메뉴 건너뛰기




Volumn 110, Issue 19, 2013, Pages 7654-7659

Histone chaperone FACT action during transcription through chromatin by RNA polymerase II

Author keywords

DNA uncoiling; Dynamics; Elongation; Mechanism

Indexed keywords

CELL DNA; CHAPERONE; DIMER; FACILITATES CHROMATIN TRANSCRIPTION FACTOR; HISTONE H2A; HISTONE H2B; OCTAMER TRANSCRIPTION FACTOR; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 84877322380     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1222198110     Document Type: Article
Times cited : (160)

References (39)
  • 1
    • 0030920334 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein
    • Wittmeyer J, Formosa T (1997) The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein. Mol Cell Biol 17(7): 4178-4190.
    • (1997) Mol Cell Biol , vol.17 , Issue.7 , pp. 4178-4190
    • Wittmeyer, J.1    Formosa, T.2
  • 2
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D (1998) FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92(1): 105-116.
    • (1998) Cell , vol.92 , Issue.1 , pp. 105-116
    • Orphanides, G.1    Leroy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 3
    • 0026782131 scopus 로고
    • Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez M, Dong F, Ausio J (1992) Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1. J Biol Chem 267(27): 19587-19595.
    • (1992) J Biol Chem , vol.267 , Issue.27 , pp. 19587-19595
    • Garcia-Ramirez, M.1    Dong, F.2    Ausio, J.3
  • 4
    • 80051734288 scopus 로고    scopus 로고
    • Curaxins: Anticancer compounds that simultaneously suppress NF-κB and activate p53 by targeting FACT
    • Gasparian AV, et al. (2011) Curaxins: Anticancer compounds that simultaneously suppress NF-κB and activate p53 by targeting FACT. Sci Transl Med 3(95):95ra74.
    • (2011) Sci Transl Med , vol.3 , Issue.95
    • Gasparian, A.V.1
  • 5
    • 0033566129 scopus 로고    scopus 로고
    • The chromatinspecific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
    • Orphanides G, Wu WH, Lane WS, Hampsey M, Reinberg D (1999) The chromatinspecific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature 400(6741): 284-288.
    • (1999) Nature , vol.400 , Issue.6741 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 6
    • 0041828954 scopus 로고    scopus 로고
    • FACT facilitates transcription-dependent nucleosome alteration
    • Belotserkovskaya R, et al. (2003) FACT facilitates transcription- dependent nucleosome alteration. Science 301(5636): 1090-1093.
    • (2003) Science , vol.301 , Issue.5636 , pp. 1090-1093
    • Belotserkovskaya, R.1
  • 7
    • 0042830962 scopus 로고    scopus 로고
    • Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo
    • Saunders A, et al. (2003) Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo. Science 301(5636): 1094-1096.
    • (2003) Science , vol.301 , Issue.5636 , pp. 1094-1096
    • Saunders, A.1
  • 8
    • 0242579933 scopus 로고    scopus 로고
    • The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo
    • Mason PB, Struhl K (2003) The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo. Mol Cell Biol 23(22): 8323-8333.
    • (2003) Mol Cell Biol , vol.23 , Issue.22 , pp. 8323-8333
    • Mason, P.B.1    Struhl, K.2
  • 9
    • 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, 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(4): 1557-1571.
    • (2002) Genetics , vol.162 , Issue.4 , pp. 1557-1571
    • Formosa, T.1
  • 10
    • 56849114880 scopus 로고    scopus 로고
    • Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome
    • Cheung V, et al. (2008) Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome. PLoS Biol 6(11):e277.
    • (2008) PLoS Biol , vol.6 , Issue.11
    • Cheung, V.1
  • 11
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan CD, Laprade L, Winston F (2003) Transcription elongation factors repress transcription initiation from cryptic sites. Science 301(5636): 1096-1099.
    • (2003) Science , vol.301 , Issue.5636 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 12
    • 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, et al. (2011) Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone. Genetics 188(4): 835-846.
    • (2011) Genetics , vol.188 , Issue.4 , pp. 835-846
    • McCullough, L.1
  • 13
    • 68349131435 scopus 로고    scopus 로고
    • YFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement
    • Xin H, et al. (2009) yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement. Mol Cell 35(3): 365-376.
    • (2009) Mol Cell , vol.35 , Issue.3 , pp. 365-376
    • Xin, H.1
  • 14
    • 33750442129 scopus 로고    scopus 로고
    • Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II
    • Bondarenko VA, et al. (2006) Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II. Mol Cell 24(3): 469-479.
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 469-479
    • Bondarenko, V.A.1
  • 15
    • 71449127067 scopus 로고    scopus 로고
    • Mechanism of chromatin remodeling and recovery during passage of RNA polymerase II
    • Kulaeva OI, et al. (2009) Mechanism of chromatin remodeling and recovery during passage of RNA polymerase II. Nat Struct Mol Biol 16(12): 1272-1278.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.12 , pp. 1272-1278
    • Kulaeva, O.I.1
  • 16
    • 34147168036 scopus 로고    scopus 로고
    • Transcription through chromatin by RNA polymerase II: Histone displacement and exchange
    • Kulaeva OI, Gaykalova DA, Studitsky VM (2007) Transcription through chromatin by RNA polymerase II: Histone displacement and exchange. Mutat Res 618(1-2): 116-129.
    • (2007) Mutat Res , vol.618 , Issue.1-2 , pp. 116-129
    • Kulaeva, O.I.1    Gaykalova, D.A.2    Studitsky, V.M.3
  • 17
    • 77954934291 scopus 로고    scopus 로고
    • RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones
    • Kulaeva OI, Hsieh FK, Studitsky VM (2010) RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones. Proc Natl Acad Sci USA 107(25): 11325-11330.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.25 , pp. 11325-11330
    • Kulaeva, O.I.1    Hsieh, F.K.2    Studitsky, V.M.3
  • 18
    • 79952263239 scopus 로고    scopus 로고
    • Mechanism of histone survival during transcription by RNA polymerase II
    • Kulaeva OI, Studitsky VM (2010) Mechanism of histone survival during transcription by RNA polymerase II. Transcription 1(2): 85-88.
    • (2010) Transcription , vol.1 , Issue.2 , pp. 85-88
    • Kulaeva, O.I.1    Studitsky, V.M.2
  • 19
    • 77949548012 scopus 로고    scopus 로고
    • The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone-DNA interactions
    • Andrews AJ, Chen X, Zevin A, Stargell LA, Luger K (2010) The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone-DNA interactions. Mol Cell 37(6): 834-842.
    • (2010) Mol Cell , vol.37 , Issue.6 , pp. 834-842
    • Andrews, A.J.1    Chen, X.2    Zevin, A.3    Stargell, L.A.4    Luger, K.5
  • 20
    • 59649112972 scopus 로고    scopus 로고
    • High-resolution dynamic mapping of histone-DNA interactions in a nucleosome
    • Hall MA, et al. (2009) High-resolution dynamic mapping of histone-DNA interactions in a nucleosome. Nat Struct Mol Biol 16(2): 124-129.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.2 , pp. 124-129
    • Hall, M.A.1
  • 21
    • 77956231587 scopus 로고    scopus 로고
    • Histone Sin mutations promote nucleosome traversal and histone displacement by RNA polymerase II
    • Hsieh FK, Fisher M, Ujvári A, Studitsky VM, Luse DS (2010) Histone Sin mutations promote nucleosome traversal and histone displacement by RNA polymerase II. EMBO Rep 11(9): 705-710.
    • (2010) EMBO Rep , vol.11 , Issue.9 , pp. 705-710
    • Hsieh, F.K.1    Fisher, M.2    Ujvári, A.3    Studitsky, V.M.4    Luse, D.S.5
  • 22
    • 79960100503 scopus 로고    scopus 로고
    • The mechanism of nucleosome traversal by RNA polymerase II: Roles for template uncoiling and transcript elongation factors
    • Luse DS, Studitsky VM (2011) The mechanism of nucleosome traversal by RNA polymerase II: Roles for template uncoiling and transcript elongation factors. RNA Biol 8(4): 581-585.
    • (2011) RNA Biol , vol.8 , Issue.4 , pp. 581-585
    • Luse, D.S.1    Studitsky, V.M.2
  • 23
    • 0141704307 scopus 로고    scopus 로고
    • Bacterial polymerase and yeast polymerase II use similar mechanisms for transcription through nucleosomes
    • Walter W, Kireeva ML, Studitsky VM, Kashlev M (2003) Bacterial polymerase and yeast polymerase II use similar mechanisms for transcription through nucleosomes. J Biol Chem 278(38): 36148-36156.
    • (2003) J Biol Chem , vol.278 , Issue.38 , pp. 36148-36156
    • Walter, W.1    Kireeva, M.L.2    Studitsky, V.M.3    Kashlev, M.4
  • 24
    • 79956057367 scopus 로고    scopus 로고
    • A polar barrier to transcription can be circumvented by remodeler-induced nucleosome translocation
    • Gaykalova DA, et al. (2011) A polar barrier to transcription can be circumvented by remodeler-induced nucleosome translocation. Nucleic Acids Res 39(9): 3520-3528.
    • (2011) Nucleic Acids Res , vol.39 , Issue.9 , pp. 3520-3528
    • Gaykalova, D.A.1
  • 25
    • 77952995507 scopus 로고    scopus 로고
    • Experimental and computational analysis of DNA unwinding and polymerization kinetics
    • Pandey M, Levin MK, Patel SS (2010) Experimental and computational analysis of DNA unwinding and polymerization kinetics. Methods Mol Biol 587: 57-83.
    • (2010) Methods Mol Biol , vol.587 , pp. 57-83
    • Pandey, M.1    Levin, M.K.2    Patel, S.S.3
  • 26
    • 0025877255 scopus 로고
    • Transcription on nucleosomal templates by RNA polymerase II in vitro: Inhibition of elongation with enhancement of sequence-specific pausing
    • Izban MG, Luse DS (1991) Transcription on nucleosomal templates by RNA polymerase II in vitro: Inhibition of elongation with enhancement of sequence-specific pausing. Genes Dev 5(4): 683-696.
    • (1991) Genes Dev , vol.5 , Issue.4 , pp. 683-696
    • Izban, M.G.1    Luse, D.S.2
  • 27
    • 15944393126 scopus 로고    scopus 로고
    • Nature of the nucleosomal barrier to RNA polymerase II
    • Kireeva ML, et al. (2005) Nature of the nucleosomal barrier to RNA polymerase II. Mol Cell 18(1): 97-108.
    • (2005) Mol Cell , vol.18 , Issue.1 , pp. 97-108
    • Kireeva, M.L.1
  • 28
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • Kireeva ML, et al. (2002) Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription. Mol Cell 9(3): 541-552.
    • (2002) Mol Cell , vol.9 , Issue.3 , pp. 541-552
    • Kireeva, M.L.1
  • 29
    • 0027220943 scopus 로고
    • Lifetime of the histone octamer studied by continuous-flow quasielastic light scattering: Test of a model for nucleosome transcription
    • Feng HP, Scherl DS, Widom J (1993) Lifetime of the histone octamer studied by continuous-flow quasielastic light scattering: Test of a model for nucleosome transcription. Biochemistry 32(30): 7824-7831.
    • (1993) Biochemistry , vol.32 , Issue.30 , pp. 7824-7831
    • Feng, H.P.1    Scherl, D.S.2    Widom, J.3
  • 30
    • 0242413271 scopus 로고    scopus 로고
    • Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes
    • Ruone S, Rhoades AR, Formosa T (2003) Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes. J Biol Chem 278(46): 45288-45295.
    • (2003) J Biol Chem , vol.278 , Issue.46 , pp. 45288-45295
    • Ruone, S.1    Rhoades, A.R.2    Formosa, T.3
  • 31
    • 33746856074 scopus 로고    scopus 로고
    • De FACTo nucleosome dynamics
    • Reinberg D, Sims RJ, 3rd (2006) de FACTo nucleosome dynamics. J Biol Chem 281(33): 23297-23301.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23297-23301
    • Reinberg, D.1    Sims Iii, R.J.2
  • 32
    • 79955844395 scopus 로고    scopus 로고
    • The histone chaperone FACT: Structural insights and mechanisms for nucleosome reorganization
    • Winkler DD, Luger K (2011) The histone chaperone FACT: Structural insights and mechanisms for nucleosome reorganization. J Biol Chem 286(21): 18369-18374.
    • (2011) J Biol Chem , vol.286 , Issue.21 , pp. 18369-18374
    • Winkler, D.D.1    Luger, K.2
  • 33
    • 79958078987 scopus 로고    scopus 로고
    • Mutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3
    • Myers CN, et al. (2011) Mutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3. PLoS ONE 6(6):e20847.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Myers, C.N.1
  • 34
    • 68349148027 scopus 로고    scopus 로고
    • Histone chaperone spt16 promotes redeposition of the original h3-h4 histones evicted by elongating RNA polymerase
    • Jamai A, Puglisi A, Strubin M (2009) Histone chaperone spt16 promotes redeposition of the original h3-h4 histones evicted by elongating RNA polymerase. Mol Cell 35(3): 377-383.
    • (2009) Mol Cell , vol.35 , Issue.3 , pp. 377-383
    • Jamai, A.1    Puglisi, A.2    Strubin, M.3
  • 35
    • 82355184456 scopus 로고    scopus 로고
    • Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events
    • Winkler DD, Muthurajan UM, Hieb AR, Luger K (2011) Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events. J Biol Chem 286(48): 41883-41892.
    • (2011) J Biol Chem , vol.286 , Issue.48 , pp. 41883-41892
    • Winkler, D.D.1    Muthurajan, U.M.2    Hieb, A.R.3    Luger, K.4
  • 37
    • 1542334851 scopus 로고    scopus 로고
    • Reconstitution of nucleosome core particles from recombinant histones and DNA
    • Dyer PN, et al. (2004) Reconstitution of nucleosome core particles from recombinant histones and DNA. Methods Enzymol 375: 23-44.
    • (2004) Methods Enzymol , vol.375 , pp. 23-44
    • Dyer, P.N.1
  • 38
    • 60549105802 scopus 로고    scopus 로고
    • Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson KA, Simpson ZB, Blom T (2009) Global Kinetic Explorer: A new computer program for dynamic simulation and fitting of kinetic data. Anal Biochem 387(1): 20-29.
    • (2009) Anal Biochem , vol.387 , Issue.1 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 39
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace Explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson KA, Simpson ZB, Blom T (2009) FitSpace Explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data. Anal Biochem 387(1): 30-41.
    • (2009) Anal Biochem , vol.387 , Issue.1 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.