메뉴 건너뛰기




Volumn 330, Issue 3, 2003, Pages 503-511

The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A

Author keywords

Crystal structure; Histone macroH2A; P loop nucleotide hydrolases; RNA binding; X chromosome inactivation

Indexed keywords

CYTOSOL AMINOPEPTIDASE; HYDROLASE; PROTEIN; PROTEIN AF 1521; UNCLASSIFIED DRUG;

EID: 0038047136     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00473-X     Document Type: Article
Times cited : (107)

References (48)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Angstrom resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Angstrom resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 0035685516 scopus 로고    scopus 로고
    • Histone variants and histone modifications: A structural perspective
    • Ausio J., Abbott D.W., Wang X.Y., Moore S.C. Histone variants and histone modifications: a structural perspective. Biochem. Cell Biol. 79:2001;693-708.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 693-708
    • Ausio, J.1    Abbott, D.W.2    Wang, X.Y.3    Moore, S.C.4
  • 4
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • Pehrson J.R., Fried V.A. MacroH2A, a core histone containing a large nonhistone region. Science. 257:1992;1398-1400.
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 5
    • 0035877759 scopus 로고    scopus 로고
    • MACROH2A2, a new member of the MACROH2A core histone family
    • Costanzi C., Pehrson J.R. MACROH2A2, a new member of the MACROH2A core histone family. J. Biol. Chem. 276:2001;21776-21784.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21776-21784
    • Costanzi, C.1    Pehrson, J.R.2
  • 6
    • 0035336967 scopus 로고    scopus 로고
    • Histone H2A variants and the inactive X chromosome: Identification of a second macroH2A variant
    • Chadwick B.P., Willard H.F. Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant. Hum. Mol. Genet. 10:2001;1101-1113.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1101-1113
    • Chadwick, B.P.1    Willard, H.F.2
  • 7
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi C., Pehrson J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature. 393:1998;599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 9
    • 0035473989 scopus 로고    scopus 로고
    • Forty years of decoding the silence in X-chromosome inactivation
    • Boumil R.M., Lee J.T. Forty years of decoding the silence in X-chromosome inactivation. Hum. Mol. Genet. 10:2001;2225-2232.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2225-2232
    • Boumil, R.M.1    Lee, J.T.2
  • 10
    • 0026489906 scopus 로고
    • The product of the mouse Xist gene is a 15 Kb inactive X-specific transcript containing no conserved ORF and located in the nucleus
    • Brockdorff N., Ashworth A., Kay G.F., McCabe V.M., Norris D.P., Cooper P.J., et al. The product of the mouse Xist gene is a 15 Kb inactive X-specific transcript containing no conserved ORF and located in the nucleus. Cell. 71:1992;515-526.
    • (1992) Cell , vol.71 , pp. 515-526
    • Brockdorff, N.1    Ashworth, A.2    Kay, G.F.3    McCabe, V.M.4    Norris, D.P.5    Cooper, P.J.6
  • 11
    • 0026456701 scopus 로고
    • The human Xist gene - Analysis of a 17 Kb inactive X-specific RNA that contains conserved repeats and is highly localized within the nucleus
    • Brown C.J., Hendrich B.D., Rupert J.L., Lafreniere R.G., Xing Y., Lawrence J., Willard H.F. The human Xist gene - analysis of a 17 Kb inactive X-specific RNA that contains conserved repeats and is highly localized within the nucleus. Cell. 71:1992;527-542.
    • (1992) Cell , vol.71 , pp. 527-542
    • Brown, C.J.1    Hendrich, B.D.2    Rupert, J.L.3    Lafreniere, R.G.4    Xing, Y.5    Lawrence, J.6    Willard, H.F.7
  • 12
    • 0036532224 scopus 로고    scopus 로고
    • X-chromosome inactivation and the search for chromosome-wide silencers
    • Cohen D.E., Lee J.T. X-chromosome inactivation and the search for chromosome-wide silencers. Curr. Opin. Genet. Dev. 12:2002;219-224.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 219-224
    • Cohen, D.E.1    Lee, J.T.2
  • 13
    • 0032805149 scopus 로고    scopus 로고
    • Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation
    • Csankovszki G., Panning B., Bates B., Pehrson J.R., Jaenisch R. Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation. Nature Genet. 22:1999;323-324.
    • (1999) Nature Genet. , vol.22 , pp. 323-324
    • Csankovszki, G.1    Panning, B.2    Bates, B.3    Pehrson, J.R.4    Jaenisch, R.5
  • 14
    • 0032526621 scopus 로고    scopus 로고
    • Evolutionary conservation of histone macroH2A subtypes and domains
    • Pehrson J.R., Fuji R.N. Evolutionary conservation of histone macroH2A subtypes and domains. Nucl. Acids Res. 26:1998;2837-2842.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 2837-2842
    • Pehrson, J.R.1    Fuji, R.N.2
  • 15
    • 0035338814 scopus 로고    scopus 로고
    • The WWE domain: A common interaction module in protein ubiquitination and ADP ribosylation
    • Aravind L. The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Trends Biochem. Sci. 26:2001;273-275.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 273-275
    • Aravind, L.1
  • 16
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • Aguiar R.C.T., Yakushijin Y., Kharbanda S., Salgia R., Fletcher J.A., Shipp M.A. BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood. 96:2000;4328-4334.
    • (2000) Blood , vol.96 , pp. 4328-4334
    • Aguiar, R.C.T.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5    Shipp, M.A.6
  • 18
    • 0027234403 scopus 로고
    • An NAD derivative produced during transfer-RNA splicing - ADP-ribose 1″-2″ cyclic phosphate
    • Culver G.M., McCraith S.M., Zillmann M., Kierzek R., Michaud N., Lareau R.D., et al. An NAD derivative produced during transfer-RNA splicing - ADP-ribose 1″-2″ cyclic phosphate. Science. 261:1993;206-208.
    • (1993) Science , vol.261 , pp. 206-208
    • Culver, G.M.1    McCraith, S.M.2    Zillmann, M.3    Kierzek, R.4    Michaud, N.5    Lareau, R.D.6
  • 19
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell. 94:1998;525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 20
    • 0026584599 scopus 로고
    • Structure of the RecA protein-ADP complex
    • Story R.M., Steitz T.A. Structure of the RecA protein-ADP complex. Nature. 355:1992;374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 21
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story R.M., Li H., Abelson J.N. Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc. Natl Acad. Sci. USA. 98:2001;1465-1470.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 22
    • 0028114231 scopus 로고
    • Structure at 2.8-Angstrom resolution of F1-ATPase from bovine heart-mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E. Structure at 2.8-Angstrom resolution of F1-ATPase from bovine heart-mitochondria. Nature. 370:1994;621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 23
    • 0035895343 scopus 로고    scopus 로고
    • Three-dimensional structure of ATP: Corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP
    • Bauer C.B., Fonseca M.V., Holden H.M., Thoden J.B., Thompson T.B., Escalante-Semerena J.C., Rayment I. Three-dimensional structure of ATP: corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP. Biochemistry. 40:2001;361-374.
    • (2001) Biochemistry , vol.40 , pp. 361-374
    • Bauer, C.B.1    Fonseca, M.V.2    Holden, H.M.3    Thoden, J.B.4    Thompson, T.B.5    Escalante-Semerena, J.C.6    Rayment, I.7
  • 24
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-subunits and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha-subunits and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 25
    • 0028871926 scopus 로고
    • Dali - A network tool for protein-structure comparison
    • Holm L., Sander C. Dali - a network tool for protein-structure comparison. Trends Biochem. Sci. 20:1995;478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 27
    • 0344931801 scopus 로고    scopus 로고
    • X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination
    • Strater N., Sherratt D.J., Colloms S.D. X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination. EMBO J. 18:1999;4513-4522.
    • (1999) EMBO J. , vol.18 , pp. 4513-4522
    • Strater, N.1    Sherratt, D.J.2    Colloms, S.D.3
  • 30
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342:1999;249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 31
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin A., Stewart D., Spradling A.C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 16:2002;2108-2119.
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 32
    • 0032925999 scopus 로고    scopus 로고
    • Reduced levels of poly(ADP-ribosyl)ation result in chromatin compaction and hypermethylation as shown by cell-by-cell computer-assisted quantitative analysis
    • De Capoa A., Febbo F.R., Giovannelli F., Niveleau A., Zardo G., Marenzi S., Caiafa P. Reduced levels of poly(ADP-ribosyl)ation result in chromatin compaction and hypermethylation as shown by cell-by-cell computer-assisted quantitative analysis. FASEB J. 13:1999;89-93.
    • (1999) FASEB J. , vol.13 , pp. 89-93
    • De Capoa, A.1    Febbo, F.R.2    Giovannelli, F.3    Niveleau, A.4    Zardo, G.5    Marenzi, S.6    Caiafa, P.7
  • 33
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic L., Vodenicharov M., Affar E.B., Poirier G.G. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Expt. Cell Res. 268:2001;7-13.
    • (2001) Expt. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 34
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 37
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D. 56:2000;965-972.
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 40
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 42
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of Hidden Markov Models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., Chothia C. Assignment of homology to genome sequences using a library of Hidden Markov Models that represent all proteins of known structure. J. Mol. Biol. 313:2001;903-919.
    • (2001) J. Mol. Biol. , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 45
    • 0032970896 scopus 로고    scopus 로고
    • Isolation of 10 differentially expressed cDNAs in differentiated Neuro2a cells induced through controlled expression of the GD3 synthase gene
    • Liu H., Nakagawa T., Kanematsu T., Uchida T., Tsuji S. Isolation of 10 differentially expressed cDNAs in differentiated Neuro2a cells induced through controlled expression of the GD3 synthase gene. J. Neurochem. 72:1999;1781-1790.
    • (1999) J. Neurochem. , vol.72 , pp. 1781-1790
    • Liu, H.1    Nakagawa, T.2    Kanematsu, T.3    Uchida, T.4    Tsuji, S.5
  • 46
    • 0033602422 scopus 로고    scopus 로고
    • Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling
    • Aravind L., Neuwald A.F., Ponting C.P. Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling. Curr. Biol. 9:1999;195-197.
    • (1999) Curr. Biol. , vol.9 , pp. 195-197
    • Aravind, L.1    Neuwald, A.F.2    Ponting, C.P.3
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.