메뉴 건너뛰기




Volumn 6, Issue 12, 2007, Pages 1764-1773

Alkyladenine DNA glycosylase (Aag) in somatic hypermutation and class switch recombination

Author keywords

Alkyladenine DNA glycosylase; Class switch recombination; Immunoglobulin genes; Somatic hypermutation

Indexed keywords

ALKYLADENINE DNA GLYCOSYLTRANSFERASE; CYTOSINE; DNA GLYCOSYLTRANSFERASE; HYPOXANTHINE; UNCLASSIFIED DRUG;

EID: 36048978959     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2007.06.012     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 33644636246 scopus 로고    scopus 로고
    • AID in somatic hypermutation and class switch recombination
    • Longerich S., Basu U., Alt F., and Storb U. AID in somatic hypermutation and class switch recombination. Curr. Opin. Immunol. 18 (2006) 164-174
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 164-174
    • Longerich, S.1    Basu, U.2    Alt, F.3    Storb, U.4
  • 4
    • 33646018048 scopus 로고    scopus 로고
    • A role for the MutL mismatch repair Mlh3 protein in immunoglobulin class switch DNA recombination and somatic hypermutation
    • Wu X., Tsai C.Y., Patam M.B., Zan H., Chen J.P., Lipkin S.M., and Casali P. A role for the MutL mismatch repair Mlh3 protein in immunoglobulin class switch DNA recombination and somatic hypermutation. J. Immunol. 176 (2006) 5426-5437
    • (2006) J. Immunol. , vol.176 , pp. 5426-5437
    • Wu, X.1    Tsai, C.Y.2    Patam, M.B.3    Zan, H.4    Chen, J.P.5    Lipkin, S.M.6    Casali, P.7
  • 5
    • 0037108463 scopus 로고    scopus 로고
    • Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice
    • Rada C., Williams G., Nilsen H., Barnes D., Lindahl T., and Neuberger M. Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice. Curr. Biol. 12 (2002) 1748-1755
    • (2002) Curr. Biol. , vol.12 , pp. 1748-1755
    • Rada, C.1    Williams, G.2    Nilsen, H.3    Barnes, D.4    Lindahl, T.5    Neuberger, M.6
  • 7
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A., and Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J. 16 (1997) 3341-3348
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 8
    • 28544439696 scopus 로고    scopus 로고
    • DNA polymerases and somatic hypermutation of immunoglobulin genes
    • Seki M., Gearhart P.J., and Wood R.D. DNA polymerases and somatic hypermutation of immunoglobulin genes. EMBO Rep. 6 (2005) 1143-1148
    • (2005) EMBO Rep. , vol.6 , pp. 1143-1148
    • Seki, M.1    Gearhart, P.J.2    Wood, R.D.3
  • 10
    • 3142674907 scopus 로고    scopus 로고
    • Examination of Msh6- and Msh3-deficient mice in class switching reveals overlapping distinct roles of MutS homologues in antibody diversification
    • Li Z., Scherer S., D R., Iglesias-Ussel M., Peled J., Bardwell P., Zhuang M., Lee K., Martin A., Edelmann W., and Scharff M. Examination of Msh6- and Msh3-deficient mice in class switching reveals overlapping distinct roles of MutS homologues in antibody diversification. J. Exp. Med. 200 (2004) 47-59
    • (2004) J. Exp. Med. , vol.200 , pp. 47-59
    • Li, Z.1    Scherer, S.2    Iglesias-Ussel, M.3    Peled, J.4    Bardwell, P.5    Zhuang, M.6    Lee, K.7    Martin, A.8    Edelmann, W.9    Scharff, M.10
  • 13
    • 0035377269 scopus 로고    scopus 로고
    • DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes
    • Zeng X., Winter D., Kasmer C., Kraemer K., Lehmann A., and Gearhart P. DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes. Nature Immunology 2 (2001) 537-541
    • (2001) Nature Immunology , vol.2 , pp. 537-541
    • Zeng, X.1    Winter, D.2    Kasmer, C.3    Kraemer, K.4    Lehmann, A.5    Gearhart, P.6
  • 14
    • 1642499721 scopus 로고    scopus 로고
    • DNA polymerase eta is involved in hypermutation occurring during immunoglobulin class switch recombination
    • Faili A., Aoufouchi S., Weller S., Vuillier F., Stary A., Sarasin A., Reynaud C., and Weill J. DNA polymerase eta is involved in hypermutation occurring during immunoglobulin class switch recombination. J. Exp. Med. 199 (2004) 265-270
    • (2004) J. Exp. Med. , vol.199 , pp. 265-270
    • Faili, A.1    Aoufouchi, S.2    Weller, S.3    Vuillier, F.4    Stary, A.5    Sarasin, A.6    Reynaud, C.7    Weill, J.8
  • 15
    • 1842732235 scopus 로고    scopus 로고
    • Absence of DNA polymerase eta reveals targeting of C mutations on the nontranscribed strand in immunoglobulin switch regions
    • Zeng X., Negrete G., Kasmer C., Yang W., and Gearhart P. Absence of DNA polymerase eta reveals targeting of C mutations on the nontranscribed strand in immunoglobulin switch regions. J. Exp. Med. 199 (2004) 917-924
    • (2004) J. Exp. Med. , vol.199 , pp. 917-924
    • Zeng, X.1    Negrete, G.2    Kasmer, C.3    Yang, W.4    Gearhart, P.5
  • 16
    • 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 J.-C., and Reynaud C.-A. Contribution of DNA polymerase eta to immunoglobulin gene hypermutation in the mouse. J. Exp. Med. 201 (2005) 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    Reynaud, C.-A.6
  • 17
    • 0019331557 scopus 로고
    • Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus
    • Karran P., and Lindahl T. Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus. Biochemistry 19 (1980) 6005-6011
    • (1980) Biochemistry , vol.19 , pp. 6005-6011
    • Karran, P.1    Lindahl, T.2
  • 18
    • 0022993948 scopus 로고
    • Site-specific mutagenesis in vivo by single methylated or deaminated purine bases
    • Hill-Perkins M., Jones M.D., and Karran P. Site-specific mutagenesis in vivo by single methylated or deaminated purine bases. Mutat. Res. 162 (1986) 153-163
    • (1986) Mutat. Res. , vol.162 , pp. 153-163
    • Hill-Perkins, M.1    Jones, M.D.2    Karran, P.3
  • 19
    • 0037449770 scopus 로고    scopus 로고
    • A-to-I RNA editing: recent news and residual mysteries
    • Maas S., Rich A., and Nishikura K. A-to-I RNA editing: recent news and residual mysteries. J. Biol. Chem. 278 (2003) 1391-1394
    • (2003) J. Biol. Chem. , vol.278 , pp. 1391-1394
    • Maas, S.1    Rich, A.2    Nishikura, K.3
  • 22
    • 27944493275 scopus 로고    scopus 로고
    • The very 5′ end and the constant region of Ig genes are spared from somatic mutation because AID does not access these regions
    • Longerich S., Tanaka A., Bozek G., Nicolae D., and Storb U. The very 5′ end and the constant region of Ig genes are spared from somatic mutation because AID does not access these regions. J. Exp. Med. 202 (2005) 1443-1454
    • (2005) J. Exp. Med. , vol.202 , pp. 1443-1454
    • Longerich, S.1    Tanaka, A.2    Bozek, G.3    Nicolae, D.4    Storb, U.5
  • 23
    • 0035881820 scopus 로고    scopus 로고
    • The intrinsic hypermutability of antibody heavy and light chain genes decays exponentially
    • Rada C., and Milstein C. The intrinsic hypermutability of antibody heavy and light chain genes decays exponentially. EMBO J. 20 (2001) 4570-4576
    • (2001) EMBO J. , vol.20 , pp. 4570-4576
    • Rada, C.1    Milstein, C.2
  • 24
    • 0030845386 scopus 로고    scopus 로고
    • Rapid methods for the analysis of Ig gene hypermutation: application to transgenic and gene targeted mice
    • Jolly C., Klix N., and Neuberger M. Rapid methods for the analysis of Ig gene hypermutation: application to transgenic and gene targeted mice. Nucleic Acids Res. 25 (1997) 1913-19199
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1913-19199
    • Jolly, C.1    Klix, N.2    Neuberger, M.3
  • 25
    • 0033603340 scopus 로고    scopus 로고
    • Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells
    • Muramatsu M., Sankaranand V.S., Anant S., Sugai M., Kinoshita K., Davidson N.O., and Honjo T. Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells. J. Biol. Chem. 274 (1999) 18470-18476
    • (1999) J. Biol. Chem. , vol.274 , pp. 18470-18476
    • Muramatsu, M.1    Sankaranand, V.S.2    Anant, S.3    Sugai, M.4    Kinoshita, K.5    Davidson, N.O.6    Honjo, T.7
  • 26
    • 0036468545 scopus 로고    scopus 로고
    • 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance
    • Roth R.B., and Samson L.D. 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance. Cancer Res. 62 (2002) 656-660
    • (2002) Cancer Res. , vol.62 , pp. 656-660
    • Roth, R.B.1    Samson, L.D.2
  • 27
    • 0019798417 scopus 로고
    • Induction of the DNA repair enzymes uracil DNA glycosylase and 3-methyladenine DNA glycosylase in regenerating rat liver
    • Gombar C.T., Katz E.J., Magee P.N., and Sirover M.A. Induction of the DNA repair enzymes uracil DNA glycosylase and 3-methyladenine DNA glycosylase in regenerating rat liver. Carcinogenesis 2 (1981) 595-599
    • (1981) Carcinogenesis , vol.2 , pp. 595-599
    • Gombar, C.T.1    Katz, E.J.2    Magee, P.N.3    Sirover, M.A.4
  • 28
    • 0034282422 scopus 로고    scopus 로고
    • The zab domain of the human RNA editing enzyme ADAR1 recognizes Z-DNA when surrounded by B-DNA
    • Kim Y.G., Lowenhaupt K., Maas S., Herbert A., Schwartz T., and Rich A. The zab domain of the human RNA editing enzyme ADAR1 recognizes Z-DNA when surrounded by B-DNA. J. Biol. Chem. 275 (2000) 26828-26833
    • (2000) J. Biol. Chem. , vol.275 , pp. 26828-26833
    • Kim, Y.G.1    Lowenhaupt, K.2    Maas, S.3    Herbert, A.4    Schwartz, T.5    Rich, A.6
  • 29
    • 33744944261 scopus 로고    scopus 로고
    • Non-B DNA structure-induced genetic instability
    • Wang G., and Vasquez K.M. Non-B DNA structure-induced genetic instability. Mutat. Res. 598 (2006) 103-119
    • (2006) Mutat. Res. , vol.598 , pp. 103-119
    • Wang, G.1    Vasquez, K.M.2
  • 30
    • 10744223020 scopus 로고    scopus 로고
    • Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes
    • Keegan L.P., Leroy A., Sproul D., and O'Connell M.A. Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes. Genome Biol. 5 (2004) 209
    • (2004) Genome Biol. , vol.5 , pp. 209
    • Keegan, L.P.1    Leroy, A.2    Sproul, D.3    O'Connell, M.A.4
  • 32
    • 1642411206 scopus 로고    scopus 로고
    • Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase
    • O'Brien P.J., and Ellenberger T. Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase. J. Biol. Chem. 279 (2004) 9750-9757
    • (2004) J. Biol. Chem. , vol.279 , pp. 9750-9757
    • O'Brien, P.J.1    Ellenberger, T.2
  • 33
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the E. coli antimutator enzyme endonuclease V
    • Moe A., Ringvoll J., Nordstrand L., Eide L., Bjoras M., Seeberg E., Rognes T., and Klungland A. Incision at hypoxanthine residues in DNA by a mammalian homologue of the E. coli antimutator enzyme endonuclease V. Nucl. Acids Res. 31 (2004) 3893-3900
    • (2004) Nucl. Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.3    Eide, L.4    Bjoras, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 34
    • 0032806424 scopus 로고    scopus 로고
    • Endonuclease V protects Escherichia coli against specific mutations caused by nitrous acid
    • Schouten K.A., and Weiss B. Endonuclease V protects Escherichia coli against specific mutations caused by nitrous acid. Mutat. Res. 435 (1999) 245-254
    • (1999) Mutat. Res. , vol.435 , pp. 245-254
    • Schouten, K.A.1    Weiss, B.2
  • 35
    • 32544439248 scopus 로고    scopus 로고
    • SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair
    • Di Noia J.M., Rada C., and Neuberger M.S. SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair. EMBO J. 25 (2006) 585-595
    • (2006) EMBO J. , vol.25 , pp. 585-595
    • Di Noia, J.M.1    Rada, C.2    Neuberger, M.S.3
  • 37
    • 0037415391 scopus 로고    scopus 로고
    • Functions of human DNA polymerases eta, kappa, and iota
    • Kunkel T., Pavlov Y., and Bebenek K. Functions of human DNA polymerases eta, kappa, and iota. DNA Rep. 2 (2003) 135-149
    • (2003) DNA Rep. , vol.2 , pp. 135-149
    • Kunkel, T.1    Pavlov, Y.2    Bebenek, K.3
  • 38
    • 0034214838 scopus 로고    scopus 로고
    • pol iota, a remarkably error-prone human DNA polymerase
    • Tissier A., McDonald J.P., Frank E.G., and Woodgate R. pol iota, a remarkably error-prone human DNA polymerase. Genes Dev. 14 (2000) 1642-1650
    • (2000) Genes Dev. , vol.14 , pp. 1642-1650
    • Tissier, A.1    McDonald, J.P.2    Frank, E.G.3    Woodgate, R.4
  • 39
    • 33846404877 scopus 로고    scopus 로고
    • DNA polymerase eta is the sole contributor of A/T modifications during immunoglobulin gene hypermutation in the mouse
    • Delbos F., Aoufouchi S., Faili A., Weill J.C., and Reynaud C.A. DNA polymerase eta is the sole contributor of A/T modifications during immunoglobulin gene hypermutation in the mouse. J. Exp. Med. 204 (2007) 17-23
    • (2007) J. Exp. Med. , vol.204 , pp. 17-23
    • Delbos, F.1    Aoufouchi, S.2    Faili, A.3    Weill, J.C.4    Reynaud, C.A.5
  • 41
    • 4444239054 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase (AID) can target both DNA strands when the DNA is supercoiled
    • Shen H.M., and Storb U. Activation-induced cytidine deaminase (AID) can target both DNA strands when the DNA is supercoiled. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 12997-13002
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12997-13002
    • Shen, H.M.1    Storb, U.2
  • 42
    • 28544447014 scopus 로고    scopus 로고
    • Targeting of the activation-induced cytosine deaminase is strongly influenced by the sequence and structure of the targeted DNA
    • Shen H., Ratnam S., and Storb U. Targeting of the activation-induced cytosine deaminase is strongly influenced by the sequence and structure of the targeted DNA. Mol. Cell Biol. 25 (2005) 10815-10821
    • (2005) Mol. Cell Biol. , vol.25 , pp. 10815-10821
    • Shen, H.1    Ratnam, S.2    Storb, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.