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Volumn 201, Issue 3, 2015, Pages 1030-1045

The abundant histone chaperones Spt6 and FACT collaborate to assemble, inspect, and maintain chromatin structure in saccharomyces cerevisiae

Author keywords

FACT; Histone chaperones; Nucleosome reorganization; Spt6

Indexed keywords

CHAPERONE; HISTONE; HISTONE CHAPERONE FACT; HISTONE CHAPERONE SPT6; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG; CHROMATIN; DNA BINDING PROTEIN; FACT PROTEIN, S CEREVISIAE; HIGH MOBILITY GROUP PROTEIN; MULTIPROTEIN COMPLEX; NUCLEOSOME; POB3 PROTEIN, S CEREVISIAE; PROTEIN BINDING; SPT16 PROTEIN, S CEREVISIAE; SPT6 PROTEIN, S CEREVISIAE; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION FACTOR;

EID: 84946950170     PISSN: 00166731     EISSN: 19432631     Source Type: Journal    
DOI: 10.1534/genetics.115.180794     Document Type: Article
Times cited : (49)

References (57)
  • 1
    • 31544446038 scopus 로고    scopus 로고
    • Transcriptional activators are dispensable for transcription in the absence of Spt6- mediated chromatin reassembly of promoter regions
    • Adkins, M. W., and J. K. Tyler, 2006 Transcriptional activators are dispensable for transcription in the absence of Spt6- mediated chromatin reassembly of promoter regions. Mol. Cell 21: 405-416.
    • (2006) Mol. Cell , vol.21 , pp. 405-416
    • Adkins, M.W.1    Tyler, J.K.2
  • 2
    • 33846574739 scopus 로고    scopus 로고
    • Structure of the yeast histone H3-ASF1 interaction: Implications for chaperone mechanism, species-specific interactions, and epigenetics
    • Antczak, A. J., T. Tsubota, P. D. Kaufman, and J. M. Berger, 2006 Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. BMC Struct. Biol. 6: 26.
    • (2006) BMC Struct. Biol , vol.6 , pp. 26
    • Antczak, A.J.1    Tsubota, T.2    Kaufman, P.D.3    Berger, J.M.4
  • 3
    • 67349153355 scopus 로고    scopus 로고
    • Spt6 enhances the elongation rate of RNA polymerase II in vivo
    • Ardehali, M. B., J. Yao, K. Adelman, N. J. Fuda, S. J. Petesch et al., 2009 Spt6 enhances the elongation rate of RNA polymerase II in vivo. EMBO J. 28: 1067-1077.
    • (2009) EMBO J , vol.28 , pp. 1067-1077
    • Ardehali, M.B.1    Yao, J.2    Adelman, K.3    Fuda, N.J.4    Petesch, S.J.5
  • 5
    • 0036460783 scopus 로고    scopus 로고
    • Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism
    • Betz, J. L., M. Chang, T. M. Washburn, S. E. Porter, C. L. Mueller et al., 2002 Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol. Genet. Genomics 268: 272-285.
    • (2002) Mol. Genet. Genomics , vol.268 , pp. 272-285
    • Betz, J.L.1    Chang, M.2    Washburn, T.M.3    Porter, S.E.4    Mueller, C.L.5
  • 6
    • 0029890667 scopus 로고    scopus 로고
    • Evidence that Spt6p controls chromatin structure by a direct interaction with histones
    • Bortvin, A., and F. Winston, 1996 Evidence that Spt6p controls chromatin structure by a direct interaction with histones. Science 272: 1473-1476.
    • (1996) Science , vol.272 , pp. 1473-1476
    • Bortvin, A.1    Winston, F.2
  • 7
    • 21844435714 scopus 로고    scopus 로고
    • Npl3 is an antagonist of mRNA 39 end formation by RNA polymerase II
    • Bucheli, M. E., and S. Buratowski, 2005 Npl3 is an antagonist of mRNA 39 end formation by RNA polymerase II. EMBO J. 24: 2150-2160.
    • (2005) EMBO J , vol.24 , pp. 2150-2160
    • Bucheli, M.E.1    Buratowski, S.2
  • 8
    • 84933514672 scopus 로고    scopus 로고
    • Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2
    • Chen, S., A. Rufiange, H. Huang, K. R. Rajashankar, A. Nourani et al., 2015 Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2. Genes Dev. 29: 1326-1340.
    • (2015) Genes Dev , vol.29 , pp. 1326-1340
    • Chen, S.1    Rufiange, A.2    Huang, H.3    Rajashankar, K.R.4    Nourani, A.5
  • 10
    • 79955015015 scopus 로고    scopus 로고
    • Crystal Structures of the S. cerevisiae Spt6 Core and C-Terminal Tandem SH2 Domain
    • Close, D., S. J. Johnson, M. A. Sdano, S. M. McDonald, H. Robinson et al., 2011 Crystal Structures of the S. cerevisiae Spt6 Core and C-Terminal Tandem SH2 Domain. J. Mol. Biol. 408: 697-713.
    • (2011) J. Mol. Biol , vol.408 , pp. 697-713
    • Close, D.1    Johnson, S.J.2    Sdano, M.A.3    McDonald, S.M.4    Robinson, H.5
  • 11
    • 0029817632 scopus 로고    scopus 로고
    • Mutations in the SPT4, SPT5, and SPT6 genes alter transcription of a subset of histone genes in Saccharomyces cerevisiae
    • Compagnone-Post, P. A., and M. A. Osley, 1996 Mutations in the SPT4, SPT5, and SPT6 genes alter transcription of a subset of histone genes in Saccharomyces cerevisiae. Genetics 143: 1543-1554.
    • (1996) Genetics , vol.143 , pp. 1543-1554
    • Compagnone-Post, P.A.1    Osley, M.A.2
  • 12
    • 84857117928 scopus 로고    scopus 로고
    • Histone exchange and histone modifications during transcription and aging
    • Das, C., and J. K. Tyler, 2012 Histone exchange and histone modifications during transcription and aging. Biochim. Biophys. Acta 1819: 332-342.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 332-342
    • Das, C.1    Tyler, J.K.2
  • 13
    • 84893040276 scopus 로고    scopus 로고
    • Spt6 regulates intragenic and antisense transcription, nucleosome positioning, and histone modifications genome-wide in fission yeast
    • DeGennaro, C. M., B. H. Alver, S. Marguerat, E. Stepanova, C. P. Davis et al., 2013 Spt6 regulates intragenic and antisense transcription, nucleosome positioning, and histone modifications genome-wide in fission yeast. Mol. Cell. Biol. 33: 4779-4792.
    • (2013) Mol. Cell. Biol , vol.33 , pp. 4779-4792
    • DeGennaro, C.M.1    Alver, B.H.2    Marguerat, S.3    Stepanova, E.4    Davis, C.P.5
  • 14
    • 78649717707 scopus 로고    scopus 로고
    • The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26
    • Diebold, M. L., M. Koch, E. Loeliger, V. Cura, F. Winston et al., 2010a The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26. EMBO J. 29: 3979-3991.
    • (2010) EMBO J , vol.29 , pp. 3979-3991
    • Diebold, M.L.1    Koch, M.2    Loeliger, E.3    Cura, V.4    Winston, F.5
  • 15
    • 78649684166 scopus 로고    scopus 로고
    • A non-canonical tandem SH2 enables interaction of elongation factor SPT6 with RNA polymerase II
    • Diebold, M. L., E. Loeliger, M. Koch, F. Winston, J. Cavarelli et al., 2010b A non-canonical tandem SH2 enables interaction of elongation factor SPT6 with RNA polymerase II. J. Biol Chem. 285: 38389-38391.
    • (2010) J. Biol Chem , vol.285 , pp. 38389-38391
    • Diebold, M.L.1    Loeliger, E.2    Koch, M.3    Winston, F.4    Cavarelli, J.5
  • 16
    • 84893320560 scopus 로고    scopus 로고
    • A feed forward circuit comprising Spt6, Ctk1 and PAF regulates Pol II CTD phosphorylation and transcription elongation
    • Dronamraju, R., and B. D. Strahl, 2013 A feed forward circuit comprising Spt6, Ctk1 and PAF regulates Pol II CTD phosphorylation and transcription elongation. Nucleic Acids Res. 42: 870-871.
    • (2013) Nucleic Acids Res , vol.42 , pp. 870-871
    • Dronamraju, R.1    Strahl, B.D.2
  • 17
    • 11144357677 scopus 로고    scopus 로고
    • Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro
    • Endoh, M., W. Zhu, J. Hasegawa, H. Watanabe, D. K. Kim et al., 2004 Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro. Mol. Cell. Biol. 24: 3324-3336.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3324-3336
    • Endoh, M.1    Zhu, W.2    Hasegawa, J.3    Watanabe, H.4    Kim, D.K.5
  • 18
    • 33750477650 scopus 로고    scopus 로고
    • Structural basis for the histone chaperone activity of Asf1
    • English, C. M., M. W. Adkins, J. J. Carson, M. E. Churchill, and J. K. Tyler, 2006 Structural basis for the histone chaperone activity of Asf1. Cell 127: 495-508.
    • (2006) Cell , vol.127 , pp. 495-508
    • English, C.M.1    Adkins, M.W.2    Carson, J.J.3    Churchill, M.E.4    Tyler, J.K.5
  • 19
    • 84860573339 scopus 로고    scopus 로고
    • Regulation of histone gene expression in budding yeast
    • Eriksson, P. R., D. Ganguli, V. Nagarajavel, and D. J. Clark, 2012 Regulation of histone gene expression in budding yeast. Genetics 191: 7-20.
    • (2012) Genetics , vol.191 , pp. 7-20
    • Eriksson, P.R.1    Ganguli, D.2    Nagarajavel, V.3    Clark, D.J.4
  • 20
    • 77956520661 scopus 로고    scopus 로고
    • Elevated histone expression promotes life span extension
    • Feser, J., D. Truong, C. Das, J. J. Carson, J. Kieft et al., 2010 Elevated histone expression promotes life span extension. Mol. Cell 39: 724-735.
    • (2010) Mol. Cell , vol.39 , pp. 724-735
    • Feser, J.1    Truong, D.2    Das, C.3    Carson, J.J.4    Kieft, J.5
  • 21
    • 84857119549 scopus 로고    scopus 로고
    • The role of FACT in making and breaking nucleosomes
    • Formosa, T., 2012 The role of FACT in making and breaking nucleosomes. Biochim. Biophys. Acta 1819: 247-255.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 247-255
    • Formosa, T.1
  • 22
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: Polymerase passage may degrade chromatin structure
    • Formosa, T., S. Ruone, M. D. Adams, A. E. Olsen, P. Eriksson et al., 2002 Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure. Genetics 162: 1557-1571.
    • (2002) Genetics , vol.162 , pp. 1557-1571
    • Formosa, T.1    Ruone, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5
  • 25
    • 4844228020 scopus 로고    scopus 로고
    • Systematic quantification of gene interactions by phenotypic array analysis
    • Hartman, J. L. t., and N. P. Tippery, 2004 Systematic quantification of gene interactions by phenotypic array analysis. Genome Biol. 5: R49.
    • (2004) Genome Biol , vol.5
    • Hartman, J.L.T.1    Tippery, N.P.2
  • 26
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog, G. A., T. Wada, H. Handa, and F. Winston, 1998 Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12: 357-369.
    • (1998) Genes Dev , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 27
    • 84898841862 scopus 로고    scopus 로고
    • The yeast and human FACT chromatinreorganizing complexes solve R-loop-mediated transcriptionreplication conflicts
    • Herrera-Moyano, E., X. Mergui, M. L. Garcia-Rubio, S. Barroso, and A. Aguilera, 2014 The yeast and human FACT chromatinreorganizing complexes solve R-loop-mediated transcriptionreplication conflicts. Genes Dev. 28: 735-748.
    • (2014) Genes Dev , vol.28 , pp. 735-748
    • Herrera-Moyano, E.1    Mergui, X.2    Garcia-Rubio, M.L.3    Barroso, S.4    Aguilera, A.5
  • 28
    • 84879883663 scopus 로고    scopus 로고
    • Structural basis of histone H2A-H2B recognition by the essential chaperone FACT
    • Hondele, M., T. Stuwe, M. Hassler, F. Halbach, A. Bowman et al., 2013 Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 499: 111-114.
    • (2013) Nature , vol.499 , pp. 111-114
    • Hondele, M.1    Stuwe, T.2    Hassler, M.3    Halbach, F.4    Bowman, A.5
  • 29
    • 84877322380 scopus 로고    scopus 로고
    • Histone chaperone FACT action during transcription through chromatin by RNA polymerase II
    • Hsieh, F. K., O. I. Kulaeva, S. S. Patel, P. N. Dyer, K. Luger et al., 2013 Histone chaperone FACT action during transcription through chromatin by RNA polymerase II. Proc. Natl. Acad. Sci. USA 110: 7654-7659.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7654-7659
    • Hsieh, F.K.1    Kulaeva, O.I.2    Patel, S.S.3    Dyer, P.N.4    Luger, K.5
  • 30
    • 78751498728 scopus 로고    scopus 로고
    • Control of chromatin structure by spt6: Different consequences in coding and regulatory regions
    • Ivanovska, I., P. E. Jacques, O. J. Rando, F. Robert, and F. Winston, 2011 Control of chromatin structure by spt6: different consequences in coding and regulatory regions. Mol. Cell. Biol. 31: 531-541.
    • (2011) Mol. Cell. Biol , vol.31 , pp. 531-541
    • Ivanovska, I.1    Jacques, P.E.2    Rando, O.J.3    Robert, F.4    Winston, F.5
  • 31
    • 68349148027 scopus 로고    scopus 로고
    • Histone chaperone spt16 promotes redeposition of the original H3-H4 histones evicted by elongating RNA polymerase
    • Jamai, A., A. Puglisi, and M. Strubin, 2009 Histone chaperone spt16 promotes redeposition of the original H3-H4 histones evicted by elongating RNA polymerase. Mol. Cell 35: 377-383.
    • (2009) Mol. Cell , vol.35 , pp. 377-383
    • Jamai, A.1    Puglisi, A.2    Strubin, M.3
  • 32
    • 40849094161 scopus 로고    scopus 로고
    • Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa
    • Johnson, S. J., D. Close, H. Robinson, I. Vallet-Gely, S. L. Dove et al., 2008 Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. J. Mol. Biol. 377: 1460-1473.
    • (2008) J. Mol. Biol , vol.377 , pp. 1460-1473
    • Johnson, S.J.1    Close, D.2    Robinson, H.3    Vallet-Gely, I.4    Dove, S.L.5
  • 33
    • 12544260507 scopus 로고    scopus 로고
    • Interaction between transcription elongation factors and mRNA 39-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus
    • Kaplan, C. D., M. J. Holland, and F. Winston, 2005 Interaction between transcription elongation factors and mRNA 39-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus. J. Biol. Chem. 280: 913-922.
    • (2005) J. Biol. Chem , vol.280 , pp. 913-922
    • Kaplan, C.D.1    Holland, M.J.2    Winston, F.3
  • 34
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan, C. D., L. Laprade, and F. Winston, 2003 Transcription elongation factors repress transcription initiation from cryptic sites. Science 301: 1096-1099.
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 35
    • 84880393238 scopus 로고    scopus 로고
    • Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3
    • Kato, H., K. Okazaki, T. Iida, J. Nakayama, Y. Murakami et al., 2013a Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3. Sci. Rep. 3: 2186.
    • (2013) Sci. Rep , vol.3 , pp. 2186
    • Kato, H.1    Okazaki, K.2    Iida, T.3    Nakayama, J.4    Murakami, Y.5
  • 36
    • 84888805749 scopus 로고    scopus 로고
    • Spt6: Two fundamentally distinct functions in the regulation of histone modification
    • Kato, H., K. Okazaki, and T. Urano, 2013b Spt6: two fundamentally distinct functions in the regulation of histone modification. Epigenetics 8: 1249-1253.
    • (2013) Epigenetics , vol.8 , pp. 1249-1253
    • Kato, H.1    Okazaki, K.2    Urano, T.3
  • 37
    • 84876275605 scopus 로고    scopus 로고
    • Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT
    • Kemble, D. J., F. G. Whitby, H. Robinson, L. L. McCullough, T. Formosa et al., 2013 Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT. J. Biol. Chem. 288: 10188-10194.
    • (2013) J. Biol. Chem , vol.288 , pp. 10188-10194
    • Kemble, D.J.1    Whitby, F.G.2    Robinson, H.3    McCullough, L.L.4    Formosa, T.5
  • 38
    • 0036787862 scopus 로고    scopus 로고
    • RNA polymerase II elongation factors of Saccharomyces cerevisiae: A targeted proteomics approach
    • Krogan, N. J., M. Kim, S. H. Ahn, G. Zhong, M. S. Kobor et al., 2002 RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol. Cell. Biol. 22: 6979-6992.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6979-6992
    • Krogan, N.J.1    Kim, M.2    Ahn, S.H.3    Zhong, G.4    Kobor, M.S.5
  • 40
    • 84887161037 scopus 로고    scopus 로고
    • Control of transcriptional elongation
    • Kwak, H., and J. T. Lis, 2013 Control of transcriptional elongation. Annu. Rev. Genet. 47: 483-508.
    • (2013) Annu. Rev. Genet , vol.47 , pp. 483-508
    • Kwak, H.1    Lis, J.T.2
  • 41
    • 0037313160 scopus 로고    scopus 로고
    • Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5- associated proteins
    • Lindstrom, D. L., S. L. Squazzo, N. Muster, T. A. Burckin, K. C. Wachter et al., 2003 Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5- associated proteins. Mol. Cell. Biol. 23: 1368-1378.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 1368-1378
    • Lindstrom, D.L.1    Squazzo, S.L.2    Muster, N.3    Burckin, T.A.4    Wachter, K.C.5
  • 42
    • 80051520840 scopus 로고    scopus 로고
    • Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone
    • McCullough, L., R. Rawlins, A. E. Olsen, H. Xin, D. J. Stillman et al., 2011 Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone. Genetics 188: 835-846.
    • (2011) Genetics , vol.188 , pp. 835-846
    • McCullough, L.1    Rawlins, R.2    Olsen, A.E.3    Xin, H.4    Stillman, D.J.5
  • 43
    • 84883807292 scopus 로고    scopus 로고
    • The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae
    • McCullough, L., B. Poe, Z. Connell, H. Xin, and T. Formosa, 2013 The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae. Genetics 195: 101-113.
    • (2013) Genetics , vol.195 , pp. 101-113
    • McCullough, L.1    Poe, B.2    Connell, Z.3    Xin, H.4    Formosa, T.5
  • 44
    • 78649903576 scopus 로고    scopus 로고
    • Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding
    • McDonald, S. M., D. Close, H. Xin, T. Formosa, and C. P. Hill, 2010 Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding. Mol. Cell 40: 725-735.
    • (2010) Mol. Cell , vol.40 , pp. 725-735
    • McDonald, S.M.1    Close, D.2    Xin, H.3    Formosa, T.4    Hill, C.P.5
  • 45
    • 0022482135 scopus 로고
    • Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission
    • Meeks-Wagner, D., and L. H. Hartwell, 1986 Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission. Cell 44: 43-52.
    • (1986) Cell , vol.44 , pp. 43-52
    • Meeks-Wagner, D.1    Hartwell, L.H.2
  • 46
    • 0345541427 scopus 로고
    • Tymediated gene expression of the LYS2 and HIS4 genes of Saccharomyces cerevisiae is controlled by the same SPT genes
    • Simchen, G., F. Winston, C. A. Styles, and G. R. Fink, 1984 Tymediated gene expression of the LYS2 and HIS4 genes of Saccharomyces cerevisiae is controlled by the same SPT genes. Proc. Natl. Acad. Sci. USA 81: 2431-2434.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2431-2434
    • Simchen, G.1    Winston, F.2    Styles, C.A.3    Fink, G.R.4
  • 47
    • 78649713364 scopus 로고    scopus 로고
    • A tandem SH2 domain in transcription elongation factor Spt6 binds the phosphorylated RNA polymerase II CTD
    • Sun, M., L. Lariviere, S. Dengl, A. Mayer, and P. Cramer, 2010 A tandem SH2 domain in transcription elongation factor Spt6 binds the phosphorylated RNA polymerase II CTD. J. Biol. Chem. 285: 1597-1603.
    • (2010) J. Biol. Chem , vol.285 , pp. 1597-1603
    • Sun, M.1    Lariviere, L.2    Dengl, S.3    Mayer, A.4    Cramer, P.5
  • 48
    • 79952269552 scopus 로고    scopus 로고
    • Transcription regulation by the noncoding RNA SRG1 requires Spt2-dependent chromatin deposition in the wake of RNA polymerase II
    • Thebault, P., G. Boutin, W. Bhat, A. Rufiange, J. Martens et al., 2011 Transcription regulation by the noncoding RNA SRG1 requires Spt2-dependent chromatin deposition in the wake of RNA polymerase II. Mol. Cell. Biol. 31: 1288-1300.
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1288-1300
    • Thebault, P.1    Boutin, G.2    Bhat, W.3    Rufiange, A.4    Martens, J.5
  • 49
    • 33646153980 scopus 로고    scopus 로고
    • The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition
    • VanDemark, A. P., M. Blanksma, E. Ferris, A. Heroux, C. P. Hill et al., 2006 The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition. Mol. Cell 22: 363-374.
    • (2006) Mol. Cell , vol.22 , pp. 363-374
    • VanDemark, A.P.1    Blanksma, M.2    Ferris, E.3    Heroux, A.4    Hill, C.P.5
  • 50
    • 41949125350 scopus 로고    scopus 로고
    • Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits
    • VanDemark, A. P., H. Xin, L. McCullough, R. Rawlins, S. Bentley et al., 2008 Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits. J. Biol. Chem. 283: 5058-5068.
    • (2008) J. Biol. Chem , vol.283 , pp. 5058-5068
    • VanDemark, A.P.1    Xin, H.2    McCullough, L.3    Rawlins, R.4    Bentley, S.5
  • 51
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White, C. L., R. K. Suto, and K. Luger, 2001 Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 20: 5207-5218.
    • (2001) EMBO J , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 52
    • 79955844395 scopus 로고    scopus 로고
    • The histone chaperone FACT: Structural insights and mechanisms for nucleosome reorganization
    • Winkler, D. D., and K. Luger, 2011 The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization. J. Biol. Chem. 286: 18369-18374.
    • (2011) J. Biol. Chem , vol.286 , pp. 18369-18374
    • Winkler, D.D.1    Luger, K.2
  • 53
    • 82355184456 scopus 로고    scopus 로고
    • The histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events
    • Winkler, D. D., U. M. Muthurajan, A. R. Hieb, and K. Luger, 2011 The histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events. J. Biol. Chem. 286: 41883-41892.
    • (2011) J. Biol. Chem , vol.286 , pp. 41883-41892
    • Winkler, D.D.1    Muthurajan, U.M.2    Hieb, A.R.3    Luger, K.4
  • 54
    • 68349131435 scopus 로고    scopus 로고
    • yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement
    • Xin, H., S. Takahata,M. Blanksma, L. McCullough, D. J. Stillman et al., 2009 yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement. Mol. Cell 35: 365- 376.
    • (2009) Mol. Cell , vol.35 , pp. 365-376
    • Xin, H.1    Takahata, S.2    Blanksma, M.3    McCullough, L.4    Stillman, D.J.5
  • 55
    • 33846525436 scopus 로고    scopus 로고
    • The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export
    • Yoh, S. M., H. Cho, L. Pickle, R. M. Evans, and K. A. Jones, 2007 The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export. Genes Dev. 21: 160-174.
    • (2007) Genes Dev , vol.21 , pp. 160-174
    • Yoh, S.M.1    Cho, H.2    Pickle, L.3    Evans, R.M.4    Jones, K.A.5
  • 56
    • 58049206591 scopus 로고    scopus 로고
    • The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation
    • Yoh, S. M., J. S. Lucas, and K. A. Jones, 2008 The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation. Genes Dev. 22: 3422-3434.
    • (2008) Genes Dev , vol.22 , pp. 3422-3434
    • Yoh, S.M.1    Lucas, J.S.2    Jones, K.A.3
  • 57
    • 38949154793 scopus 로고    scopus 로고
    • Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II
    • Zhang, L., A. G. Fletcher, V. Cheung, F. Winston, and L. A. Stargell, 2008 Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II. Mol. Cell. Biol. 28: 1393-1403.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 1393-1403
    • Zhang, L.1    Fletcher, A.G.2    Cheung, V.3    Winston, F.4    Stargell, L.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.