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Volumn 42, Issue 9, 2014, Pages 5532-5542

Scm3 deposits a (Cse4-H4)2 tetramer onto DNA through a Cse4-H4 dimer intermediate

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE H2A; HISTONE H2B; PROTEIN SCM3; UNCLASSIFIED DRUG;

EID: 84901381917     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku205     Document Type: Article
Times cited : (12)

References (77)
  • 1
    • 0037459109 scopus 로고    scopus 로고
    • Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling
    • DOI 10.1016/S0092-8674(03)00115-6
    • Cleveland, D.W., Mao, Y. and Sullivan, K.F. (2003) Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling. Cell, 112, 407-421. (Pubitemid 36263076
    • (2003) Cell , vol.112 , Issue.4 , pp. 407-421
    • Cleveland, D.W.1    Mao, Y.2    Sullivan, K.F.3
  • 2
    • 0020325948 scopus 로고
    • Nucleotide sequence comparisons and functional analysis of yeast centromere DNAs
    • Fitzgerald-Hayes, M., Clarke, L. and Carbon, J. (1982) Nucleotide sequence comparisons and functional analysis of yeast centromere DNAs. Cell, 29, 235-244. (Pubitemid 12027685
    • (1982) Cell , vol.29 , Issue.1 , pp. 235-244
    • Fitzgerald-Hayes, M.1    Clarke, L.2    Carbon, J.3
  • 3
    • 0024406285 scopus 로고
    • A 125-base-pair CEN6 DNA fragment is sufficient for complete meiotic and mitotic centromere functions in Saccharomyces cerevisiae
    • Cottarel, G., Shero, J.H., Hieter, P. and Hegemann, J.H. (1989) A 125-base-pair CEN6 DNA fragment is sufficient for complete meiotic and mitotic centromere functions in Saccharomyces cerevisiae. Mol. Cell. Biol., 9, 3342-3349.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3342-3349
    • Cottarel, G.1    Shero, J.H.2    Hieter, P.3    Hegemann, J.H.4
  • 5
    • 84859599040 scopus 로고    scopus 로고
    • Point centromeres of Saccharomyces harbor single centromere-specific nucleosomes
    • Henikoff, S. and Henikoff, J.G. (2012) "Point" centromeres of Saccharomyces harbor single centromere-specific nucleosomes. Genetics, 190, 1575-1577.
    • (2012) Genetics , vol.190 , pp. 1575-1577
    • Henikoff, S.1    Henikoff, J.G.2
  • 6
    • 84861849547 scopus 로고    scopus 로고
    • Perfect and imperfect nucleosome positioning in yeast
    • Cole, H.A., Nagarajavel, V. and Clark, D.J. (2012) Perfect and imperfect nucleosome positioning in yeast. Biochim. Biophys. Acta, 1819, 639-643.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 639-643
    • Cole, H.A.1    Nagarajavel, V.2    Clark, D.J.3
  • 8
    • 0023275058 scopus 로고
    • A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones
    • DOI 10.1083/jcb.104.4.805
    • Palmer, D.K., O'Day, K., Wener, M.H., Andrews, B.S. and Margolis, R.L. (1987) A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones. J. Cell Biol., 104, 805-815. (Pubitemid 17068653
    • (1987) Journal of Cell Biology , vol.104 , Issue.4 , pp. 805-815
    • Palmer, D.K.1    O'Day, K.2    Wener, M.H.3
  • 9
    • 0028946805 scopus 로고
    • A mutation in CSE4, an essential gene encoding a novel chromatin-Associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis
    • Stoler, S., Keith, K.C., Curnick, K.E. and Fitzgerald-Hayes, M. (1995) A mutation in CSE4, an essential gene encoding a novel chromatin-Associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis. Genes Dev., 9, 573-586.
    • (1995) Genes Dev. , vol.9 , pp. 573-586
    • Stoler, S.1    Keith, K.C.2    Curnick, K.E.3    Fitzgerald-Hayes, M.4
  • 11
    • 0035340898 scopus 로고    scopus 로고
    • Epigenetic analysis of kinetochore assembly on variant human centromeres
    • Warburton, P.E. (2001) Epigenetic analysis of kinetochore assembly on variant human centromeres. Trends Genet., 17, 243-247.
    • (2001) Trends Genet. , vol.17 , pp. 243-247
    • Warburton, P.E.1
  • 15
    • 77956897642 scopus 로고    scopus 로고
    • The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres
    • Sekulic, N., Bassett, E.A., Rogers, D.J. and Black, B.E. (2010) The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres. Nature, 467, 347-351.
    • (2010) Nature , vol.467 , pp. 347-351
    • Sekulic, N.1    Bassett, E.A.2    Rogers, D.J.3    Black, B.E.4
  • 16
    • 79956267847 scopus 로고    scopus 로고
    • Structure and Scm3-mediated assembly of budding yeast centromeric nucleosomes
    • Dechassa, M.L., Wyns, K., Li, M., Hall, M.A., Wang, M.D. and Luger, K. (2011) Structure and Scm3-mediated assembly of budding yeast centromeric nucleosomes. Nat. Commun., 2, 313.
    • (2011) Nat. Commun. , vol.2 , pp. 313
    • Dechassa, M.L.1    Wyns, K.2    Li, M.3    Hall, M.A.4    Wang, M.D.5    Luger, K.6
  • 17
    • 79951711785 scopus 로고    scopus 로고
    • Biophysical characterization of the centromere-specific nucleosome from budding yeast
    • Kingston, I.J., Yung, J.S. and Singleton, M.R. (2011) Biophysical characterization of the centromere-specific nucleosome from budding yeast. J. Biol. Chem., 286, 4021-4026.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4021-4026
    • Kingston, I.J.1    Yung, J.S.2    Singleton, M.R.3
  • 20
    • 80052849224 scopus 로고    scopus 로고
    • In vitro centromere and kinetochore assembly on defined chromatin templates
    • Guse, A., Carroll, C.W., Moree, B., Fuller, C.J. and Straight, A.F. (2011) In vitro centromere and kinetochore assembly on defined chromatin templates. Nature, 477, 354-358.
    • (2011) Nature , vol.477 , pp. 354-358
    • Guse, A.1    Carroll, C.W.2    Moree, B.3    Fuller, C.J.4    Straight, A.F.5
  • 21
    • 34548267126 scopus 로고    scopus 로고
    • Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells
    • Dalal, Y., Wang, H., Lindsay, S. and Henikoff, S. (2007) Tetrameric structure of centromeric nucleosomes in interphase Drosophila cells. PLoS Biol., 5, e218.
    • (2007) PLoS Biol. , vol.5
    • Dalal, Y.1    Wang, H.2    Lindsay, S.3    Henikoff, S.4
  • 22
    • 34250316190 scopus 로고    scopus 로고
    • Scm3 is essential to recruit the histone h3 variant cse4 to centromeres and to maintain a functional kinetochore
    • Camahort, R., Li, B., Florens, L., Swanson, S.K., Washburn, M.P. and Gerton, J.L. (2007) Scm3 is essential to recruit the histone h3 variant cse4 to centromeres and to maintain a functional kinetochore. Mol. Cell, 26, 853-865.
    • (2007) Mol. Cell , vol.26 , pp. 853-865
    • Camahort, R.1    Li, B.2    Florens, L.3    Swanson, S.K.4    Washburn, M.P.5    Gerton, J.L.6
  • 23
    • 34250173486 scopus 로고    scopus 로고
    • Nonhistone scm3 and histones cenh3-h4 assemble the core of centromere-specific nucleosomes
    • DOI 10.1016/j.cell.2007.04.026, PII S0092867407005338
    • Mizuguchi, G., Xiao, H., Wisniewski, J., Smith, M.M. and Wu, C. (2007) Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes. Cell, 129, 1153-1164. (Pubitemid 46900852
    • (2007) Cell , vol.129 , Issue.6 , pp. 1153-1164
    • Mizuguchi, G.1    Xiao, H.2    Wisniewski, J.3    Smith, M.M.4    Wu, C.5
  • 24
    • 67649664594 scopus 로고    scopus 로고
    • Centromeric nucleosomes induce positive DNA supercoils
    • Furuyama, T. and Henikoff, S. (2009) Centromeric nucleosomes induce positive DNA supercoils. Cell, 138, 104-113.
    • (2009) Cell , vol.138 , pp. 104-113
    • Furuyama, T.1    Henikoff, S.2
  • 26
    • 84877577424 scopus 로고    scopus 로고
    • Octameric CENP-A nucleosomes are present at human centromeres throughout the cell cycle
    • Padeganeh, A., Ryan, J., Boisvert, J., Ladouceur, A.M., Dorn, J.F. and Maddox, P.S. (2013) Octameric CENP-A nucleosomes are present at human centromeres throughout the cell cycle. Curr. Biol., 23, 764-769.
    • (2013) Curr. Biol. , vol.23 , pp. 764-769
    • Padeganeh, A.1    Ryan, J.2    Boisvert, J.3    Ladouceur, A.M.4    Dorn, J.F.5    Maddox, P.S.6
  • 27
    • 84863638252 scopus 로고    scopus 로고
    • Histone h3 localizes to the centromeric DNA in budding yeast
    • Lochmann, B. and Ivanov, D. (2012) Histone h3 localizes to the centromeric DNA in budding yeast. PLoS Genet., 8, e1002739.
    • (2012) PLoS Genet. , vol.8
    • Lochmann, B.1    Ivanov, D.2
  • 29
    • 84864262744 scopus 로고    scopus 로고
    • Cell-cycle-coupled structural oscillation of centromeric nucleosomes in yeast
    • Shivaraju, M., Unruh, J.R., Slaughter, B.D., Mattingly, M., Berman, J. and Gerton, J.L. (2012) Cell-cycle-coupled structural oscillation of centromeric nucleosomes in yeast. Cell, 150, 304-316.
    • (2012) Cell , vol.150 , pp. 304-316
    • Shivaraju, M.1    Unruh, J.R.2    Slaughter, B.D.3    Mattingly, M.4    Berman, J.5    Gerton, J.L.6
  • 30
    • 84877583970 scopus 로고    scopus 로고
    • The budding yeast point centromere associates with two Cse4 molecules during mitosis
    • Aravamudhan, P., Felzer-Kim, I. and Joglekar, A.P. (2013) The budding yeast point centromere associates with two Cse4 molecules during mitosis. Curr. Biol., 23, 770-774.
    • (2013) Curr. Biol. , vol.23 , pp. 770-774
    • Aravamudhan, P.1    Felzer-Kim, I.2    Joglekar, A.P.3
  • 31
    • 34547112848 scopus 로고    scopus 로고
    • Scm3 an essential saccharomyces cerevisiae centromere protein required for g2/m progression and cse4 localization
    • Stoler, S., Rogers, K., Weitze, S., Morey, L., Fitzgerald-Hayes, M. and Baker, R.E. (2007) Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization. PNAS, 104, 10571-10576.
    • (2007) PNAS , vol.104 , pp. 10571-10576
    • Stoler, S.1    Rogers, K.2    Weitze, S.3    Morey, L.4    Fitzgerald-Hayes, M.5    Baker, R.E.6
  • 32
    • 59649107021 scopus 로고    scopus 로고
    • Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin
    • Williams, J.S., Hayashi, T., Yanagida, M. and Russell, P. (2009) Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin. Mol. Cell, 33, 287-298.
    • (2009) Mol. Cell , vol.33 , pp. 287-298
    • Williams, J.S.1    Hayashi, T.2    Yanagida, M.3    Russell, P.4
  • 36
    • 76549131870 scopus 로고    scopus 로고
    • HJURP binds CENP-A via a highly conserved N-Terminal domain and mediates its deposition at centromeres
    • Shuaib, M., Ouararhni, K., Dimitrov, S. and Hamiche, A. (2010) HJURP binds CENP-A via a highly conserved N-Terminal domain and mediates its deposition at centromeres. PNAS, 107, 1349-1354.
    • (2010) PNAS , vol.107 , pp. 1349-1354
    • Shuaib, M.1    Ouararhni, K.2    Dimitrov, S.3    Hamiche, A.4
  • 40
    • 79951484009 scopus 로고    scopus 로고
    • The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation
    • Bowman, A., Ward, R., Wiechens, N., Singh, V., El-Mkami, H., Norman, D.G. and Owen-Hughes, T. (2011) The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation. Mol. Cell, 41, 398-408.
    • (2011) Mol. Cell , vol.41 , pp. 398-408
    • Bowman, A.1    Ward, R.2    Wiechens, N.3    Singh, V.4    El-Mkami, H.5    Norman, D.G.6    Owen-Hughes, T.7
  • 41
    • 84883785467 scopus 로고    scopus 로고
    • Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form
    • Darcy, S., Martin, K.W., Panchenko, T., Chen, X., Bergeron, S., Stargell, L.A., Black, B.E. and Luger, K. (2013) Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form. Mol. Cell, 51, 662-677.
    • (2013) Mol. Cell , vol.51 , pp. 662-677
    • Darcy, S.1    Martin, K.W.2    Panchenko, T.3    Chen, X.4    Bergeron, S.5    Stargell, L.A.6    Black, B.E.7    Luger, K.8
  • 42
    • 79959331606 scopus 로고    scopus 로고
    • Recognition of the centromere-specific histone Cse4 by the chaperone Scm3
    • Cho, U.S. and Harrison, S.C. (2011) Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. PNAS, 108, 9367-9371.
    • (2011) PNAS , vol.108 , pp. 9367-9371
    • Cho, U.S.1    Harrison, S.C.2
  • 44
    • 79955678169 scopus 로고    scopus 로고
    • Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP
    • Hu, H., Liu, Y., Wang, M., Fang, J., Huang, H., Yang, N., Li, Y., Wang, J., Yao, X., Shi, Y. et al. (2011) Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev., 25, 901-906.
    • (2011) Genes Dev. , vol.25 , pp. 901-906
    • Hu, H.1    Liu, Y.2    Wang, M.3    Fang, J.4    Huang, H.5    Yang, N.6    Li, Y.7    Wang, J.8    Yao, X.9    Shi, Y.10
  • 45
    • 84872832798 scopus 로고    scopus 로고
    • Identification of functionally conserved regions in the structure of the chaperone/Cen H3/H4 complex
    • Hong, J., Feng, H., Zhou, Z., Ghirlando, R. and Bai, Y. (2012) Identification of functionally conserved regions in the structure of the chaperone/Cen H3/H4 complex. J. Mol. Biol., 425, 536-545.
    • (2012) J. Mol. Biol. , vol.425 , pp. 536-545
    • Hong, J.1    Feng, H.2    Zhou, Z.3    Ghirlando, R.4    Bai, Y.5
  • 46
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary, P.T. and Widom, J. (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol., 276, 19-42.
    • (1998) J. Mol. Biol. , vol.276 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 47
    • 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
  • 48
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • DOI 10.1016/S0076-6879(99)04003-3
    • Luger, K., Rechsteiner, T.J. and Richmond, T.J. (1999) Preparation of nucleosome core particle from recombinant histones. Methods Enzymol., 304, 3-19. (Pubitemid 29268874
    • (1999) Methods in Enzymology , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 49
    • 84865310327 scopus 로고    scopus 로고
    • Quantifying chromatin-Associated interactions: The HI-FI system
    • Winkler, D.D., Luger, K. and Hieb, A.R. (2012) Quantifying chromatin-Associated interactions: The HI-FI system. Methods Enzymol., 512, 243-274.
    • (2012) Methods Enzymol. , vol.512 , pp. 243-274
    • Winkler, D.D.1    Luger, K.2    Hieb, A.R.3
  • 50
    • 84858419821 scopus 로고    scopus 로고
    • Fluorescence strategies for high-Throughput quantification of protein interactions
    • Hieb, A.R., Darcy, S., Kramer, M.A., White, A.E. and Luger, K. (2012) Fluorescence strategies for high-Throughput quantification of protein interactions. Nucleic Acids Res., 40, e33.
    • (2012) Nucleic Acids Res. , vol.40
    • Hieb, A.R.1    Darcy, S.2    Kramer, M.A.3    White, A.E.4    Luger, K.5
  • 52
    • 0036837670 scopus 로고    scopus 로고
    • High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2
    • Kassabov, S.R., Henry, N.M., Zofall, M., Tsukiyama, T. and Bartholomew, B. (2002) High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2. Mol. Cell. Biol., 22, 7524-7534.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7524-7534
    • Kassabov, S.R.1    Henry, N.M.2    Zofall, M.3    Tsukiyama, T.4    Bartholomew, B.5
  • 55
    • 82355184456 scopus 로고    scopus 로고
    • Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events
    • Winkler, D.D., Muthurajan, U.M., Hieb, A.R. and Luger, K. (2011) 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
  • 56
    • 84869061403 scopus 로고    scopus 로고
    • Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition
    • Winkler, D.D., Zhou, H., Dar, M.A., Zhang, Z. and Luger, K. (2012) Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition. Nucleic Acids Res., 40, 10139-10149.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10139-10149
    • Winkler, D.D.1    Zhou, H.2    Dar, M.A.3    Zhang, Z.4    Luger, K.5
  • 57
    • 84871212864 scopus 로고    scopus 로고
    • CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA
    • Liu, W.H., Roemer, S.C., Port, A.M. and Churchill, M.E. (2012) CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA. Nucleic Acids Res., 40, 11229-11239.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11229-11239
    • Liu, W.H.1    Roemer, S.C.2    Port, A.M.3    Churchill, M.E.4
  • 58
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • DOI 10.1038/38444
    • 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 A resolution. Nature, 389, 251-260. (Pubitemid 27406632
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 59
    • 84855905982 scopus 로고    scopus 로고
    • Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4
    • Bowman, A. and Owen-Hughes, T. (2012) Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. Methods Mol. Biol., 833, 373-387.
    • (2012) Methods Mol. Biol. , vol.833 , pp. 373-387
    • Bowman, A.1    Owen-Hughes, T.2
  • 60
    • 79960897478 scopus 로고    scopus 로고
    • Nonhistone Scm3 binds to AT-rich DNA to organize atypical centromeric nucleosome of budding yeast
    • Xiao, H., Mizuguchi, G., Wisniewski, J., Huang, Y., Wei, D. and Wu, C. (2011) Nonhistone Scm3 binds to AT-rich DNA to organize atypical centromeric nucleosome of budding yeast. Mol. Cell, 43, 369-380.
    • (2011) Mol. Cell , vol.43 , pp. 369-380
    • Xiao, H.1    Mizuguchi, G.2    Wisniewski, J.3    Huang, Y.4    Wei, D.5    Wu, C.6
  • 61
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • DOI 10.1093/emboj/20.18.5207
    • White, C.L., Suto, R.K. and Luger, K. (2001) Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J., 20, 5207-5218. (Pubitemid 32910915
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 62
    • 80052247642 scopus 로고    scopus 로고
    • The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes
    • Donham, D.C. 2nd, Scorgie, J.K. and Churchill, M.E. (2011) The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes. Nucleic Acids Res., 39, 5449-5458.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5449-5458
    • Donham II, D.C.1    Scorgie, J.K.2    Churchill, M.E.3
  • 63
    • 84881476542 scopus 로고    scopus 로고
    • Dimerization of the CENP-A assembly factor HJURP is required for centromeric nucleosome deposition
    • Zasadzinska, E., Barnhart-Dailey, M.C., Kuich, P.H. and Foltz, D.R. (2013) Dimerization of the CENP-A assembly factor HJURP is required for centromeric nucleosome deposition. EMBO J., 32, 2113-2124.
    • (2013) EMBO J. , vol.32 , pp. 2113-2124
    • Zasadzinska, E.1    Barnhart-Dailey, M.C.2    Kuich, P.H.3    Foltz, D.R.4
  • 64
    • 35848960342 scopus 로고    scopus 로고
    • Domain architectures of the Scm3p protein provide insights into centromere function and evolution
    • Aravind, L., Iyer, L.M. and Wu, C. (2007) Domain architectures of the Scm3p protein provide insights into centromere function and evolution. Cell Cycle, 6, 2511-2515. (Pubitemid 350058669
    • (2007) Cell Cycle , vol.6 , Issue.20 , pp. 2511-2515
    • Aravind, L.1    Iyer, L.M.2    Wu, C.3
  • 65
    • 33646589676 scopus 로고    scopus 로고
    • Chaperone-mediated assembly of centromeric chromatin in vitro
    • Furuyama, T., Dalal, Y. and Henikoff, S. (2006) Chaperone-mediated assembly of centromeric chromatin in vitro. PNAS, 103, 6172-6177.
    • (2006) PNAS , vol.103 , pp. 6172-6177
    • Furuyama, T.1    Dalal, Y.2    Henikoff, S.3
  • 69
    • 33947274529 scopus 로고    scopus 로고
    • Propagation of centromeric chromatin requires exit from mitosis
    • DOI 10.1083/jcb.200701066
    • Jansen, L.E., Black, B.E., Foltz, D.R. and Cleveland, D.W. (2007) Propagation of centromeric chromatin requires exit from mitosis. J. Cell Biol., 176, 795-805. (Pubitemid 46425540
    • (2007) Journal of Cell Biology , vol.176 , Issue.6 , pp. 795-805
    • Jansen, L.E.T.1    Black, B.E.2    Foltz, D.R.3    Cleveland, D.W.4
  • 70
    • 33846638827 scopus 로고    scopus 로고
    • Incorporation of Drosophila CID/CENP-A and CENP-C into centromeres during early embryonic anaphase
    • Schuh, M., Lehner, C.F. and Heidmann, S. (2007) Incorporation of Drosophila CID/CENP-A and CENP-C into centromeres during early embryonic anaphase. Curr. Biol., 17, 237-243.
    • (2007) Curr. Biol. , vol.17 , pp. 237-243
    • Schuh, M.1    Lehner, C.F.2    Heidmann, S.3
  • 72
    • 80053934686 scopus 로고    scopus 로고
    • CENP-C recruits M18BP1 to centromeres to promote CENP-A chromatin assembly
    • Moree, B., Meyer, C.B., Fuller, C.J. and Straight, A.F. (2011) CENP-C recruits M18BP1 to centromeres to promote CENP-A chromatin assembly. J. Cell Biol., 194, 855-871.
    • (2011) J. Cell Biol. , vol.194 , pp. 855-871
    • Moree, B.1    Meyer, C.B.2    Fuller, C.J.3    Straight, A.F.4
  • 74
    • 84875445835 scopus 로고    scopus 로고
    • Assembly in G1 phase and long-Term stability are unique intrinsic features of CENP-A nucleosomes
    • Bodor, D.L., Valente, L.P., Mata, J.F., Black, B.E. and Jansen, L.E. (2013) Assembly in G1 phase and long-Term stability are unique intrinsic features of CENP-A nucleosomes. Mol. Biol. Cell, 24, 923-932.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 923-932
    • Bodor, D.L.1    Valente, L.P.2    Mata, J.F.3    Black, B.E.4    Jansen, L.E.5
  • 75
    • 84855956123 scopus 로고    scopus 로고
    • H3.3 is deposited at centromeres in S phase as a placeholder for newly assembled CENP-A in G(1) phase
    • Dunleavy, E.M., Almouzni, G. and Karpen, G.H. (2011) H3.3 is deposited at centromeres in S phase as a placeholder for newly assembled CENP-A in G(1) phase. Nucleus, 2, 146-157.
    • (2011) Nucleus , vol.2 , pp. 146-157
    • Dunleavy, E.M.1    Almouzni, G.2    Karpen, G.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.