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Volumn 26, Issue 4, 2012, Pages 1517-1525

Differences in the enzymatic efficiency of human and bony fish AID are mediated by a single residue in the C terminus modulating single-stranded DNA binding

Author keywords

Antibody diversification; DNA mutating enzymes; Mechanisms of enzyme thermosensitivity

Indexed keywords

ACTIVATION INDUCED CYTIDINE DEAMINASE; AMINO ACID; SINGLE STRANDED DNA;

EID: 84860914465     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-198135     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 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., and Honjo, T. (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    Honjo, T.6
  • 4
    • 0037926476 scopus 로고    scopus 로고
    • Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation
    • DOI 10.1038/nature01760
    • Pham, P., Bransteitter, R., Petruska, J., and Goodman, M. F. (2003) Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 424, 103-107 (Pubitemid 36834850)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 103-107
    • Pham, P.1    Bransteitter, R.2    Petruska, J.3    Goodman, M.F.4
  • 5
    • 0037901850 scopus 로고    scopus 로고
    • Human activation-induced cytidine deaminase causes transcription- dependent, strand-biased C to U deaminations
    • DOI 10.1093/nar/gkg464
    • Sohail, A., Klapacz, J., Samaranayake, M., Ullah, A., and Bhagwat, A. S. (2003) Human activation-induced cytidine deaminase causes transcription- dependent, strand-biased C to U deaminations. Nucleic Acids Res. 31, 2990-2994 (Pubitemid 37441756)
    • (2003) Nucleic Acids Research , vol.31 , Issue.12 , pp. 2990-2994
    • Sohail, A.1    Klapacz, J.2    Samaranayake, M.3    Ullah, A.4    Bhagwat, A.S.5
  • 6
    • 17144424674 scopus 로고    scopus 로고
    • -/- mice
    • DOI 10.1007/s00251-004-0748-0
    • Larijani, M., Frieder, D., Basit, W., and Martin, A. (2005) The mutation spectrum of purified AID is similar to the mutability index in Ramos cells and in ung(-/-)msh2(-/-) mice. Immunogenetics 56, 840-845 (Pubitemid 40558087)
    • (2005) Immunogenetics , vol.56 , Issue.11 , pp. 840-845
    • Larijani, M.1    Frieder, D.2    Basit, W.3    Martin, A.4
  • 7
    • 3142765336 scopus 로고    scopus 로고
    • Class-switch recombination: Interplay of transcription, DNA deamination and DNA repair
    • Chaudhuri, J., and Alt, F. W. (2004) Class-switch recombination: interplay of transcription, DNA deamination and DNA repair. Nat. Rev. Immunol. 4, 541-552 (Pubitemid 38931769)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.7 , pp. 541-552
    • Chaudhuri, J.1    Alt, F.W.2
  • 9
    • 17144432313 scopus 로고    scopus 로고
    • Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities
    • DOI 10.1093/nar/gki343
    • Langlois, M. A., Beale, R. C., Conticello, S. G., and Neuberger, M. S. (2005) Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities. Nucleic Acids Res. 33, 1913-1923 (Pubitemid 41748336)
    • (2005) Nucleic Acids Research , vol.33 , Issue.6 , pp. 1913-1923
    • Langlois, M.-A.1    Beale, R.C.L.2    Conticello, S.G.3    Neuberger, M.S.4
  • 10
    • 1542328859 scopus 로고    scopus 로고
    • Comparison of the Differential Context-dependence of DNA Deamination by APOBEC Enzymes: Correlation with Mutation Spectra in Vivo
    • DOI 10.1016/j.jmb.2004.01.046, PII S0022283604001196
    • Beale, R. C., Petersen-Mahrt, S. K., Watt, I. N., Harris, R. S., Rada, C., and Neuberger, M. S. (2004) Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J. Mol. Biol. 337, 585-596 (Pubitemid 38326879)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 585-596
    • Beale, R.C.L.1    Petersen-Mahrt, S.K.2    Watt, I.N.3    Harris, R.S.4    Rada, C.5    Neuberger, M.S.6
  • 11
    • 1342282983 scopus 로고    scopus 로고
    • DNA Substrate Length and Surrounding Sequence Affect the Activation-induced Deaminase Activity at Cytidine
    • DOI 10.1074/jbc.M311616200
    • Yu, K., Huang, F. T., and Lieber, M. R. (2004) DNA substrate length and surrounding sequence affect the activation-induced deaminase activity at cytidine. J. Biol. Chem. 279, 6496-6500 (Pubitemid 38248783)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6496-6500
    • Yu, K.1    Huang, F.-T.2    Lieber, M.R.3
  • 12
    • 33845730352 scopus 로고    scopus 로고
    • AID associates with single-stranded DNA with high affinity and a long complex half-life in a sequence-independent manner
    • DOI 10.1128/MCB.00824-06
    • Larijani, M., Petrov, A. P., Kolenchenko, O., Berru, M., Krylov, S. N., and Martin, A. (2007) AID associates with single-stranded DNA with high affinity and a long complex half-life in a sequence-independent manner. Mol. Cell. Biol. 27, 20-30 (Pubitemid 46013229)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.1 , pp. 20-30
    • Larijani, M.1    Petrov, A.P.2    Kolenchenko, O.3    Berru, M.4    Krylov, S.N.5    Martin, A.6
  • 13
    • 34247595465 scopus 로고    scopus 로고
    • DNA deaminases AID and APOBEC3G act processively on single-stranded DNA
    • author reply 693-684
    • Pham, P., Chelico, L., and Goodman, M. F. (2007) DNA deaminases AID and APOBEC3G act processively on single-stranded DNA. DNA Repair (Amst.) 6, 689-692; author reply 693-684
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 689-692
    • Pham, P.1    Chelico, L.2    Goodman, M.F.3
  • 14
    • 33846066628 scopus 로고    scopus 로고
    • The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action
    • DOI 10.1016/j.dnarep.2006.10.001, PII S1568786406003089
    • Coker, H. A., and Petersen-Mahrt, S. K. (2007) The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action. DNA Repair (Amst.) 6, 235-243 (Pubitemid 46074495)
    • (2007) DNA Repair , vol.6 , Issue.2 , pp. 235-243
    • Coker, H.A.1    Petersen-Mahrt, S.K.2
  • 15
    • 67650330317 scopus 로고    scopus 로고
    • AID upmutants isolated using a high-throughput screen highlight the immunity/cancer balance limiting DNA deaminase activity
    • Wang, M., Yang, Z., Rada, C., and Neuberger, M. S. (2009) AID upmutants isolated using a high-throughput screen highlight the immunity/cancer balance limiting DNA deaminase activity. Nat. Struct. Mol. Biol. 16, 769-776
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 769-776
    • Wang, M.1    Yang, Z.2    Rada, C.3    Neuberger, M.S.4
  • 16
    • 76149119416 scopus 로고    scopus 로고
    • Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID
    • Wang, M., Rada, C., and Neuberger, M. S. (2010) Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID. J. Exp. Med. 207, 141-153
    • (2010) J. Exp. Med. , vol.207 , pp. 141-153
    • Wang, M.1    Rada, C.2    Neuberger, M.S.3
  • 18
    • 79959560118 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase structure and functions: A species comparative view
    • Barreto, V. M., and Magor, B. G. (2011) Activation-induced cytidine deaminase structure and functions: a species comparative view. Dev. Comp. Immunol. 35, 991-1007
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 991-1007
    • Barreto, V.M.1    Magor, B.G.2
  • 21
    • 77649336969 scopus 로고    scopus 로고
    • The cellular context of AID expressing cells in fish lymphoid tissues
    • Saunders, H. L., Oko, A. L., Scott, A. N., Fan, C. W., and Magor, B. G. (2010) The cellular context of AID expressing cells in fish lymphoid tissues. Dev. Comp. Immunol. 34, 669-676
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 669-676
    • Saunders, H.L.1    Oko, A.L.2    Scott, A.N.3    Fan, C.W.4    Magor, B.G.5
  • 22
    • 14944348431 scopus 로고    scopus 로고
    • The immunoglobulin heavy-chain locus in zebrafish: Identification and expression of a previously unknown isotype, immunoglobulin Z
    • DOI 10.1038/ni1166
    • Danilova, N., Bussmann, J., Jekosch, K., and Steiner, L. A. (2005) The immunoglobulin heavy-chain locus in zebrafish: identification and expression of a previously unknown isotype, immunoglobulin Z. Nat. Immunol. 6, 295-302 (Pubitemid 41724767)
    • (2005) Nature Immunology , vol.6 , Issue.3 , pp. 295-302
    • Danilova, N.1    Bussmann, J.2    Jekosch, K.3    Steiner, L.A.4
  • 23
    • 18744371880 scopus 로고    scopus 로고
    • Discovery of a unique Ig heavy-chain (IgT) in rainbow trout: Implications for a distinctive B cell developmental pathway in teleost fish
    • DOI 10.1073/pnas.0500027102
    • Hansen, J. D., Landis, E. D., and Phillips, R. B. (2005) Discovery of a unique Ig heavy-chain isotype (IgT) in rainbow trout: Implications for a distinctive B cell developmental pathway in teleost fish. Proc. Natl. Acad. Sci. U. S. A. 102, 6919-6924 (Pubitemid 40675417)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.19 , pp. 6919-6924
    • Hansen, J.D.1    Landis, E.D.2    Phillips, R.B.3
  • 24
    • 1842298136 scopus 로고    scopus 로고
    • Microsites for immunoglobulin switch recombination breakpoints from Xenopus to mammals
    • DOI 10.1002/eji.1830271021
    • Mussmann, R., Courtet, M., Schwager, J., and Du Pasquier, L. (1997) Microsites for immunoglobulin switch recombination breakpoints from Xenopus to mammals. Eur. J. Immunol. 27, 2610-2619 (Pubitemid 27453851)
    • (1997) European Journal of Immunology , vol.27 , Issue.10 , pp. 2610-2619
    • Mussmann, R.1    Courtet, M.2    Schwager, J.3    Du, P.L.4
  • 25
    • 7444271524 scopus 로고    scopus 로고
    • Evolution of isotype switching
    • DOI 10.1016/j.smim.2004.08.005, PII S1044532304000387, The Evolution of Rearranging Receptor Families
    • Stavnezer, J., and Amemiya, C. T. (2004) Evolution of isotype switching. Semin. Immunol. 16, 257-275 (Pubitemid 39445624)
    • (2004) Seminars in Immunology , vol.16 , Issue.4 , pp. 257-275
    • Stavnezer, J.1    Amemiya, C.T.2
  • 28
    • 12744259733 scopus 로고    scopus 로고
    • Activation-induced deaminase: Controversies and open questions
    • Barreto, V. M., Ramiro, A. R., and Nussenzweig, M. C. (2005) Activation-induced deaminase: controversies and open questions. Trends Immunol. 26, 90-96
    • (2005) Trends Immunol. , vol.26 , pp. 90-96
    • Barreto, V.M.1    Ramiro, A.R.2    Nussenzweig, M.C.3
  • 29
    • 1642334586 scopus 로고    scopus 로고
    • Cloning and expression of the AID gene in the channel catfish
    • DOI 10.1016/j.dci.2004.01.002, PII S0145305X04000175
    • Saunders, H. L., and Magor, B. G. (2004) Cloning and expression of the AID gene in the channel catfish. Dev. Comp. Immunol. 28, 657-663 (Pubitemid 38388237)
    • (2004) Developmental and Comparative Immunology , vol.28 , Issue.7-8 , pp. 657-663
    • Saunders, H.L.1    Magor, B.G.2
  • 30
    • 4344654828 scopus 로고    scopus 로고
    • Identification of the activation-induced cytidine deaminase gene from zebrafish: An evolutionary analysis
    • Zhao, Y., Pan-Hammarstr√∂m, Q., Zhao, Z., and Hammarstr√∂m, L. (2005) Identification of the activation-induced cytidine deaminase gene from zebrafish: an evolutionary analysis. Devel. Comp. Immunol. 29, 61-71
    • (2005) Devel. Comp. Immunol. , vol.29 , pp. 61-71
    • Zhao, Y.1    Pan-Hammarstrm, Q.2    Zhao, Z.3    Hammarstrm, L.4
  • 31
    • 36849011485 scopus 로고    scopus 로고
    • Single-stranded DNA structure and positional context of the target cytidine determine the enzymatic efficiency of AID
    • DOI 10.1128/MCB.01046-07
    • Larijani, M., and Martin, A. (2007) Single-stranded DNA structure and positional context of the target cytidine determine the enzymatic efficiency of AID. Mol. Cell. Biol. 27, 8038-8048 (Pubitemid 350234221)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.23 , pp. 8038-8048
    • Larijani, M.1    Martin, A.2
  • 34
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • DOI 10.1038/nature06638, PII NATURE06638
    • Chen, K. M., Harjes, E., Gross, P. J., Fahmy, A., Lu, Y., Shindo, K., Harris, R. S., and Matsuo, H. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452, 116-119 (Pubitemid 351355093)
    • (2008) Nature , vol.452 , Issue.7183 , pp. 116-119
    • Chen, K.-M.1    Harjes, E.2    Gross, P.J.3    Fahmy, A.4    Lu, Y.5    Shindo, K.6    Harris, R.S.7    Matsuo, H.8
  • 35
    • 34249807921 scopus 로고    scopus 로고
    • DNA Deamination in Immunity: AID in the Context of Its APOBEC Relatives
    • DOI 10.1016/S0065-2776(06)94002-4, PII S0065277606940024, AID for Immunoglobulin Diversity
    • Conticello, S. G., Langlois, M. A., Yang, Z., and Neuberger, M. S. (2007) DNA deamination in immunity: AID in the context of its APOBEC relatives. Adv. Immunol. 94, 37-73 (Pubitemid 46856607)
    • (2007) Advances in Immunology , vol.94 , pp. 37-73
    • Conticello, S.G.1    Langlois, M.2    Yang, Z.3    Neuberger, M.S.4
  • 36
    • 33750975915 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase: Structure-function relationship as based on the study of mutants
    • DOI 10.1002/humu.20414
    • Durandy, A., Peron, S., Taubenheim, N., and Fischer, A. (2006) Activation-induced cytidine deaminase: structure-function relationship as based on the study of mutants. Hum. Mutat. 27, 1185-1191 (Pubitemid 44749720)
    • (2006) Human Mutation , vol.27 , Issue.12 , pp. 1185-1191
    • Durandy, A.1    Peron, S.2    Taubenheim, N.3    Fischer, A.4
  • 39
    • 0030749081 scopus 로고    scopus 로고
    • Cold-adapted enzymes
    • Marshall, C. J. (1997) Cold-adapted enzymes. Trends Biotechnol. 15, 359-364
    • (1997) Trends Biotechnol. , vol.15 , pp. 359-364
    • Marshall, C.J.1
  • 42
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G., and Gerday, C. (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1, 200-208
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 43
    • 32944477673 scopus 로고    scopus 로고
    • The evolution of adaptive immunity
    • Pancer, Z., and Cooper, M. D. (2006) The evolution of adaptive immunity. Annu. Rev. Immunol. 24, 497-518
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 497-518
    • Pancer, Z.1    Cooper, M.D.2
  • 44
    • 72849115174 scopus 로고    scopus 로고
    • Origin and evolution of the adaptive immune system: Genetic events and selective pressures
    • Flajnik, M. F., and Kasahara, M. (2010) Origin and evolution of the adaptive immune system: genetic events and selective pressures. Nat. Rev. Genet. 11, 47-59
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 47-59
    • Flajnik, M.F.1    Kasahara, M.2
  • 45
    • 79959348651 scopus 로고    scopus 로고
    • Evolutionary history of Otophysi (Teleostei), a major clade of the modern freshwater fishes: Pangaean origin and Mesozoic radiation
    • Nakatani, M., Miya, M., Mabuchi, K., Saitoh, K., and Nishida, M. (2011) Evolutionary history of Otophysi (Teleostei), a major clade of the modern freshwater fishes: Pangaean origin and Mesozoic radiation. BMC Evol. Biol. 11, 177
    • (2011) BMC Evol. Biol. , vol.11 , pp. 177
    • Nakatani, M.1    Miya, M.2    Mabuchi, K.3    Saitoh, K.4    Nishida, M.5
  • 46
    • 33646878378 scopus 로고    scopus 로고
    • Novel relationships among ten fish model species revealed based on a phylogenomic analysis using ESTs
    • DOI 10.1007/s00239-005-0170-8
    • Steinke, D., Salzburger, W., and Meyer, A. (2006) Novel relationships among ten fish model species revealed based on a phylogenomic analysis using ESTs. J. Mol. Evol. 62, 772-784 (Pubitemid 43847227)
    • (2006) Journal of Molecular Evolution , vol.62 , Issue.6 , pp. 772-784
    • Steinke, D.1    Salzburger, W.2    Meyer, A.3
  • 47
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • DOI 10.1038/nature05492, PII NATURE05492
    • Prochnow, C., Bransteitter, R., Klein, M. G., Goodman, M. F., and Chen, X. S. (2007) The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 445, 447-451 (Pubitemid 46160914)
    • (2007) Nature , vol.445 , Issue.7126 , pp. 447-451
    • Prochnow, C.1    Bransteitter, R.2    Klein, M.G.3    Goodman, M.F.4    Chen, X.S.5
  • 48
    • 4344700569 scopus 로고    scopus 로고
    • Replication protein A interacts with AID to promote deamination of somatic hypermutation targets
    • DOI 10.1038/nature02821
    • Chaudhuri, J., Khuong, C., and Alt, F. W. (2004) Replication protein A interacts with AID to promote deamination of somatic hypermutation targets. Nature 430, 992-998 (Pubitemid 39128379)
    • (2004) Nature , vol.430 , Issue.7003 , pp. 992-998
    • Chaudhuri, J.1    Khuong, C.2    Alt, F.W.3
  • 49
    • 53949103770 scopus 로고    scopus 로고
    • Evolution of phosphorylation- dependent regulation of activation-induced cytidine deaminase
    • Basu, U., Wang, Y., and Alt, F. W. (2008) Evolution of phosphorylation- dependent regulation of activation-induced cytidine deaminase. Mol. Cell. 32, 285-291
    • (2008) Mol. Cell. , vol.32 , pp. 285-291
    • Basu, U.1    Wang, Y.2    Alt, F.W.3


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