loxP vectors for selectable marker recycle and conditional knock-outs
    • Arakawa H, Lodygin D, Buerstedde JM (2001) Mutant loxP vectors for selectable marker recycle and conditional knock-outs. BMC Biotechnol 1: 7.
    • (2001) BMC Biotechnol , vol.1 , pp. 7
    • Arakawa, H.1    Lodygin, D.2    Buerstedde, J.M.3
  • 32
    • 0037083364 scopus 로고    scopus 로고
    • Requirement of the activation-induced deaminase (AID) gene for immunoglobulin gene conversion
    • Arakawa H, Hauschild J, Buerstedde JM (2002) Requirement of the activation-induced deaminase (AID) gene for immunoglobulin gene conversion. Science 295: 1301-1306.
    • (2002) Science , vol.295 , pp. 1301-1306
    • Arakawa, H.1    Hauschild, J.2    Buerstedde, J.M.3
  • 33
    • 0034607653 scopus 로고    scopus 로고
    • c-Jun and p53 activity is modulated by SUMO-1 modification
    • Muller S, Berger M, Lehembre F, Seeler JS, Haupt Y, et al. (2000) c-Jun and p53 activity is modulated by SUMO-1 modification. J Biol Chem 275: 13321-13329.
    • (2000) J Biol Chem , vol.275 , pp. 13321-13329
    • Muller, S.1    Berger, M.2    Lehembre, F.3    Seeler, J.S.4    Haupt, Y.5
  • 34
    • 20144374676 scopus 로고    scopus 로고
    • RDM1, a novel RNA-recognition motif (RRM)-containing protein involved in the cell response to cisplatin in vertebrates
    • Hamimes S, Arakawa H, Stasiak AZ, Kierzek AM, Hirano S, et al. (2005) RDM1, a novel RNA-recognition motif (RRM)-containing protein involved in the cell response to cisplatin in vertebrates. J Biol Chem 280: 9225-9235.
    • (2005) J Biol Chem , vol.280 , pp. 9225-9235
    • Hamimes, S.1    Arakawa, H.2    Stasiak, A.Z.3    Kierzek, A.M.4    Hirano, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.