메뉴 건너뛰기




Volumn 19, Issue 5, 1999, Pages 3466-3473

Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOME PROTEIN; HISTONE ACETYLTRANSFERASE; NUCLEAR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0032933141     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.5.3466     Document Type: Article
Times cited : (84)

References (53)
  • 1
    • 0028274720 scopus 로고
    • The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits
    • Alfonso, P. J., M. P. Crippa, J. J. Hayes, and M. Bustin. 1994. The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits. J. Mol. Biol. 236:189-198.
    • (1994) J. Mol. Biol. , vol.236 , pp. 189-198
    • Alfonso, P.J.1    Crippa, M.P.2    Hayes, J.J.3    Bustin, M.4
  • 2
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V. G., R. Faulkner, and A. E. Mirsky. 1964. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 51:786-794.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 3
    • 0032055036 scopus 로고    scopus 로고
    • Transcription of chromatin: These are complex times
    • Armstrong, J. A., and B. M. Emerson. 1998. Transcription of chromatin: these are complex times. Curr. Opin. Genet. Dev. 8:165-172.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 165-172
    • Armstrong, J.A.1    Emerson, B.M.2
  • 4
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyze the role of histone "tails" in the stabilization of nucleosomes
    • Ausio, J., F. Dong, and K. E. van Holde. 1989. Use of selectively trypsinized nucleosome core particles to analyze the role of histone "tails" in the stabilization of nucleosomes. J. Mol. Biol. 206:451-463.
    • (1989) J. Mol. Biol. , vol.206 , pp. 451-463
    • Ausio, J.1    Dong, F.2    Van Holde, K.E.3
  • 5
    • 0029953722 scopus 로고    scopus 로고
    • Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
    • Braunstein, M., R. E. Sobel, C. D. Allis, B. M. Turner, and J. R. Broach. 1996. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16:4349-4356.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4349-4356
    • Braunstein, M.1    Sobel, R.E.2    Allis, C.D.3    Turner, B.M.4    Broach, J.R.5
  • 6
    • 0029049102 scopus 로고
    • An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei
    • Brownell, J. E., and C. D. Allis. 1995. An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc. Natl. Acad. Sci. USA 92:6364-6368.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6364-6368
    • Brownell, J.E.1    Allis, C.D.2
  • 7
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • Brownell, J. E., and C. D. Allis. 1996. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev. 6:176-184.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 8
    • 0015861257 scopus 로고
    • Arrangement of histones in chromatin
    • Bustin, M. 1973. Arrangement of histones in chromatin. Nat. New Biol. 245:207-209.
    • (1973) Nat. New Biol. , vol.245 , pp. 207-209
    • Bustin, M.1
  • 9
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin, M., D. A. Lehn, and D. Landsman, 1990. Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049: 231-243.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 10
    • 0030358586 scopus 로고    scopus 로고
    • High mobility group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M., and R. Reeves. 1996. High mobility group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54:35-100.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 11
    • 0026676799 scopus 로고
    • Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain
    • Crippa, M. P., P. J. Alfonso, and M. Bustin. 1992. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228:442-449.
    • (1992) J. Mol. Biol. , vol.228 , pp. 442-449
    • Crippa, M.P.1    Alfonso, P.J.2    Bustin, M.3
  • 12
    • 0027296065 scopus 로고
    • Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin
    • Crippa, M. P., L. Trieschmann, P. J. Alfonso, A. P. Wolffe, and M. Bustin. 1993. Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin. EMBO J. 12:3855-3864.
    • (1993) EMBO J. , vol.12 , pp. 3855-3864
    • Crippa, M.P.1    Trieschmann, L.2    Alfonso, P.J.3    Wolffe, A.P.4    Bustin, M.5
  • 13
    • 0032055037 scopus 로고    scopus 로고
    • Covalent modification of histones: Expression from chromatin templates
    • Davie, J. R. 1998. Covalent modification of histones: expression from chromatin templates. Curr. Opin. Genet. Dev. 8:173-178.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 173-178
    • Davie, J.R.1
  • 14
    • 0030610561 scopus 로고    scopus 로고
    • Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region of chromosomal protein HMG-14
    • Ding, H.-F., M. Bustin, and U. Hansen. 1997. Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region of chromosomal protein HMG-14. Mol. Cell. Biol. 17: 5843-5855.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5843-5855
    • Ding, H.-F.1    Bustin, M.2    Hansen, U.3
  • 15
    • 0028000720 scopus 로고
    • Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14
    • Ding, H. F., S. Rimsky, S. C. Batson, M. Bustin, and U. Hansen. 1994. Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14. Science 265:796-799.
    • (1994) Science , vol.265 , pp. 796-799
    • Ding, H.F.1    Rimsky, S.2    Batson, S.C.3    Bustin, M.4    Hansen, U.5
  • 16
    • 0029815618 scopus 로고    scopus 로고
    • The nucleosomal array: Structure/ function relationships
    • Fletcher, T. M., and J. C. Hansen. 1996. The nucleosomal array: structure/ function relationships. Crit. Rev. Eukaryot. Gene Expr. 6:149-188.
    • (1996) Crit. Rev. Eukaryot. Gene Expr. , vol.6 , pp. 149-188
    • Fletcher, T.M.1    Hansen, J.C.2
  • 17
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez, M., C. Rocchini, and J. Ausio. 1995. Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270:17923-17928.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17923-17928
    • Garcia-Ramirez, M.1    Rocchini, C.2    Ausio, J.3
  • 19
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. 1997. Histone acetylation in chromatin structure and transcription. Nature 389:349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 20
    • 0026600019 scopus 로고
    • Chromatin dynamics and the modulation of genetic activity
    • Hansen, J. C., and J. Ausio. 1992. Chromatin dynamics and the modulation of genetic activity. Trends Biochem. Sci. 17:187-191.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 187-191
    • Hansen, J.C.1    Ausio, J.2
  • 21
    • 0030870910 scopus 로고    scopus 로고
    • The histone acetyltransferase activity of human GCN5 and PCAF is stabilized by coenzymes
    • Herrera, J. E., M. Bergel, X. J. Yang, Y. Nakatani, and M. Bustin. 1997. The histone acetyltransferase activity of human GCN5 and PCAF is stabilized by coenzymes. J. Biol. Chem. 272:27253-27258.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27253-27258
    • Herrera, J.E.1    Bergel, M.2    Yang, X.J.3    Nakatani, Y.4    Bustin, M.5
  • 22
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyltransferases
    • Imhof, A., X. J. Yang, V. V. Ogryzko, Y. Nakatani, A. P. Wolffe, and H. Ge. 1997. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689-692.
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.J.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 27
    • 0019176523 scopus 로고
    • Nucleosome cores have two specific binding sites for nonhistone chromosomal proteins HMG 14 and HMG 17
    • Mardian, J. K., A. E. Paton, G. J. Bunick, and D. E. Olins. 1980. Nucleosome cores have two specific binding sites for nonhistone chromosomal proteins HMG 14 and HMG 17. Science 209:1534-1536.
    • (1980) Science , vol.209 , pp. 1534-1536
    • Mardian, J.K.1    Paton, A.E.2    Bunick, G.J.3    Olins, D.E.4
  • 28
    • 0015500799 scopus 로고
    • Two chemically and metabolically distinct forms of calf thymus histone F3
    • Marzluff, W. F., Jr., L. A. Sanders, D. M. Miller, and K. S. McCarty. 1972. Two chemically and metabolically distinct forms of calf thymus histone F3. J. Biol. Chem. 247:2026-2033.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2026-2033
    • Marzluff W.F., Jr.1    Sanders, L.A.2    Miller, D.M.3    McCarty, K.S.4
  • 29
    • 0031964479 scopus 로고    scopus 로고
    • Linking histone acetylation to transcriptional regulation
    • Mizzen, C. A., and C. D. Allis. 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
  • 31
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V. V., R. L. Sciltz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Sciltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 32
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill, L. P., and B. M. Turner. 1995. Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J. 14:3946-3957.
    • (1995) EMBO J. , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 33
    • 0028239906 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Paranjape, S. M., R. T. Kamakaka, and J. T. Kadonaga. 1994. Role of chromatin structure in the regulation of transcription by RNA polymerase II. Annu. Rev. Biochem. 63:265-297.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 265-297
    • Paranjape, S.M.1    Kamakaka, R.T.2    Kadonaga, J.T.3
  • 34
    • 0029131613 scopus 로고
    • HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation
    • Paranjape, S. M., A. Krumm, and J. T. Kadonaga. 1995. HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation. Genes Dev. 9:1978-1991.
    • (1995) Genes Dev. , vol.9 , pp. 1978-1991
    • Paranjape, S.M.1    Krumm, A.2    Kadonaga, J.T.3
  • 35
    • 0031565914 scopus 로고    scopus 로고
    • Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin
    • Postnikov, Y. V., J. E. Herrera, R. Hock, U. Scheer, and M. Bustin. 1997. Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin. J. Mol. Biol. 274:454-465.
    • (1997) J. Mol. Biol. , vol.274 , pp. 454-465
    • Postnikov, Y.V.1    Herrera, J.E.2    Hock, R.3    Scheer, U.4    Bustin, M.5
  • 36
    • 0028127161 scopus 로고
    • The cooperative binding of chromosomal protein HMG-14 to nucleosome cores is reduced by single point mutations in the nucleosomal binding domain
    • Postnikov, Y. V., D. A. Lehn, R. C. Robinson, F. K. Friedman, J. Shiloach, and M. Bustin. 1994. The cooperative binding of chromosomal protein HMG-14 to nucleosome cores is reduced by single point mutations in the nucleosomal binding domain. Nucleic Acids Res. 22:4520-4526.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4520-4526
    • Postnikov, Y.V.1    Lehn, D.A.2    Robinson, R.C.3    Friedman, F.K.4    Shiloach, J.5    Bustin, M.6
  • 37
    • 0029126965 scopus 로고
    • Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores
    • Postnikov, Y. V., L. Trieschmann, A. Rickers, and M. Bustin. 1995. Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores. J. Mol. Biol. 252:423-432.
    • (1995) J. Mol. Biol. , vol.252 , pp. 423-432
    • Postnikov, Y.V.1    Trieschmann, L.2    Rickers, A.3    Bustin, M.4
  • 38
    • 0018800752 scopus 로고
    • Serological analysis of the specificity of HMG chromosomal proteins
    • Romani, M., T. C. Rodman, G. Vidali, and M. Bustin. 1979. Serological analysis of the specificity of HMG chromosomal proteins. J. Biol. Chem. 254:2918-2922.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2918-2922
    • Romani, M.1    Rodman, T.C.2    Vidali, G.3    Bustin, M.4
  • 39
    • 0030271391 scopus 로고    scopus 로고
    • Histone acetylation and chromatin assembly: A single escort, multiple dances?
    • Roth, S. Y., and C. D. Allis. 1996. Histone acetylation and chromatin assembly: a single escort, multiple dances? Cell 87:5-8.
    • (1996) Cell , vol.87 , pp. 5-8
    • Roth, S.Y.1    Allis, C.D.2
  • 40
    • 0032560117 scopus 로고    scopus 로고
    • Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3
    • Rundlet, S. E., A. A. Carmen, S. Noriyuki, B. M. Turner, and M. Grunstein. 1998. Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature 392:831-835.
    • (1998) Nature , vol.392 , pp. 831-835
    • Rundlet, S.E.1    Carmen, A.A.2    Noriyuki, S.3    Turner, B.M.4    Grunstein, M.5
  • 41
    • 0019322514 scopus 로고
    • The interaction of high mobility proteins HMG14 and 17 with nucleosomes
    • Sandeen, G., W. I. Wood, and G. Felsenfeld. 1980. The interaction of high mobility proteins HMG14 and 17 with nucleosomes. Nucleic Acids Res. 8:3757-3778.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3757-3778
    • Sandeen, G.1    Wood, W.I.2    Felsenfeld, G.3
  • 42
    • 0018801554 scopus 로고
    • Studies on the acetylation and deacetylation of HMG proteins
    • Sterner, R., G. Vidali, and V. G. Allfrey. 1979. Studies on the acetylation and deacetylation of HMG proteins. J. Biol. Chem. 254:11577-11583.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 43
    • 0019877270 scopus 로고
    • Studies on the acetylation and deacetylation of HMG proteins: Identification of the sites of acetylation of HMG-14 and HMG-17
    • Sterner, R., G. Vidali, and V. G. Allfrey. 1981. Studies on the acetylation and deacetylation of HMG proteins: identification of the sites of acetylation of HMG-14 and HMG-17. J. Biol. Chem. 256:8892-8895.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8892-8895
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 44
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl, K. 1998. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12:599-606.
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 45
    • 17544363212 scopus 로고    scopus 로고
    • High mobility group proteins 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA
    • Tremethick, D. J., and L. Hyman. 1996. High mobility group proteins 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA. J. Biol. Chem. 271:12009-12016.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12009-12016
    • Tremethick, D.J.1    Hyman, L.2
  • 46
    • 0028958663 scopus 로고
    • Incorporation of chromosomal proteins HMG-14/-17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes
    • Trieschmann, L., P. J. Alfonso, M. P. Crippa, A. P. Wolfe, and M. Bustin. 1995. Incorporation of chromosomal proteins HMG-14/-17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes. EMBO J. 14:1478-1489.
    • (1995) EMBO J. , vol.14 , pp. 1478-1489
    • Trieschmann, L.1    Alfonso, P.J.2    Crippa, M.P.3    Wolfe, A.P.4    Bustin, M.5
  • 47
    • 0032510746 scopus 로고    scopus 로고
    • The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes
    • Trieschmann, L., B. Martin, and M. Buslin. 1998. The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes. Proc. Natl. Acad. Sci. USA 95:5468-5473.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5468-5473
    • Trieschmann, L.1    Martin, B.2    Buslin, M.3
  • 48
    • 0028791878 scopus 로고
    • Modular structure of chromosomal proteins HMG-14 and HMG-17: Definition of a transcriptional activation domain distinct from the nucleosomal binding domain
    • Trieschmann, L., Y. V. Postnikov, A. Rickers, and M. Bustin. 1995. Modular structure of chromosomal proteins HMG-14 and HMG-17: definition of a transcriptional activation domain distinct from the nucleosomal binding domain. Mol. Cell. Biol. 15:6663-6669.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6663-6669
    • Trieschmann, L.1    Postnikov, Y.V.2    Rickers, A.3    Bustin, M.4
  • 49
    • 0029349023 scopus 로고
    • Histone acetylation in chromatin and chromosomes
    • Turner, B. M., and L. P. O'Neill. 1995. Histone acetylation in chromatin and chromosomes. Semin. Cell Biol. 6:229-236.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 229-236
    • Turner, B.M.1    O'Neill, L.P.2
  • 50
    • 0032540235 scopus 로고    scopus 로고
    • Stimulation of replication efficiency of a chromatin template by chromosomal protein HMG-17
    • Vestner, B., M. Bustin, and C. Gruss. 1998. Stimulation of replication efficiency of a chromatin template by chromosomal protein HMG-17. J. Biol. Chem. 273:9409-9414.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9409-9414
    • Vestner, B.1    Bustin, M.2    Gruss, C.3
  • 51
    • 0029985730 scopus 로고    scopus 로고
    • Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro
    • Vettese-Dadey, M., P. A. Grant, T. R. Hebbes, C. Crane-Robinson, C. D. Allis, and J. L. Workman. 1996. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J. 15:2508-2518.
    • (1996) EMBO J. , vol.15 , pp. 2508-2518
    • Vettese-Dadey, M.1    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 52
  • 53
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with adenoviral oncoprotein E1A
    • Yang, X.-J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.-J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.