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Volumn 105, Issue 33, 2008, Pages 11703-11708

Yeast linker histone Hho1p is required for efficient RNA polymerase I processivity and transcriptional silencing at the ribosomal DNA

Author keywords

Chromatin; rDNA

Indexed keywords

DNA DIRECTED RNA POLYMERASE; HISTONE; NUCLEAR PROTEIN; PROTEIN HHO1P; PSORALEN; RIBOSOME DNA; RIBOSOME RNA;

EID: 50149111534     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0709403105     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 0029915287 scopus 로고    scopus 로고
    • Histone sequence database: A compilation of highly-conserved nucleoprotein sequences
    • Baxevanis AD, Landsman D (1996) Histone sequence database: A compilation of highly-conserved nucleoprotein sequences. Nucleic Acids Res 24:245-247.
    • (1996) Nucleic Acids Res , vol.24 , pp. 245-247
    • Baxevanis, A.D.1    Landsman, D.2
  • 2
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • Woodcock CL, Skoultchi AI, Fan Y (2006) Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res 14:17-25.
    • (2006) Chromosome Res , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3
  • 3
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • Simpson RT (1978) Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 17:5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 5
    • 0028068811 scopus 로고
    • Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of histone H5
    • Cerf C, et al. (1994) Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of histone H5. Biochemistry 33:11079-11086.
    • (1994) Biochemistry , vol.33 , pp. 11079-11086
    • Cerf, C.1
  • 6
    • 0023355070 scopus 로고
    • The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore GM, Gronenborn AM, Nilges M, Sukumaran DK, Zarbock J (1987) The polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J 6:1833-1842.
    • (1987) EMBO J , vol.6 , pp. 1833-1842
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Sukumaran, D.K.4    Zarbock, J.5
  • 7
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 8
    • 0030016336 scopus 로고    scopus 로고
    • Identification of two DNA-binding sites on the globular domain of histone H5
    • Goytisolo FA, et al. (1996) Identification of two DNA-binding sites on the globular domain of histone H5. EMBO J 15:3421-3429.
    • (1996) EMBO J , vol.15 , pp. 3421-3429
    • Goytisolo, F.A.1
  • 10
    • 0042622604 scopus 로고    scopus 로고
    • Linker histone-dependent organization and dynamics of nucleosome entry/exit DNAs
    • Sivolob A, Prunell A (2003) Linker histone-dependent organization and dynamics of nucleosome entry/exit DNAs. J Mol Biol 331:1025-1040.
    • (2003) J Mol Biol , vol.331 , pp. 1025-1040
    • Sivolob, A.1    Prunell, A.2
  • 12
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • Hansen JC, Lu X, Ross ED, Woody RW (2006) Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 281:1853-1856.
    • (2006) J Biol Chem , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 13
    • 0022539023 scopus 로고
    • Cell-cycle regulation of histone gene expression
    • Schumperli D (1986) Cell-cycle regulation of histone gene expression. Cell 45:471-472.
    • (1986) Cell , vol.45 , pp. 471-472
    • Schumperli, D.1
  • 14
    • 0031742022 scopus 로고    scopus 로고
    • Comprehensive identification of cell cycle-regulated genes of the yeast. Saccharomyces cerevisiae by microarray hybridization
    • Spellman PT, et al. (1998) Comprehensive identification of cell cycle-regulated genes of the yeast. Saccharomyces cerevisiae by microarray hybridization. Mol Biol Cell 9:3273-3297.
    • (1998) Mol Biol Cell , vol.9 , pp. 3273-3297
    • Spellman, P.T.1
  • 15
    • 33747351584 scopus 로고    scopus 로고
    • Full and partial genome-wide assembly and disassembly of the yeast transcription machinery in response to heat shock
    • Zanton SJ, Pugh BF (2006) Full and partial genome-wide assembly and disassembly of the yeast transcription machinery in response to heat shock. Genes Dev 20:2250-2265.
    • (2006) Genes Dev , vol.20 , pp. 2250-2265
    • Zanton, S.J.1    Pugh, B.F.2
  • 16
    • 29144488127 scopus 로고    scopus 로고
    • The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in endogenous NPC-mediated transcriptional control
    • Dilworth DJ, et al. (2005) The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in endogenous NPC-mediated transcriptional control. J Cell Biol 171:955-965.
    • (2005) J Cell Biol , vol.171 , pp. 955-965
    • Dilworth, D.J.1
  • 17
    • 33751112515 scopus 로고    scopus 로고
    • Inhibition of homologous recombination by a cohesin-associated clamp complex recruited to the rDNA recombination enhancer
    • Huang J, et al. (2006) Inhibition of homologous recombination by a cohesin-associated clamp complex recruited to the rDNA recombination enhancer. Genes Dev 20:2887-2901.
    • (2006) Genes Dev , vol.20 , pp. 2887-2901
    • Huang, J.1
  • 18
    • 0030219940 scopus 로고    scopus 로고
    • Histone H1 in Saccharomyces cerevisiae - a double mystery solved
    • Landsman D (1996) Histone H1 in Saccharomyces cerevisiae - a double mystery solved. Trends Biochem Sci 21:287-288.
    • (1996) Trends Biochem Sci , vol.21 , pp. 287-288
    • Landsman, D.1
  • 19
    • 1842523300 scopus 로고    scopus 로고
    • Distinct properties of the two putative "globular domains" of the yeast linker histone, Hho1p
    • Ali T, Thomas JO (2004) Distinct properties of the two putative "globular domains" of the yeast linker histone, Hho1p. J Mol Biol 337:1123-1135.
    • (2004) J Mol Biol , vol.337 , pp. 1123-1135
    • Ali, T.1    Thomas, J.O.2
  • 20
    • 1842474282 scopus 로고    scopus 로고
    • Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p
    • Ali T, Coles P, Stevens TJ, Stott K, Thomas JO (2004) Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. J Mol Biol 338:139-148.
    • (2004) J Mol Biol , vol.338 , pp. 139-148
    • Ali, T.1    Coles, P.2    Stevens, T.J.3    Stott, K.4    Thomas, J.O.5
  • 21
    • 0019326442 scopus 로고
    • Deoxyribonuclease II as a probe for chromatin structure. I. Location of cleavage sites
    • Horz W, Zachau HG (1980) Deoxyribonuclease II as a probe for chromatin structure. I. Location of cleavage sites. J Mol Biol 144:305-327.
    • (1980) J Mol Biol , vol.144 , pp. 305-327
    • Horz, W.1    Zachau, H.G.2
  • 22
    • 0017610585 scopus 로고
    • Comparative subunit structure of HeLa, yeast, and chicken erythrocyte chromatin
    • Lohr D, et al. (1977) Comparative subunit structure of HeLa, yeast, and chicken erythrocyte chromatin. Proc Natl Acad Sci USA 74:79-83.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 79-83
    • Lohr, D.1
  • 23
    • 0017115264 scopus 로고
    • Yeast chromatin structure
    • Thomas JO, Furber V (1976) Yeast chromatin structure. FEBS Lett 66:274-280.
    • (1976) FEBS Lett , vol.66 , pp. 274-280
    • Thomas, J.O.1    Furber, V.2
  • 24
    • 0347519278 scopus 로고    scopus 로고
    • The linker histone homolog Hho1p from. Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy
    • Ono K, et al. (2003) The linker histone homolog Hho1p from. Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. Nucleic Acids Res 31:7199-7207.
    • (2003) Nucleic Acids Res , vol.31 , pp. 7199-7207
    • Ono, K.1
  • 25
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen X, Yu L, Weir JW, Gorovsky MA (1995) Linker histones are not essential and affect chromatin condensation in vivo. Cell 82:47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 26
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone
    • Downs JA, Kosmidou E, Morgan A, Jackson SP (2003) Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone. Mol Cell 11:1685-1692.
    • (2003) Mol Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 27
    • 0038721220 scopus 로고    scopus 로고
    • H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo
    • Fan Y, et al. (2003) H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol Cell Biol 23:4559-4572.
    • (2003) Mol Cell Biol , vol.23 , pp. 4559-4572
    • Fan, Y.1
  • 28
    • 29244449333 scopus 로고    scopus 로고
    • Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation
    • Fan Y, et al. (2005) Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell 123:1199-1212.
    • (2005) Cell , vol.123 , pp. 1199-1212
    • Fan, Y.1
  • 29
    • 0035477211 scopus 로고    scopus 로고
    • Specific distribution of the. Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin
    • Freidkin I, Katcoff DJ (2001) Specific distribution of the. Saccharomyces cerevisiae linker histone homolog HHO1p in the chromatin. Nucleic Acids Res 29:4043-4051.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4043-4051
    • Freidkin, I.1    Katcoff, D.J.2
  • 30
    • 0031056907 scopus 로고    scopus 로고
    • An unusual form of transcriptional silencing in yeast ribosomal DNA
    • Smith JS, Boeke JD (1997) An unusual form of transcriptional silencing in yeast ribosomal DNA. Genes Dev 11:241-254.
    • (1997) Genes Dev , vol.11 , pp. 241-254
    • Smith, J.S.1    Boeke, J.D.2
  • 31
    • 19444366667 scopus 로고    scopus 로고
    • Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p
    • Sanderson A, Stott K, Stevens TJ, Thomas JO (2005) Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. J Mol Biol 349:608-620.
    • (2005) J Mol Biol , vol.349 , pp. 608-620
    • Sanderson, A.1    Stott, K.2    Stevens, T.J.3    Thomas, J.O.4
  • 32
    • 0034903337 scopus 로고    scopus 로고
    • In vivo site-directed mutagenesis using oligonucleotides
    • Storici F, Lewis LK, Resnick MA (2001) In vivo site-directed mutagenesis using oligonucleotides. Nat Biotechnol 19:773-776.
    • (2001) Nat Biotechnol , vol.19 , pp. 773-776
    • Storici, F.1    Lewis, L.K.2    Resnick, M.A.3
  • 33
    • 16544382021 scopus 로고    scopus 로고
    • RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components
    • Gallagher JE, et al. (2004) RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components. Genes Dev 18:2506-2517.
    • (2004) Genes Dev , vol.18 , pp. 2506-2517
    • Gallagher, J.E.1
  • 34
    • 0027270476 scopus 로고
    • Chromatin structures and transcription of rDNA in yeast. Saccharomyces cerevisiae
    • Dammann R, Lucchini R, Koller T, Sogo JM (1993) Chromatin structures and transcription of rDNA in yeast. Saccharomyces cerevisiae. Nucleic Acids Res 21:2331-2338.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2331-2338
    • Dammann, R.1    Lucchini, R.2    Koller, T.3    Sogo, J.M.4
  • 35
    • 0035958006 scopus 로고    scopus 로고
    • Decreased expression of specific genes in yeast cells lacking histone H1
    • Hellauer K, Sirard E, Turcotte B (2001) Decreased expression of specific genes in yeast cells lacking histone H1. J Biol Chem 276:13587-13592.
    • (2001) J Biol Chem , vol.276 , pp. 13587-13592
    • Hellauer, K.1    Sirard, E.2    Turcotte, B.3
  • 36
    • 6944244084 scopus 로고    scopus 로고
    • A module map showing conditional activity of expression modules in cancer
    • Segal E, Friedman N, Koller D, Regev A (2004) A module map showing conditional activity of expression modules in cancer. Nat Genet 36:1090-1098.
    • (2004) Nat Genet , vol.36 , pp. 1090-1098
    • Segal, E.1    Friedman, N.2    Koller, D.3    Regev, A.4
  • 37
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • Bustin M, Catez F, Lim JH (2005) The dynamics of histone H1 function in chromatin. Mol Cell 17:617-620.
    • (2005) Mol Cell , vol.17 , pp. 617-620
    • Bustin, M.1    Catez, F.2    Lim, J.H.3
  • 38
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • Bednar J, et al. (1998) Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc Natl Acad Sci USA 95:14173-14178.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14173-14178
    • Bednar, J.1
  • 39
    • 0028282152 scopus 로고
    • Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing
    • Linder C, Thoma F (1994) Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing. Mol Cell Biol 14:2822-2835.
    • (1994) Mol Cell Biol , vol.14 , pp. 2822-2835
    • Linder, C.1    Thoma, F.2
  • 41
    • 29244485591 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae linker histone Hho1p, with two globular domains, can simultaneously bind to two four-way junction DNA molecules
    • Schäfer G, Smith EM, Patterton HG (2005) The Saccharomyces cerevisiae linker histone Hho1p, with two globular domains, can simultaneously bind to two four-way junction DNA molecules. Biochemistry 44:16766-16775.
    • (2005) Biochemistry , vol.44 , pp. 16766-16775
    • Schäfer, G.1    Smith, E.M.2    Patterton, H.G.3
  • 42
    • 22544477069 scopus 로고    scopus 로고
    • Histones are required for transcription of yeast rRNA genes by RNA polymerase I
    • Tongaonkar P, et al. (2005) Histones are required for transcription of yeast rRNA genes by RNA polymerase I. Proc Natl Acad Sci USA 102:10129-10134.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10129-10134
    • Tongaonkar, P.1
  • 43
    • 33846946112 scopus 로고    scopus 로고
    • RNA polymerase I in yeast transcribes dynamic nucleosomal rDNA
    • Jones HS, et al. (2007) RNA polymerase I in yeast transcribes dynamic nucleosomal rDNA. Nat Struct Mol Biol 14:123-130.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 123-130
    • Jones, H.S.1
  • 44
    • 33846614928 scopus 로고    scopus 로고
    • Is ribosome synthesis controlled by pol I transcription?
    • Chédin S, et al. (2007) Is ribosome synthesis controlled by pol I transcription? Cell Cycle 6:11-15.
    • (2007) Cell Cycle , vol.6 , pp. 11-15
    • Chédin, S.1
  • 45
    • 33746631755 scopus 로고    scopus 로고
    • The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components
    • Laferté A, et al. (2006) The transcriptional activity of RNA polymerase I is a key determinant for the level of all ribosome components. Genes Dev 20:2030-2040.
    • (2006) Genes Dev , vol.20 , pp. 2030-2040
    • Laferté, A.1
  • 46
    • 0034934774 scopus 로고    scopus 로고
    • Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association
    • Lieb JD, Liu X, Botstein D, Brown PO (2001) Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association. Nat Genet 28:327-334.
    • (2001) Nat Genet , vol.28 , pp. 327-334
    • Lieb, J.D.1    Liu, X.2    Botstein, D.3    Brown, P.O.4
  • 47
    • 0036649756 scopus 로고    scopus 로고
    • Genome-wide binding map of the histone deacetylase Rpd3 in yeast
    • Kurdistani SK, Robyr D, Tavazoie S, Grunstein M (2002) Genome-wide binding map of the histone deacetylase Rpd3 in yeast. Nat Genet 31:248-254.
    • (2002) Nat Genet , vol.31 , pp. 248-254
    • Kurdistani, S.K.1    Robyr, D.2    Tavazoie, S.3    Grunstein, M.4
  • 48
    • 0037119973 scopus 로고    scopus 로고
    • RPD3 is required for the inactivation of yeast ribosomal DNA genes in stationary phase
    • Sandmeier JJ, et al. (2002) RPD3 is required for the inactivation of yeast ribosomal DNA genes in stationary phase. EMBO J 21:4959-4968.
    • (2002) EMBO J , vol.21 , pp. 4959-4968
    • Sandmeier, J.J.1
  • 49
    • 33646577130 scopus 로고    scopus 로고
    • Role of histone deacetylase Rpd3 in regulating rRNA gene transcription and nucleolar structure in yeast
    • Oakes ML, et al. (2006) Role of histone deacetylase Rpd3 in regulating rRNA gene transcription and nucleolar structure in yeast. Mol Cell Biol 26:3889-3901.
    • (2006) Mol Cell Biol , vol.26 , pp. 3889-3901
    • Oakes, M.L.1
  • 51
    • 0034704248 scopus 로고    scopus 로고
    • Genome-wide location and function of DNA binding proteins
    • Ren B, et al. (2002) Genome-wide location and function of DNA binding proteins, Science 290:2306-2309.
    • (2002) Science , vol.290 , pp. 2306-2309
    • Ren, B.1
  • 52
    • 0029112540 scopus 로고
    • Transcription in the yeast rRNA gene locus: Distribution of the active gene copies and chromatin structure of their flanking regulatory sequences
    • Dammann R, Lucchini R, Koller T, Sogo JM (1995) Transcription in the yeast rRNA gene locus: Distribution of the active gene copies and chromatin structure of their flanking regulatory sequences. Mol Cell Biol 15:5294-5303.
    • (1995) Mol Cell Biol , vol.15 , pp. 5294-5303
    • Dammann, R.1    Lucchini, R.2    Koller, T.3    Sogo, J.M.4


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