메뉴 건너뛰기




Volumn 46, Issue 8, 2007, Pages 2091-2099

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE (HAT) COMPLEXES; HISTONE-FOLD DOMAIN (HFD) REGIONS; PICCOLO NUA4 (PICNUA4); TETRA-ACETYLATES;

EID: 33847655626     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602366n     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • Carrozza, M. J., Utley, R. T., Workman, J. L., and Cote, J. (2003) The diverse functions of histone acetyltransferase complexes, Trends Genet. 19, 321-329.
    • (2003) Trends Genet , vol.19 , pp. 321-329
    • Carrozza, M.J.1    Utley, R.T.2    Workman, J.L.3    Cote, J.4
  • 2
    • 0035097883 scopus 로고    scopus 로고
    • The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition,
    • 2
    • Akhtar, A., and Becker, P. B. (2001) The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition, EMBO Rep. 2, 113-118.
    • (2001) EMBO Rep , pp. 113-118
    • Akhtar, A.1    Becker, P.B.2
  • 3
    • 17044365726 scopus 로고    scopus 로고
    • Nucleosome and chromatin fiber dynamics
    • Luger, K., and Hansen, J. C. (2005) Nucleosome and chromatin fiber dynamics, Curr. Opin. Struct. Biol. 15, 188-196.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 188-196
    • Luger, K.1    Hansen, J.C.2
  • 4
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • Marmorstein, R., and Roth, S. Y. (2001) Histone acetyltransferases: Function, structure, and catalysis, Curr. Opin. Genet. Dev. 11, 155-161.
    • (2001) Curr. Opin. Genet. Dev , vol.11 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 5
    • 0141994824 scopus 로고    scopus 로고
    • Perturbations of chromatin structure in human genetic disease: Recent advances
    • Bickmore, W. A., and van der Maarel, S. M. (2003) Perturbations of chromatin structure in human genetic disease: Recent advances, Hum. Mol. Genet. 12, R207-R213.
    • (2003) Hum. Mol. Genet , vol.12
    • Bickmore, W.A.1    van der Maarel, S.M.2
  • 6
    • 0031876314 scopus 로고    scopus 로고
    • Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III
    • Tse, C., Sera, T., Wolffe, A. P., and Hansen, J. C. (1998) Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III, Mol. Cell. Biol. 18, 4629-4638.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4629-4638
    • Tse, C.1    Sera, T.2    Wolffe, A.P.3    Hansen, J.C.4
  • 7
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V. G., Faulkner, R., and Mirsky, A. E. (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis, Proc. Natl. Acad. Sci. U.S.A. 51, 786-794.
    • (1964) Proc. Natl. Acad. Sci. U.S.A , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 10
    • 1942439646 scopus 로고    scopus 로고
    • The highly conserved and multifunctional NuA4 HAT complex
    • Doyon, Y., and Cote, J. (2004) The highly conserved and multifunctional NuA4 HAT complex, Curr. Opin. Genet. Dev. 14, 147-154.
    • (2004) Curr. Opin. Genet. Dev , vol.14 , pp. 147-154
    • Doyon, Y.1    Cote, J.2
  • 11
    • 0347481147 scopus 로고    scopus 로고
    • Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and non-histone substrates
    • Poux, A. N., and Marmorstein, R. (2003) Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and non-histone substrates, Biochemistry 42, 14366-14374.
    • (2003) Biochemistry , vol.42 , pp. 14366-14374
    • Poux, A.N.1    Marmorstein, R.2
  • 13
    • 0034515772 scopus 로고    scopus 로고
    • Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase
    • Reid, J. L., Iyer, V. R., Brown, P. O., and Struhl, K. (2000) Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase, Mol. Cell 6, 1297-1307.
    • (2000) Mol. Cell , vol.6 , pp. 1297-1307
    • Reid, J.L.1    Iyer, V.R.2    Brown, P.O.3    Struhl, K.4
  • 15
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • Doyon, Y., Selleck, W., Lane, W. S., Tan, S., and Cote, J. (2004) Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans, Mol. Cell. Biol. 24, 1884-1896.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 16
    • 33645224956 scopus 로고    scopus 로고
    • Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae
    • Durant, M., and Pugh, B. F. (2006) Genome-wide relationships between TAF1 and histone acetyltransferases in Saccharomyces cerevisiae, Mol. Cell. Biol. 26, 2791-2802.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2791-2802
    • Durant, M.1    Pugh, B.F.2
  • 17
    • 0141992114 scopus 로고    scopus 로고
    • Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase
    • Clements, A., Poux, A. N., Lo, W. S., Pillus, L., Berger, S. L., and Marmorstein, R. (2003) Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase, Mol. Cell 12, 461-473.
    • (2003) Mol. Cell , vol.12 , pp. 461-473
    • Clements, A.1    Poux, A.N.2    Lo, W.S.3    Pillus, L.4    Berger, S.L.5    Marmorstein, R.6
  • 19
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and Allis, C. D. (2000) The language of covalent histone modifications, Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 20
    • 24344481673 scopus 로고    scopus 로고
    • Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4
    • Utley, R. T., Lacoste, N., Jobin-Robitaille, O., Allard, S., and Cote, J. (2005) Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4, Mol. Cell. Biol. 25, 8179-8190.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8179-8190
    • Utley, R.T.1    Lacoste, N.2    Jobin-Robitaille, O.3    Allard, S.4    Cote, J.5
  • 21
    • 20744445493 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the enhancer of polycomb A domain and chromodomain to acetylate nucleosomes
    • Selleck, W., Fortin, I., Sermwittayawong, D., Cote, J., and Tan, S. (2005) The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the enhancer of polycomb A domain and chromodomain to acetylate nucleosomes, Mol. Cell. Biol. 25, 5535-5542.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 5535-5542
    • Selleck, W.1    Fortin, I.2    Sermwittayawong, D.3    Cote, J.4    Tan, S.5
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 14844303376 scopus 로고    scopus 로고
    • The pST44 polycistronic expression system for producing protein complexes in Escherichia coli
    • Tan, S., Kern, R. C., and Selleck, W. (2005) The pST44 polycistronic expression system for producing protein complexes in Escherichia coli, Protein Expression Purif. 40, 385-395.
    • (2005) Protein Expression Purif , vol.40 , pp. 385-395
    • Tan, S.1    Kern, R.C.2    Selleck, W.3
  • 24
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger, K., Rechsteiner, T. J., and Richmond, T. J. (1999) Expression and purification of recombinant histones and nucleosome reconstitution, Methods Mol. Biol. 119, 1-16.
    • (1999) Methods Mol. Biol , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 25
    • 0033067219 scopus 로고    scopus 로고
    • Assembly of defined nucleosomal and chromatin arrays from pure components
    • Carruthers, L. M., Tse, C., Walker, K. P., III, and Hansen, J. C. (1999) Assembly of defined nucleosomal and chromatin arrays from pure components, Methods Enzymol. 304, 19-35.
    • (1999) Methods Enzymol , vol.304 , pp. 19-35
    • Carruthers, L.M.1    Tse, C.2    Walker III, K.P.3    Hansen, J.C.4
  • 26
    • 23944525341 scopus 로고    scopus 로고
    • Assays for mechanistic investigations of protein/histone acetyltransferases
    • Berndsen, C. E., and Denu, J. M. (2005) Assays for mechanistic investigations of protein/histone acetyltransferases, Methods 36, 321-331.
    • (2005) Methods , vol.36 , pp. 321-331
    • Berndsen, C.E.1    Denu, J.M.2
  • 27
    • 0018722047 scopus 로고
    • Kinetic analysis of progress curves
    • Orsi, B. A., and Tipton, K. F. (1979) Kinetic analysis of progress curves, Methods Enzymol. 63, 159-183.
    • (1979) Methods Enzymol , vol.63 , pp. 159-183
    • Orsi, B.A.1    Tipton, K.F.2
  • 28
    • 0032953154 scopus 로고    scopus 로고
    • Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds
    • Kaiser, R., and Metzka, L. (1999) Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds, Anal. Biochem. 266, 1-8.
    • (1999) Anal. Biochem , vol.266 , pp. 1-8
    • Kaiser, R.1    Metzka, L.2
  • 31
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke, A. S., Lowell, J. E., Jacobson, S. J., and Pillus, L. (1999) Esa1p is an essential histone acetyltransferase required for cell cycle progression, Mol. Cell. Biol. 19, 2515-2526.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 32
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard, S., Utley, R. T., Savard, J., Clarke, A., Grant, P., Brandl, C. J., Pillus, L., Workman, J. L., and Cote, J. (1999) NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p, EMBO J. 18, 5108-5119.
    • (1999) EMBO J , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5    Brandl, C.J.6    Pillus, L.7    Workman, J.L.8    Cote, J.9
  • 33
    • 0032558998 scopus 로고    scopus 로고
    • Structure and function of the core histone N-termini: More than meets the eye
    • Hansen, J. C., Tse, C., and Wolffe, A. P. (1998) Structure and function of the core histone N-termini: More than meets the eye, Biochemistry 37, 17637-17641.
    • (1998) Biochemistry , vol.37 , pp. 17637-17641
    • Hansen, J.C.1    Tse, C.2    Wolffe, A.P.3
  • 34
    • 26644471508 scopus 로고    scopus 로고
    • The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays
    • Gordon, F., Luger, K., and Hansen, J. C. (2005) The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays, J. Biol. Chem. 280, 33701-33706.
    • (2005) J. Biol. Chem , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 35
    • 0027412701 scopus 로고
    • Assembly and structural properties of subsaturated chromatin arrays
    • Hansen, J. C., and Lohr, D. (1993) Assembly and structural properties of subsaturated chromatin arrays, J. Biol. Chem. 268, 5840-5848.
    • (1993) J. Biol. Chem , vol.268 , pp. 5840-5848
    • Hansen, J.C.1    Lohr, D.2
  • 36
    • 0024462713 scopus 로고
    • Analysis of histone subtypes and their modified forms by polyacrylamide gel electrophoresis
    • Lennox, R. W., and Cohen, L. H. (1989) Analysis of histone subtypes and their modified forms by polyacrylamide gel electrophoresis, Methods Enzymol. 170, 532-549.
    • (1989) Methods Enzymol , vol.170 , pp. 532-549
    • Lennox, R.W.1    Cohen, L.H.2
  • 37
    • 0034780285 scopus 로고    scopus 로고
    • Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex
    • Nourani, A., Doyon, Y., Utley, R. T., Allard, S., Lane, W. S., and Cote, J. (2001) Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex, Mol. Cell. Biol. 21, 7629-7640.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 7629-7640
    • Nourani, A.1    Doyon, Y.2    Utley, R.T.3    Allard, S.4    Lane, W.S.5    Cote, J.6
  • 38
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution, Nature 389, 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
  • 39
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson, B. P., Martinez-Yamout, M. A., Dyson, H. J., and Wright, P. E. (2000) Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain, J. Mol. Biol. 304, 355-370.
    • (2000) J. Mol. Biol , vol.304 , pp. 355-370
    • Hudson, B.P.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 40
    • 0033635283 scopus 로고    scopus 로고
    • Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases
    • Yan, Y., Barlev, N. A., Haley, R. H., Berger, S. L., and Marmorstein, R. (2000) Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases, Mol. Cell 6, 1195-1205.
    • (2000) Mol. Cell , vol.6 , pp. 1195-1205
    • Yan, Y.1    Barlev, N.A.2    Haley, R.H.3    Berger, S.L.4    Marmorstein, R.5
  • 41
    • 0036830560 scopus 로고    scopus 로고
    • The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate
    • Yan, Y., Harper, S., Speicher, D. W., and Marmorstein, R. (2002) The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate, Nat. Struct. Biol. 9, 862-869.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 862-869
    • Yan, Y.1    Harper, S.2    Speicher, D.W.3    Marmorstein, R.4
  • 42
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • Tanner, K. G., Trievel, R. C., Kuo, M. H., Howard, R. M., Berger, S. L., Allis, C. D., Marmorstein, R., and Denu, J. M. (1999) Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator, J. Biol. Chem. 274, 18157-18160.
    • (1999) J. Biol. Chem , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Kuo, M.H.3    Howard, R.M.4    Berger, S.L.5    Allis, C.D.6    Marmorstein, R.7    Denu, J.M.8
  • 43
    • 0034698085 scopus 로고    scopus 로고
    • Kinetic mechanism of the histone acetyltransferase GCN5 from yeast
    • Tanner, K. G., Langer, M. R., Kim, Y., and Denu, J. M. (2000) Kinetic mechanism of the histone acetyltransferase GCN5 from yeast, J. Biol. Chem. 275, 22048-22055.
    • (2000) J. Biol. Chem , vol.275 , pp. 22048-22055
    • Tanner, K.G.1    Langer, M.R.2    Kim, Y.3    Denu, J.M.4
  • 44
    • 0035823497 scopus 로고    scopus 로고
    • Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
    • Thompson, P. R., Kurooka, H., Nakatani, Y., and Cole, P. A. (2001) Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity, J. Biol. Chem. 276, 33721-33729.
    • (2001) J. Biol. Chem , vol.276 , pp. 33721-33729
    • Thompson, P.R.1    Kurooka, H.2    Nakatani, Y.3    Cole, P.A.4
  • 45
    • 0033590107 scopus 로고    scopus 로고
    • Sas3 is a histone acetyl-transferase and requires a zinc finger motif
    • Takechi, S., and Nakayama, T. (1999) Sas3 is a histone acetyl-transferase and requires a zinc finger motif, Biochem. Biophys. Res. Commun. 266, 405-410.
    • (1999) Biochem. Biophys. Res. Commun , vol.266 , pp. 405-410
    • Takechi, S.1    Nakayama, T.2
  • 47
    • 0037837745 scopus 로고    scopus 로고
    • Tip60 is a co-repressor for STAT3
    • Xiao, H., Chung, J., Kao, H. Y., and Yang, Y. C. (2003) Tip60 is a co-repressor for STAT3, J. Biol. Chem. 278, 11197-11204.
    • (2003) J. Biol. Chem , vol.278 , pp. 11197-11204
    • Xiao, H.1    Chung, J.2    Kao, H.Y.3    Yang, Y.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.