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Volumn 29, Issue , 2000, Pages 81-103

GCN5-related N-acetyltransferases: A structural overview

Author keywords

Acetyl coenzyme A; Aminoglycoside; GNAT; Histone acetylation; Melatonin

Indexed keywords

ACYLTRANSFERASE;

EID: 0033877252     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.29.1.81     Document Type: Review
Times cited : (399)

References (45)
  • 1
    • 0031788774 scopus 로고    scopus 로고
    • Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs
    • 1. Bhatnagar RS, Futterer K, Farazi TA, Korolev S, Murray CL, et al. 1998. Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs. Nat. Struct. Biol. 5:1091-97
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1091-1097
    • Bhatnagar, R.S.1    Futterer, K.2    Farazi, T.A.3    Korolev, S.4    Murray, C.L.5
  • 2
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
    • 2. Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R. 1999. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18:3521-32
    • (1999) EMBO J. , vol.18 , pp. 3521-3532
    • Clements, A.1    Rojas, J.R.2    Trievel, R.C.3    Wang, L.4    Berger, S.L.5    Marmorstein, R.6
  • 3
    • 0029593545 scopus 로고
    • Pineal serotonin N-acetyltransferase: Expression cloning and molecular analysis
    • 3. Coon SL, Roseboom PH, Baler R, Weller JL, Namboodiri MAA, et al. 1995. Pineal serotonin N-acetyltransferase: expression cloning and molecular analysis. Science 270:1681-83
    • (1995) Science , vol.270 , pp. 1681-1683
    • Coon, S.L.1    Roseboom, P.H.2    Baler, R.3    Weller, J.L.4    Namboodiri, M.A.A.5
  • 4
    • 0032579377 scopus 로고    scopus 로고
    • Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87)
    • 4. De Angelis J, Gastel J, Klein DC, Cole PA. 1998. Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87). J. Biol. Chem. 273:3045-50
    • (1998) J. Biol. Chem. , vol.273 , pp. 3045-3050
    • De Angelis, J.1    Gastel, J.2    Klein, D.C.3    Cole, P.A.4
  • 6
    • 0026648960 scopus 로고
    • Site-directed mutagenesis of recombinant human arylamine N-acetyltransferase expressed in Escherichia coli
    • 6. Dupret J, Grant DM. 1992. Site-directed mutagenesis of recombinant human arylamine N-acetyltransferase expressed in Escherichia coli. J. Biol. Chem. 267:7381-85
    • (1992) J. Biol. Chem. , vol.267 , pp. 7381-7385
    • Dupret, J.1    Grant, D.M.2
  • 7
    • 0032555689 scopus 로고    scopus 로고
    • Structure of the histone acetyltransferase Hat1: A paradigm for the GCN5-related N-acetyltransferase superfamily
    • 7. Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. 1998. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94:427-38
    • (1998) Cell , vol.94 , pp. 427-438
    • Dutnall, R.N.1    Tafrov, S.T.2    Sternglanz, R.3    Ramakrishnan, V.4
  • 8
    • 0030444352 scopus 로고    scopus 로고
    • The diverse world of coenzyme A binding proteins
    • 8. Engel C, Wierenga R. 1996. The diverse world of coenzyme A binding proteins. Curr. Opin. Struct. Biol. 6:790-97
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 790-797
    • Engel, C.1    Wierenga, R.2
  • 9
    • 0032570593 scopus 로고    scopus 로고
    • Melatonin production: Proteolysis in serotonin N-acetyltransferase regulation
    • 9. Gastel JA, Roseboom PH, Rinaldi PA, Weller JL, Klein DC. 1998. Melatonin production: proteolysis in serotonin N-acetyltransferase regulation. Science 279:1358-60
    • (1998) Science , vol.279 , pp. 1358-1360
    • Gastel, J.A.1    Roseboom, P.H.2    Rinaldi, P.A.3    Weller, J.L.4    Klein, D.C.5
  • 10
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • 10. Grunstein M. 1997. Histone acetylation in chromatin structure and transcription. Nature 389:349-52
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 11
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosyntheses: The structure of serotonin N-acetyltransferase at 2.5 Å resolution suggests a catalytic mechanism
    • 11. Hickman AB, Klein DC, Dyda F. 1999. Melatonin biosyntheses: the structure of serotonin N-acetyltransferase at 2.5 Å resolution suggests a catalytic mechanism. Mol. Cell. 3:23-32
    • (1999) Mol. Cell. , vol.3 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 12
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 Å resolution with a bisubstrate analog
    • 12. Hickman AB, Namboodiri MAA, Klein DC, Dyda F. 1999. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97:361-69
    • (1999) Cell , vol.97 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.A.2    Klein, D.C.3    Dyda, F.4
  • 13
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 13. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-19
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
    • 0031781177 scopus 로고    scopus 로고
    • A potent inhibitor of the melatonin rhythm enzyme
    • 14. Khalil EM, Cole PA. 1998. A potent inhibitor of the melatonin rhythm enzyme. J. Am. Chem. Soc. 120:6195-96
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6195-6196
    • Khalil, E.M.1    Cole, P.A.2
  • 15
    • 0032514895 scopus 로고    scopus 로고
    • Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase
    • 15. Khalil EM, De Angelis J, Cole PA. 1998. Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase. J. Biol. Chem. 273:30321-27
    • (1998) J. Biol. Chem. , vol.273 , pp. 30321-30327
    • Khalil, E.M.1    De Angelis, J.2    Cole, P.A.3
  • 16
    • 0030626244 scopus 로고    scopus 로고
    • The melatonin rhythm-generating enzyme: Molecular regulation of serotonin N-acetyltransferase in the pineal gland
    • 16. Klein DC, Coon SL, Roseboom PH, Weller JL, Bernard M, et al. 1997. The melatonin rhythm-generating enzyme: molecular regulation of serotonin N-acetyltransferase in the pineal gland. Recent Prog. Horm. Res. 52:307-58
    • (1997) Recent Prog. Horm. Res. , vol.52 , pp. 307-358
    • Klein, D.C.1    Coon, S.L.2    Roseboom, P.H.3    Weller, J.L.4    Bernard, M.5
  • 17
    • 0015502984 scopus 로고
    • Rapid light induced decrease in pineal serotonin N-acetyltransferase activity
    • 17. Klein DC, Weller JL. 1972. Rapid light induced decrease in pineal serotonin N-acetyltransferase activity. Science 177:532-33
    • (1972) Science , vol.177 , pp. 532-533
    • Klein, D.C.1    Weller, J.L.2
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 18. Kraulis PJ. 1991.MOLSCRIPT: aprogram to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-50
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0007715651 scopus 로고
    • Structure of chloramphenicol acetyltransferase at 1.75 Å resolution
    • 19. Leslie AGW, Moody PCE, Shaw VW. 1988. Structure of chloramphenicol acetyltransferase at 1.75 Å resolution. Proc. Natl. Acad. Sci. USA 85:4133-37
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4133-4137
    • Leslie, A.G.W.1    Moody, P.C.E.2    Shaw, V.W.3
  • 20
    • 0033168497 scopus 로고    scopus 로고
    • Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A
    • 20. Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G. 1999. Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Nature 400:86-89
    • (1999) Nature , vol.400 , pp. 86-89
    • Lin, Y.1    Fletcher, C.M.2    Zhou, J.3    Allis, C.D.4    Wagner, G.5
  • 21
    • 0032906633 scopus 로고    scopus 로고
    • p53 Sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage
    • 21. Liu L, Scolnick DM, Trievel RC, Zhang HB, Marmorstein R, et al. 1999. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol. Cell. Biol. 19:1202-9
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1202-1209
    • Liu, L.1    Scolnick, D.M.2    Trievel, R.C.3    Zhang, H.B.4    Marmorstein, R.5
  • 23
    • 0027157439 scopus 로고
    • Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 Å resolution
    • 23. Mattevi A, Obmolova G, Kalk KH, Westphal AH, de Kok A, Hol WGJ. 1993. Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 Å resolution. J. Mol. Biol. 230:1183-99
    • (1993) J. Mol. Biol. , vol.230 , pp. 1183-1199
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Westphal, A.H.4    De Kok, A.5    Hol, W.G.J.6
  • 24
    • 0003601534 scopus 로고
    • Rahway, NJ: Merck & Co. 9th ed.
    • 24. Merck Index. 1976. p. 1095. Rahway, NJ: Merck & Co. 9th ed.
    • (1976) Merck Index , pp. 1095
  • 25
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • 25. Meyer E. 1992. Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications. Protein Sci. 1:1543-62
    • (1992) Protein Sci. , vol.1 , pp. 1543-1562
    • Meyer, E.1
  • 26
    • 0032898932 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis
    • 26. Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H. 1999. Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. J. Biol. Chem. 274:424-29
    • (1999) J. Biol. Chem. , vol.274 , pp. 424-429
    • Mio, T.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 27
    • 0031964479 scopus 로고    scopus 로고
    • Linking histone acetylation to transcriptional regulation
    • 27. Mizzen CA, Allis CD. 1998. Linking histone acetylation to transcriptional regulation. Cell. Mol. Life Sci. 54:6-20
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 6-20
    • Mizzen, C.A.1    Allis, C.D.2
  • 28
    • 0032534050 scopus 로고    scopus 로고
    • Two crystal structures of N-acetyltransferases reveal a new fold for CoA-dependent enzymes
    • 28. Modis Y, Wierenga R. 1998. Two crystal structures of N-acetyltransferases reveal a new fold for CoA-dependent enzymes. Structure 6:1345-50
    • (1998) Structure , vol.6 , pp. 1345-1350
    • Modis, Y.1    Wierenga, R.2
  • 29
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • 29. Murzin AG, Brenner SE, Hubbard T, Chothia C. 1995. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:536-40
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 30
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • 30. Neuwald AF, Landsman D. 1997. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:154-55
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 32
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • 32. Rao ST, Rossman MG. 1973. Comparison of super-secondary structures in proteins. J. Mol. Biol. 76:241-56
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossman, M.G.2
  • 33
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • 33. Richardson JS. 1981. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34:167-330
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-330
    • Richardson, J.S.1
  • 34
    • 0033517354 scopus 로고    scopus 로고
    • Crystal structure of Tetrahymena GCN5 with bound coenzyme-A and histone H3 peptide
    • 34. Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, et al. 1999. Crystal structure of Tetrahymena GCN5 with bound coenzyme-A and histone H3 peptide. Nature 401:93-98
    • (1999) Nature , vol.401 , pp. 93-98
    • Rojas, J.R.1    Trievel, R.C.2    Zhou, J.3    Mo, Y.4    Li, X.5
  • 35
    • 0033529962 scopus 로고    scopus 로고
    • Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases
    • 35. Sternglanz R, Schindelin H. 1999. Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases. Proc. Natl. Acad. Sci. USA 96:8807-8
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8807-8808
    • Sternglanz, R.1    Schindelin, H.2
  • 36
    • 0004155427 scopus 로고
    • New York: Freeman. 3rd ed.
    • 36. Stryer L. 1988. Biochemistry, p. 21. New York: Freeman. 3rd ed.
    • (1988) Biochemistry , pp. 21
    • Stryer, L.1
  • 37
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • 37. Tanner KG, Trievel RC, Kuo M, Howard RM, Berger SL, et al. 1999. Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. J. Biol. Chem. 274:18157-60
    • (1999) J. Biol. Chem. , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Kuo, M.3    Howard, R.M.4    Berger, S.L.5
  • 38
    • 0026730661 scopus 로고
    • Localized mutagenesis and evidence for post-transcriptional regulation of MAK3
    • 38. Tercero JC, Riles LE, Wickner RB. 1992. Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. J. Biol. Chem. 267:20270-76
    • (1992) J. Biol. Chem. , vol.267 , pp. 20270-20276
    • Tercero, J.C.1    Riles, L.E.2    Wickner, R.B.3
  • 39
    • 0033529845 scopus 로고    scopus 로고
    • Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
    • 39. Trievel RC, Rojas JR, Sterner DE, Venkataramani RN, Wang L, et al. 1999. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. USA 96:8931-36
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8931-8936
    • Trievel, R.C.1    Rojas, J.R.2    Sterner, D.E.3    Venkataramani, R.N.4    Wang, L.5
  • 40
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • 40. Wang L, Liu L, Berger SL. 1998. Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev. 12:640-53
    • (1998) Genes Dev. , vol.12 , pp. 640-653
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 41
    • 0026611267 scopus 로고
    • Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium
    • 41. Watanabe M, Sofuni T, Nohmi T. 1992. Involvement of Cys69 residue in the catalytic mechanism of N-hydroxyarylamine O-acetyltransferase of Salmonella typhimurium. J. Biol. Chem. 267:8429-36
    • (1992) J. Biol. Chem. , vol.267 , pp. 8429-8436
    • Watanabe, M.1    Sofuni, T.2    Nohmi, T.3
  • 43
    • 0032555691 scopus 로고    scopus 로고
    • Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
    • 43. Wolf E, Vassilev A, Makino Y, Sali A, Nakatani Y, Burley SK. 1998. Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell 94:439-49
    • (1998) Cell , vol.94 , pp. 439-449
    • Wolf, E.1    Vassilev, A.2    Makino, Y.3    Sali, A.4    Nakatani, Y.5    Burley, S.K.6
  • 44
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5 Å resolution
    • 44. Wolodko WT, Fraser ME, James MNG, Bridger WA. 1994. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5 Å resolution. J. Biol. Chem. 269:10883-90
    • (1994) J. Biol. Chem. , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.G.3    Bridger, W.A.4
  • 45
    • 0033135707 scopus 로고    scopus 로고
    • Crystal structure of an aminoglycoside 6′-N-acetyltransferase: Defining the GCN5-related N-acetyltransferase superfamily fold
    • 45. Wybenga-Groot LE, Draker K, Wright GD, Berghuis AM. 1999. Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7:497-507
    • (1999) Structure , vol.7 , pp. 497-507
    • Wybenga-Groot, L.E.1    Draker, K.2    Wright, G.D.3    Berghuis, A.M.4


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