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Volumn 21, Issue 7, 2007, Pages 1294-1310

Nap1: Taking a closer look at a juggler protein of extraordinary skills

Author keywords

Histone chaperone; Nucleosome assembly; Transcription

Indexed keywords

CHAPERONE; DIMER; HISTONE; HISTONE H2A; HISTONE H2B; PROTEIN NAP1; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 34247619728     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.06-7199rev     Document Type: Review
Times cited : (101)

References (117)
  • 1
    • 0020816370 scopus 로고
    • A protein which facilitates assembly of nucleosomelike structures in vitro in mammalian cells
    • Ishimi, Y., Yasuda, H., Hirosumi, J., Hanaoka, F., and Yamada, M. (1983) A protein which facilitates assembly of nucleosomelike structures in vitro in mammalian cells. J. Biochem. (Tokyo) 94, 735-744
    • (1983) J. Biochem. (Tokyo) , vol.94 , pp. 735-744
    • Ishimi, Y.1    Yasuda, H.2    Hirosumi, J.3    Hanaoka, F.4    Yamada, M.5
  • 2
    • 0025816844 scopus 로고
    • Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro
    • Ishimi, Y., and Kikuchi, A. (1991) Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J. Biol. Chem. 266, 7025-7029
    • (1991) J. Biol. Chem , vol.266 , pp. 7025-7029
    • Ishimi, Y.1    Kikuchi, A.2
  • 3
    • 0029778870 scopus 로고    scopus 로고
    • ATP-facilitated chromatin assembly with a nucleo-plasmin-like protein from Drosophila melanogaster
    • Ito, T., Tyler, J. K., Bulger, M., Kobayashi, R., and Kadonaga, J. T. (1996) ATP-facilitated chromatin assembly with a nucleo-plasmin-like protein from Drosophila melanogaster. J. Biol. Chem. 271, 25041-25048
    • (1996) J. Biol. Chem , vol.271 , pp. 25041-25048
    • Ito, T.1    Tyler, J.K.2    Bulger, M.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 4
    • 20644462780 scopus 로고    scopus 로고
    • Biochemical characterization of the two nucleosome assembly proteins from Plasmodium falciparum
    • Chandra, B. R., Olivieri, A., Silvestrini, F., Alano, P., and Sharma, A. (2005) Biochemical characterization of the two nucleosome assembly proteins from Plasmodium falciparum. Mol. Biochem. Parasitol. 142, 237-247
    • (2005) Mol. Biochem. Parasitol , vol.142 , pp. 237-247
    • Chandra, B.R.1    Olivieri, A.2    Silvestrini, F.3    Alano, P.4    Sharma, A.5
  • 5
    • 33745194378 scopus 로고    scopus 로고
    • The two Plasmodium falciparum nucleosome assembly proteins play distinct roles in histone transport and chromatin assembly
    • Navadgi, V. M., Chandra, B. R., Mishra, P. C., and Sharma, A. (2006) The two Plasmodium falciparum nucleosome assembly proteins play distinct roles in histone transport and chromatin assembly. J. Biol. Chem. 281, 16978-16984
    • (2006) J. Biol. Chem , vol.281 , pp. 16978-16984
    • Navadgi, V.M.1    Chandra, B.R.2    Mishra, P.C.3    Sharma, A.4
  • 6
    • 22244443411 scopus 로고    scopus 로고
    • Protein interaction of nucleosome assembly protein 1 and casein kinase 2 during desiccation response in the insect-killing nematode Steinernema feltiae IS-6
    • Gal, T. Z., Glazer, I., Sherman, A., and Koltai, H. (2005) Protein interaction of nucleosome assembly protein 1 and casein kinase 2 during desiccation response in the insect-killing nematode Steinernema feltiae IS-6. J. Parasitol. 91, 691-693
    • (2005) J. Parasitol , vol.91 , pp. 691-693
    • Gal, T.Z.1    Glazer, I.2    Sherman, A.3    Koltai, H.4
  • 7
    • 0029563615 scopus 로고
    • Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean
    • Yoon, H. W., Kim, M. C., Lee, S. Y., Hwang, I., Bahk, J. D., Hong, J. C., Ishimi, Y., and Cho, M. J. (1995) Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean. Mol. Gen. Genet. 249, 465-473
    • (1995) Mol. Gen. Genet , vol.249 , pp. 465-473
    • Yoon, H.W.1    Kim, M.C.2    Lee, S.Y.3    Hwang, I.4    Bahk, J.D.5    Hong, J.C.6    Ishimi, Y.7    Cho, M.J.8
  • 8
    • 27244449653 scopus 로고    scopus 로고
    • Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants
    • Dong, A., Liu, Z., Zhu, Y., Yu, F., Li, Z., Cao, K., and Shen, W.-H. (2005) Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants. Plant Physiol. 138, 1446-1456
    • (2005) Plant Physiol , vol.138 , pp. 1446-1456
    • Dong, A.1    Liu, Z.2    Zhu, Y.3    Yu, F.4    Li, Z.5    Cao, K.6    Shen, W.-H.7
  • 9
    • 0037977936 scopus 로고    scopus 로고
    • Regulation of biosynthesis and intracellular localization of rice and tobacco homologues of nucleosome assembly protein 1
    • Dong, A., Zhu, Y., Yu, Y., Cao, K., Sun, C., and Shen, W. H. (2003) Regulation of biosynthesis and intracellular localization of rice and tobacco homologues of nucleosome assembly protein 1. Planta 216, 561-570
    • (2003) Planta , vol.216 , pp. 561-570
    • Dong, A.1    Zhu, Y.2    Yu, Y.3    Cao, K.4    Sun, C.5    Shen, W.H.6
  • 10
    • 0029080942 scopus 로고
    • Members of the NAP/SET family of proteins interact specifically with B-type cyclins
    • Kellogg, D., Kikuchi, A., Fujii-Nakata, T., Turck, C., and Murray, A. (1995) Members of the NAP/SET family of proteins interact specifically with B-type cyclins. J. Cell Biol. 130, 661-673
    • (1995) J. Cell Biol , vol.130 , pp. 661-673
    • Kellogg, D.1    Kikuchi, A.2    Fujii-Nakata, T.3    Turck, C.4    Murray, A.5
  • 12
    • 0242349716 scopus 로고    scopus 로고
    • Yeast Nap1-binding protein Nbp2p is required for mitotic growth at high temperatures and for cell wall integrity
    • Ohkuni, K., Okuda, A., and Kikuchi, A. (2003) Yeast Nap1-binding protein Nbp2p is required for mitotic growth at high temperatures and for cell wall integrity. Genetics 165, 517-529
    • (2003) Genetics , vol.165 , pp. 517-529
    • Ohkuni, K.1    Okuda, A.2    Kikuchi, A.3
  • 13
    • 0037295514 scopus 로고    scopus 로고
    • Knockout targeting of the Drosophila NAP1 gene and examination of DNA repair tracts in the recombination products
    • Lankenau, S., Barnickel, T., Marhold, J., Lyko, F., Mechler, B. M., and Lankenau, D. H. (2003) Knockout targeting of the Drosophila NAP1 gene and examination of DNA repair tracts in the recombination products. Genetics 163, 611-623
    • (2003) Genetics , vol.163 , pp. 611-623
    • Lankenau, S.1    Barnickel, T.2    Marhold, J.3    Lyko, F.4    Mechler, B.M.5    Lankenau, D.H.6
  • 15
    • 0346252598 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ats1p interacts with Nap1p, a cytoplasmic protein that controls bud morphogenesis
    • Shields, C. M., Taylor, R., Nazarenus, T., Cheatle, J., Hou, A., Tapprich, A., Haifley, A., and Atkin, A. L. (2003) Saccharomyces cerevisiae Ats1p interacts with Nap1p, a cytoplasmic protein that controls bud morphogenesis. Curr. Genet. 44, 184-194
    • (2003) Curr. Genet , vol.44 , pp. 184-194
    • Shields, C.M.1    Taylor, R.2    Nazarenus, T.3    Cheatle, J.4    Hou, A.5    Tapprich, A.6    Haifley, A.7    Atkin, A.L.8
  • 18
    • 0032504990 scopus 로고    scopus 로고
    • Control of mitotic events by the Cdc42 GTPase, the Clb2 cyclin and a member of the PAK kinase family
    • Tjandra, H., Compton, J., and Kellogg, D. (1998) Control of mitotic events by the Cdc42 GTPase, the Clb2 cyclin and a member of the PAK kinase family. Curr. Biol. 8, 991-1000
    • (1998) Curr. Biol , vol.8 , pp. 991-1000
    • Tjandra, H.1    Compton, J.2    Kellogg, D.3
  • 19
    • 0034123011 scopus 로고    scopus 로고
    • Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae
    • Longtine, M. S., Theesfeld, C. L., McMillan, J. N., Weaver, E., Pringle, J. R., and Lew, D. J. (2000) Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae. Mol. Cell Biol. 20, 4049-4061
    • (2000) Mol. Cell Biol , vol.20 , pp. 4049-4061
    • Longtine, M.S.1    Theesfeld, C.L.2    McMillan, J.N.3    Weaver, E.4    Pringle, J.R.5    Lew, D.J.6
  • 21
  • 22
    • 0038054272 scopus 로고    scopus 로고
    • Genomewide expression analysis of NAP1 in Saccharomyces cerevisiae
    • Ohkuni, K., Shirahige, K., and Kikuchi, A. (2003) Genomewide expression analysis of NAP1 in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 306, 5-9
    • (2003) Biochem. Biophys. Res. Commun , vol.306 , pp. 5-9
    • Ohkuni, K.1    Shirahige, K.2    Kikuchi, A.3
  • 23
    • 0037050026 scopus 로고    scopus 로고
    • Gavin, A. C., Bosche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A. M., Cruciat, C. M., et al. G. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147
    • Gavin, A. C., Bosche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A. M., Cruciat, C. M., et al. G. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147
  • 25
    • 0030742542 scopus 로고    scopus 로고
    • Control of mitotic events by Nap1 and the Gin4 kinase
    • Altman, R., and Kellogg, D. (1997) Control of mitotic events by Nap1 and the Gin4 kinase. J. Cell Biol. 138, 119-130
    • (1997) J. Cell Biol , vol.138 , pp. 119-130
    • Altman, R.1    Kellogg, D.2
  • 27
    • 0032476582 scopus 로고    scopus 로고
    • The septins are required for the mitosis-specific activation of the Gin4 kinase
    • Carroll, C. W., Altman, R., Schieltz, D., Yates, J. R., and Kellogg, D. (1998) The septins are required for the mitosis-specific activation of the Gin4 kinase. J. Cell Biol. 143, 709-717
    • (1998) J. Cell Biol , vol.143 , pp. 709-717
    • Carroll, C.W.1    Altman, R.2    Schieltz, D.3    Yates, J.R.4    Kellogg, D.5
  • 30
    • 0034603853 scopus 로고    scopus 로고
    • NBP1 (Nap1 binding protein 1), an essential gene for G2/M transition of Saccharomyces cerevisiae, encodes a protein of distinct sub-nuclear localization
    • Shimizu, Y., Akashi, T., Okuda, A., Kikuchi, A., and Fukui, K. (2000) NBP1 (Nap1 binding protein 1), an essential gene for G2/M transition of Saccharomyces cerevisiae, encodes a protein of distinct sub-nuclear localization. Gene. 246, 395-404
    • (2000) Gene , vol.246 , pp. 395-404
    • Shimizu, Y.1    Akashi, T.2    Okuda, A.3    Kikuchi, A.4    Fukui, K.5
  • 32
    • 0035195046 scopus 로고    scopus 로고
    • Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae
    • Iwase, M., and Toh-e, A. (2001) Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae. Genes Genet. Syst. 76, 335-343
    • (2001) Genes Genet. Syst , vol.76 , pp. 335-343
    • Iwase, M.1    Toh-e, A.2
  • 34
    • 2542447339 scopus 로고    scopus 로고
    • Ybr267w is a new cytoplasmic protein belonging to the mitotic signaling network of Saccharomyces cerevisiae
    • Iwase, M., and Toh-e, A. (2004) Ybr267w is a new cytoplasmic protein belonging to the mitotic signaling network of Saccharomyces cerevisiae. Cell Struct. Funct. 29, 1-15
    • (2004) Cell Struct. Funct , vol.29 , pp. 1-15
    • Iwase, M.1    Toh-e, A.2
  • 35
    • 0035181837 scopus 로고    scopus 로고
    • The Sda1 protein is required for passage through start
    • Zimmerman, Z. A., and Kellogg, D. R. (2001) The Sda1 protein is required for passage through start. Mol. Biol. Cell 12, 201-219
    • (2001) Mol. Biol. Cell , vol.12 , pp. 201-219
    • Zimmerman, Z.A.1    Kellogg, D.R.2
  • 36
    • 18644372079 scopus 로고    scopus 로고
    • 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm
    • Nissan, T. A., Bassler, J., Petfalski, E., Tollervey, D., and Hurt, E. (2002) 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm. EMBO J. 21, 5539-5547
    • (2002) EMBO J , vol.21 , pp. 5539-5547
    • Nissan, T.A.1    Bassler, J.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 37
    • 20744454423 scopus 로고    scopus 로고
    • Srs2 and Sgs1 DNA helicases associate with Mre11 in different subcomplexes following checkpoint activation and Cdk1-mediated Srs2 phosphorylation
    • Chiolo, I., Carotenuto, W., Maffioletti, G., Petrini, J. H., Foiani, M., and Liberi, G. (2005) Srs2 and Sgs1 DNA helicases associate with Mre11 in different subcomplexes following checkpoint activation and Cdk1-mediated Srs2 phosphorylation. Mol. Cell Biol. 25, 5738-5751
    • (2005) Mol. Cell Biol , vol.25 , pp. 5738-5751
    • Chiolo, I.1    Carotenuto, W.2    Maffioletti, G.3    Petrini, J.H.4    Foiani, M.5    Liberi, G.6
  • 39
    • 14044261281 scopus 로고    scopus 로고
    • Modulation of histone deposition by the karyopherin Kap114
    • Mosammaparast, N., Del Rosario, B. C., and Pemberton, L. F. (2005) Modulation of histone deposition by the karyopherin Kap114. Mol. Cell Biol. 25, 1764-1778
    • (2005) Mol. Cell Biol , vol.25 , pp. 1764-1778
    • Mosammaparast, N.1    Del Rosario, B.C.2    Pemberton, L.F.3
  • 41
    • 0033550213 scopus 로고    scopus 로고
    • Casein kinase 2 binds and phosphorylates the nucleosome assembly protein-1 (Nap1) in Drosophila melanogaster
    • Li, M., Strand, D., Krehan, A., Pyerin, W., Heid, H., Neumann, B., and Mechler, B. M. (1999) Casein kinase 2 binds and phosphorylates the nucleosome assembly protein-1 (Nap1) in Drosophila melanogaster. J. Mol. Biol. 293, 1067-1084
    • (1999) J. Mol. Biol , vol.293 , pp. 1067-1084
    • Li, M.1    Strand, D.2    Krehan, A.3    Pyerin, W.4    Heid, H.5    Neumann, B.6    Mechler, B.M.7
  • 42
    • 0034724563 scopus 로고    scopus 로고
    • Nap-2: Histone chaperone function and phosphorylation state through the cell cycle
    • Rodriguez, P., Pelletier, J., Price, G. B., and Zannis-Hadjopoulos, M. (2000) Nap-2: histone chaperone function and phosphorylation state through the cell cycle. J. Mol. Biol. 298, 225-238
    • (2000) J. Mol. Biol , vol.298 , pp. 225-238
    • Rodriguez, P.1    Pelletier, J.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 43
    • 0031968760 scopus 로고    scopus 로고
    • Chromatin fiber structure: Morphology, molecular determinants, structural transitions
    • Zlatanova, J., Leuba, S. H., and van Holde, K. (1998) Chromatin fiber structure: morphology, molecular determinants, structural transitions. Biophys. J. 74, 2554-2566
    • (1998) Biophys. J , vol.74 , pp. 2554-2566
    • Zlatanova, J.1    Leuba, S.H.2    van Holde, K.3
  • 44
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents, G., and Moudrianakis, E. N. (1995) The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl. Acad. Sci. U. S. A. 92, 11170-11174
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 46
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • 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 Å resolution. Nature 389, 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 47
    • 0033200347 scopus 로고    scopus 로고
    • The nucleosome core particle: Does it have structural and physiologic relevance?
    • Van Holde, K., and Zlatanova, J. (1999) The nucleosome core particle: does it have structural and physiologic relevance? Bioessays 21, 776-780
    • (1999) Bioessays , vol.21 , pp. 776-780
    • Van Holde, K.1    Zlatanova, J.2
  • 49
    • 0029821228 scopus 로고    scopus 로고
    • Interaction of the histone (H3-H4)2 tetramer of the nucleosome with positively supercoiled DNA minicircles: Potential flipping of the protein from a left- to a right-handed superhelical form
    • Hamiche, A., Carot, V., Alilat, M., De Lucia, F., O'Donohue, M. F., Revet, B., and Prunell, A. (1996) Interaction of the histone (H3-H4)2 tetramer of the nucleosome with positively supercoiled DNA minicircles: potential flipping of the protein from a left- to a right-handed superhelical form. Proc. Natl. Acad. Sci. U. S. A. 93, 7588-7593
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 7588-7593
    • Hamiche, A.1    Carot, V.2    Alilat, M.3    De Lucia, F.4    O'Donohue, M.F.5    Revet, B.6    Prunell, A.7
  • 50
    • 31944450097 scopus 로고    scopus 로고
    • The structure of nucleosome assembly protein 1
    • Park, Y. J., and Luger, K. (2006) The structure of nucleosome assembly protein 1. Proc. Natl. Acad. Sci. U. S. A. 103, 1248-1253
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 1248-1253
    • Park, Y.J.1    Luger, K.2
  • 51
    • 0036236469 scopus 로고    scopus 로고
    • Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro
    • Asahara, H., Tartare-Deckert, S., Nakagawa, T., Ikehara, T., Hirose, F., Hunter, T., Ito, T., and Montminy, M. (2002) Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro. Mol. Cell Biol. 22, 2974-2983
    • (2002) Mol. Cell Biol , vol.22 , pp. 2974-2983
    • Asahara, H.1    Tartare-Deckert, S.2    Nakagawa, T.3    Ikehara, T.4    Hirose, F.5    Hunter, T.6    Ito, T.7    Montminy, M.8
  • 53
    • 0029946736 scopus 로고    scopus 로고
    • Drosophila Nap-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays
    • Ito, T., Bulger, M., Kobayashi, R., and Kadonaga, J. (1996) Drosophila Nap-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays. Mol. Cell Biol. 16, 3112-3124
    • (1996) Mol. Cell Biol , vol.16 , pp. 3112-3124
    • Ito, T.1    Bulger, M.2    Kobayashi, R.3    Kadonaga, J.4
  • 54
    • 0031572246 scopus 로고    scopus 로고
    • Functional characterization of human nucleosome assembly protein-2 (Nap1L4) suggests a role as a histone chaperone
    • Rodriguez, P., Munroe, D., Prawitt, D., Chu, L. L., Bric, E., Kim, J., Reid, L. H., Davies, C., Nakagama, H., Loebbert, R., et al. (1997) Functional characterization of human nucleosome assembly protein-2 (Nap1L4) suggests a role as a histone chaperone. Genomics 44, 253-265
    • (1997) Genomics , vol.44 , pp. 253-265
    • Rodriguez, P.1    Munroe, D.2    Prawitt, D.3    Chu, L.L.4    Bric, E.5    Kim, J.6    Reid, L.H.7    Davies, C.8    Nakagama, H.9    Loebbert, R.10
  • 55
    • 0032511093 scopus 로고    scopus 로고
    • Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle
    • Marheineke, K., and Krude, T. (1998) Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle. J. Biol. Chem. 273, 15279-15286
    • (1998) J. Biol. Chem , vol.273 , pp. 15279-15286
    • Marheineke, K.1    Krude, T.2
  • 56
    • 4043116212 scopus 로고    scopus 로고
    • Self-association of the yeast nucleosome assembly protein 1
    • McBryant, S. J., and Peersen, O. B. (2004) Self-association of the yeast nucleosome assembly protein 1. Biochemistry 43, 10592-10599
    • (2004) Biochemistry , vol.43 , pp. 10592-10599
    • McBryant, S.J.1    Peersen, O.B.2
  • 57
    • 18144367268 scopus 로고    scopus 로고
    • Association states of nucleosome assembly protein 1 and its complexes with histones
    • Toth, K. F., Mazurkiewicz, J., and Rippe, K. (2005) Association states of nucleosome assembly protein 1 and its complexes with histones. J. Biol. Chem. 280, 15690-15699
    • (2005) J. Biol. Chem , vol.280 , pp. 15690-15699
    • Toth, K.F.1    Mazurkiewicz, J.2    Rippe, K.3
  • 58
    • 0242497812 scopus 로고    scopus 로고
    • Preferential binding of the histone (H3-H4)2 tetramer by Nap1 is mediated by the amino-terminal histone tails
    • McBryant, S. J., Park, Y.-J., Abernathy, S. M., Laybourn, P. J., Nyborg, J. K., and Luger, K. (2003) Preferential binding of the histone (H3-H4)2 tetramer by Nap1 is mediated by the amino-terminal histone tails. J. Biol. Chem. 278, 44574-44583
    • (2003) J. Biol. Chem , vol.278 , pp. 44574-44583
    • McBryant, S.J.1    Park, Y.-J.2    Abernathy, S.M.3    Laybourn, P.J.4    Nyborg, J.K.5    Luger, K.6
  • 59
    • 26644467244 scopus 로고    scopus 로고
    • Nap1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation
    • Kepert, J. F., Mazurkiewicz, J., Heuvelman, G. L., Toth, K. F., and Rippe, K. (2005) Nap1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation. J. Biol. Chem. 280, 34063-34072
    • (2005) J. Biol. Chem , vol.280 , pp. 34063-34072
    • Kepert, J.F.1    Mazurkiewicz, J.2    Heuvelman, G.L.3    Toth, K.F.4    Rippe, K.5
  • 60
    • 0023105676 scopus 로고
    • Binding mode of nucleosome-assembly protein (AP-I) and histones
    • Ishimi, Y., Kojima, M., Yamada, M., and Hanaoka, F. (1987) Binding mode of nucleosome-assembly protein (AP-I) and histones. Eur. J. Biochem. 162, 19-24
    • (1987) Eur. J. Biochem , vol.162 , pp. 19-24
    • Ishimi, Y.1    Kojima, M.2    Yamada, M.3    Hanaoka, F.4
  • 61
    • 0035920211 scopus 로고    scopus 로고
    • Multistep chromatin assembly on supercoiled plasmid DNA by nucleosome assembly protein-1 and ATP-utilizing chromatin assembly and remodeling factor
    • Nakagawa, T., Bulger, M., Muramatsu, M., and Ito, T. (2001) Multistep chromatin assembly on supercoiled plasmid DNA by nucleosome assembly protein-1 and ATP-utilizing chromatin assembly and remodeling factor. J. Biol. Chem. 276, 27384-27391
    • (2001) J. Biol. Chem , vol.276 , pp. 27384-27391
    • Nakagawa, T.1    Bulger, M.2    Muramatsu, M.3    Ito, T.4
  • 62
    • 0021470855 scopus 로고
    • Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells
    • Ishimi, Y., Hirosumi, J., Sato, W., Sugasawa, K., Yokota, S., Hanaoka, F., and Yamada, M. (1984) Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells. Eur. J. Biochem. 142, 431-439
    • (1984) Eur. J. Biochem , vol.142 , pp. 431-439
    • Ishimi, Y.1    Hirosumi, J.2    Sato, W.3    Sugasawa, K.4    Yokota, S.5    Hanaoka, F.6    Yamada, M.7
  • 63
    • 22144435207 scopus 로고    scopus 로고
    • Zygotic nucleosome assembly protein-like 1 has a specific, non-cell autonomous role in hematopoiesis
    • Abu-Daya, A., Steer, W. M., Trollope, A. F., Friedeberg, C. E., Patient, R. K., Thorne, A. W., and Guille, M. J. (2005) Zygotic nucleosome assembly protein-like 1 has a specific, non-cell autonomous role in hematopoiesis. Blood 106, 514-520
    • (2005) Blood , vol.106 , pp. 514-520
    • Abu-Daya, A.1    Steer, W.M.2    Trollope, A.F.3    Friedeberg, C.E.4    Patient, R.K.5    Thorne, A.W.6    Guille, M.J.7
  • 64
    • 0036234551 scopus 로고    scopus 로고
    • Selective requirements for histone H3 and H4 N termini in p300-dependent transcriptional activation from chromatin
    • An, W., Palhan, V. B., Karymov, M. A., Leuba, S. H., and Roeder, R. G. (2002) Selective requirements for histone H3 and H4 N termini in p300-dependent transcriptional activation from chromatin. Mol. Cell 9, 811-821
    • (2002) Mol. Cell , vol.9 , pp. 811-821
    • An, W.1    Palhan, V.B.2    Karymov, M.A.3    Leuba, S.H.4    Roeder, R.G.5
  • 65
    • 0036132658 scopus 로고    scopus 로고
    • p300-mediated tax transactivation from recombinant chromatin: Histone tail deletion mimics coactivator function
    • Georges, S. A., Kraus, W. L., Luger, K., Nyborg, J. K., and Laybourn, P. J. (2002) p300-mediated tax transactivation from recombinant chromatin: histone tail deletion mimics coactivator function. Mol. Cell Biol. 22, 127-137
    • (2002) Mol. Cell Biol , vol.22 , pp. 127-137
    • Georges, S.A.1    Kraus, W.L.2    Luger, K.3    Nyborg, J.K.4    Laybourn, P.J.5
  • 66
    • 0032513211 scopus 로고    scopus 로고
    • Assembly, remodeling, and histone binding capabilities of yeast nucleosome assembly protein 1
    • McQuibban, G. A., Commisso-Cappelli, C. N., and Lewis, P. N. (1998) Assembly, remodeling, and histone binding capabilities of yeast nucleosome assembly protein 1. J. Biol. Chem. 273, 6582-6590
    • (1998) J. Biol. Chem , vol.273 , pp. 6582-6590
    • McQuibban, G.A.1    Commisso-Cappelli, C.N.2    Lewis, P.N.3
  • 67
    • 0034462693 scopus 로고    scopus 로고
    • Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators
    • Shikama, N., Chan, H. M., Krstic-Demonacos, M., Smith, L., Lee, C.-W., Cairns, W., and La Thangue, N. B. (2000) Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators. Mol. Cell Biol. 20, 8933-8943
    • (2000) Mol. Cell Biol , vol.20 , pp. 8933-8943
    • Shikama, N.1    Chan, H.M.2    Krstic-Demonacos, M.3    Smith, L.4    Lee, C.-W.5    Cairns, W.6    La Thangue, N.B.7
  • 68
    • 0031026487 scopus 로고    scopus 로고
    • Histones in transit: Cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
    • Chang, L., Loranger, S. S., Mizzen, C., Ernst, S. G., Allis, C. D., and Annunziato, A. T. (1997) Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells. Biochemistry 36, 469-480
    • (1997) Biochemistry , vol.36 , pp. 469-480
    • Chang, L.1    Loranger, S.S.2    Mizzen, C.3    Ernst, S.G.4    Allis, C.D.5    Annunziato, A.T.6
  • 70
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • Mosammaparast, N., Ewart, C. S., and Pemberton, L. F. (2002) A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J. 21, 6527-6538
    • (2002) EMBO J , vol.21 , pp. 6527-6538
    • Mosammaparast, N.1    Ewart, C.S.2    Pemberton, L.F.3
  • 71
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast, N., and Pemberton, L. F. (2004) Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14, 547-556
    • (2004) Trends Cell Biol , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 74
    • 27144453690 scopus 로고    scopus 로고
    • Asf1 binds to a heterodimer of histones H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
    • English, C. M., Maluf, N. K., Tripet, B., Churchill, M. E., and Tyler, J. K. (2005) Asf1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry 44, 13673-13682
    • (2005) Biochemistry , vol.44 , pp. 13673-13682
    • English, C.M.1    Maluf, N.K.2    Tripet, B.3    Churchill, M.E.4    Tyler, J.K.5
  • 75
    • 33745201632 scopus 로고    scopus 로고
    • On the mechanism of nucleosome assembly by histone chaperone Nap1
    • Mazurkiewicz, J., Kepert, J. F., and Rippe, K. (2006) On the mechanism of nucleosome assembly by histone chaperone Nap1. J. Biol. Chem. 281, 16462-16472
    • (2006) J. Biol. Chem , vol.281 , pp. 16462-16472
    • Mazurkiewicz, J.1    Kepert, J.F.2    Rippe, K.3
  • 76
    • 27744454235 scopus 로고    scopus 로고
    • Compaction kinetics on single DNAs: Purified nucleosome reconstitution systems versus crude extract
    • Wagner, G., Bancaud, A., Quivy, J. P., Clapier, C., Almouzni, G., and Viovy, J. L. (2005) Compaction kinetics on single DNAs: purified nucleosome reconstitution systems versus crude extract. Biophys. J. 89, 3647-3659
    • (2005) Biophys. J , vol.89 , pp. 3647-3659
    • Wagner, G.1    Bancaud, A.2    Quivy, J.P.3    Clapier, C.4    Almouzni, G.5    Viovy, J.L.6
  • 77
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito, T., Bulger, M., Pazin, M. J., Kobayashi, R., and Kadonaga, J. T. (1997) ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90, 145-155
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 78
    • 0031172308 scopus 로고    scopus 로고
    • Yeast chromatin reconstitution system using purified yeast core histones and yeast nucleosome assembly protein-1
    • Pilon, J., Terrell, A., and Laybourn, P. J. (1997) Yeast chromatin reconstitution system using purified yeast core histones and yeast nucleosome assembly protein-1. Prot. Expr. Purif. 10, 132-140
    • (1997) Prot. Expr. Purif , vol.10 , pp. 132-140
    • Pilon, J.1    Terrell, A.2    Laybourn, P.J.3
  • 79
    • 0037163080 scopus 로고    scopus 로고
    • Reconstitution of nucleosome positioning, remodeling, histone acetylation, and transcriptional activation on the PHO5 promoter
    • Terrell, A. R., Wongwisansri, S., Pilon, J. L., and Laybourn, P. J. (2002) Reconstitution of nucleosome positioning, remodeling, histone acetylation, and transcriptional activation on the PHO5 promoter. J. Biol. Chem. 277, 31038-31047
    • (2002) J. Biol. Chem , vol.277 , pp. 31038-31047
    • Terrell, A.R.1    Wongwisansri, S.2    Pilon, J.L.3    Laybourn, P.J.4
  • 80
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Park, Y. J., Chodaparambil, J. V., Bao, Y., McBryant, S. J., and Luger, K. (2005) Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding. J. Biol. Chem. 280, 1817-1825
    • (2005) J. Biol. Chem , vol.280 , pp. 1817-1825
    • Park, Y.J.1    Chodaparambil, J.V.2    Bao, Y.3    McBryant, S.J.4    Luger, K.5
  • 81
    • 27944478598 scopus 로고    scopus 로고
    • Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein 1
    • Okuwaki, M., Kato, K., Shimahara, H., Tate, S., and Nagata, K. (2005) Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein 1. Mol. Cell Biol. 25, 10639-10651
    • (2005) Mol. Cell Biol , vol.25 , pp. 10639-10651
    • Okuwaki, M.1    Kato, K.2    Shimahara, H.3    Tate, S.4    Nagata, K.5
  • 82
    • 2642515598 scopus 로고    scopus 로고
    • A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2A.Z stabilizes the histone octamer within the nucleosome
    • Park, Y. J., Dyer, P. N., Tremethick, D. J., and Luger, K. (2004) A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2A.Z stabilizes the histone octamer within the nucleosome. J. Biol. Chem. 279, 24274-24282
    • (2004) J. Biol. Chem , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 83
    • 33746015346 scopus 로고    scopus 로고
    • H2A.Z stabilizes chromatin in a way that is dependent on core histone acetylation
    • Thambirajah, A. A., Dryhurst, D., Ishibashi, T., Li, A., Maffey, A. H., and Ausio, J. (2006) H2A.Z stabilizes chromatin in a way that is dependent on core histone acetylation. J. Biol. Chem. 281, 20036-20044
    • (2006) J. Biol. Chem , vol.281 , pp. 20036-20044
    • Thambirajah, A.A.1    Dryhurst, D.2    Ishibashi, T.3    Li, A.4    Maffey, A.H.5    Ausio, J.6
  • 84
    • 33947524604 scopus 로고    scopus 로고
    • Histone variants - the structure behind the function
    • Ausio, J. (2006) Histone variants - the structure behind the function. Brief. Funct. Genomic Proteomic 5, 228-243
    • (2006) Brief. Funct. Genomic Proteomic , vol.5 , pp. 228-243
    • Ausio, J.1
  • 86
    • 13244255650 scopus 로고    scopus 로고
    • Histone variants: Deviants?
    • Kamakaka, R. T., and Biggins, S. (2005) Histone variants: deviants? Genes Dev. 19, 295-310
    • (2005) Genes Dev , vol.19 , pp. 295-310
    • Kamakaka, R.T.1    Biggins, S.2
  • 87
  • 92
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2A.Z variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G., Shen, X., Landry, J., Wu, W. H., Sen, S., and Wu, C. (2004) ATP-driven exchange of histone H2A.Z variant catalyzed by SWR1 chromatin remodeling complex. Science 303, 343-348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 93
    • 33744964248 scopus 로고    scopus 로고
    • Scanning chromatin: A new paradigm?
    • Van Holde, K., and Zlatanova, J. (2006) Scanning chromatin: a new paradigm? J. Biol. Chem. 281, 12197-12200
    • (2006) J. Biol. Chem , vol.281 , pp. 12197-12200
    • Van Holde, K.1    Zlatanova, J.2
  • 94
    • 1342325336 scopus 로고    scopus 로고
    • Direct interaction between nucleosome assembly protein 1 and the papillomavirus E2 proteins involved in activation of transcription
    • Rehtanz, M., Schmidt, H. M., Warthorst, U., and Steger, G. (2004) Direct interaction between nucleosome assembly protein 1 and the papillomavirus E2 proteins involved in activation of transcription. Mol. Cell Biol. 24, 2153-2168
    • (2004) Mol. Cell Biol , vol.24 , pp. 2153-2168
    • Rehtanz, M.1    Schmidt, H.M.2    Warthorst, U.3    Steger, G.4
  • 96
    • 14244267814 scopus 로고    scopus 로고
    • Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator
    • Kong, S. E., Kobor, M. S., Krogan, N. J., Somesh, B. P., Sogaard, T. M., Greenblatt, J. F., and Svejstrup, J. Q. (2005) Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator. J. Biol. Chem. 280, 4299-4306
    • (2005) J. Biol. Chem , vol.280 , pp. 4299-4306
    • Kong, S.E.1    Kobor, M.S.2    Krogan, N.J.3    Somesh, B.P.4    Sogaard, T.M.5    Greenblatt, J.F.6    Svejstrup, J.Q.7
  • 98
    • 36148934535 scopus 로고    scopus 로고
    • What happens to nucleosomes during transcription?
    • Zlatanova, J, and Leuba, S. H, eds pp, Elsevier, Amsterdam
    • Jackson, V. (2004) What happens to nucleosomes during transcription? In Chromatin Structure and Dynamics: State-of-the-Art (Zlatanova, J., and Leuba, S. H., eds) pp. 467-491, Elsevier, Amsterdam
    • (2004) Chromatin Structure and Dynamics: State-of-the-Art , pp. 467-491
    • Jackson, V.1
  • 99
    • 33746641324 scopus 로고    scopus 로고
    • Nucleosome displacement in transcription
    • Workman, J. L. (2006) Nucleosome displacement in transcription. Genes Dev. 20, 2009-2017
    • (2006) Genes Dev , vol.20 , pp. 2009-2017
    • Workman, J.L.1
  • 100
    • 0028799432 scopus 로고
    • Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer
    • Walter, P., Owen-Hughes, T., Cote, J., and Workman, J. (1995) Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer. Mol. Cell Biol. 15, 6178-6187
    • (1995) Mol. Cell Biol , vol.15 , pp. 6178-6187
    • Walter, P.1    Owen-Hughes, T.2    Cote, J.3    Workman, J.4
  • 101
    • 0033898468 scopus 로고    scopus 로고
    • p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • Ito, T., Ikehara, T., Nakagawa, T., Kraus, W. L., and Muramatsu, M. (2000) p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone. Genes Dev. 14, 1899-1907
    • (2000) Genes Dev , vol.14 , pp. 1899-1907
    • Ito, T.1    Ikehara, T.2    Nakagawa, T.3    Kraus, W.L.4    Muramatsu, M.5
  • 102
    • 28944442449 scopus 로고    scopus 로고
    • Histone release during transcription: Acetylation stabilizes the interaction of the H2AH2B dimer with the H3-H4 tetramer in nucleosomes that are on highly positively coiled DNA
    • Wunsch, A., and Jackson, V. (2005) Histone release during transcription: acetylation stabilizes the interaction of the H2AH2B dimer with the H3-H4 tetramer in nucleosomes that are on highly positively coiled DNA. Biochemistry 44, 16351-16364
    • (2005) Biochemistry , vol.44 , pp. 16351-16364
    • Wunsch, A.1    Jackson, V.2
  • 103
    • 22044436367 scopus 로고    scopus 로고
    • Forced unraveling of nucleosomes assembled on heterogeneous DNA using core histones, Nap-1, and ACF
    • Gemmen, G. J., Sim, R., Haushalter, K. A., Ke, P. C., Kadonaga, J. T., and Smith, D. E. (2005) Forced unraveling of nucleosomes assembled on heterogeneous DNA using core histones, Nap-1, and ACF. J. Mol. Biol. 351, 89-99
    • (2005) J. Mol. Biol , vol.351 , pp. 89-99
    • Gemmen, G.J.1    Sim, R.2    Haushalter, K.A.3    Ke, P.C.4    Kadonaga, J.T.5    Smith, D.E.6
  • 105
    • 0033566129 scopus 로고    scopus 로고
    • The chromatin-specific transcription elongation factor FACT comprises human Spt16 and Ssrp1 proteins
    • Orphanides, G., Wu, W. H., Lane, W. S., Hampsey, M., and Reinberg, D. (1999) The chromatin-specific transcription elongation factor FACT comprises human Spt16 and Ssrp1 proteins. Nature 400, 284-288
    • (1999) Nature , vol.400 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 107
    • 1942471690 scopus 로고    scopus 로고
    • Facts about FACT and transcript elongation through chromatin
    • Belotserkovskaya, R., and Reinberg, D. (2004) Facts about FACT and transcript elongation through chromatin. Curr. Opin. Genet. Dev. 14, 139-146
    • (2004) Curr. Opin. Genet. Dev , vol.14 , pp. 139-146
    • Belotserkovskaya, R.1    Reinberg, D.2
  • 108
    • 33746856074 scopus 로고    scopus 로고
    • de FACTo nucleosome dynamics
    • Reinberg, D., and Sims, R. J., 3rd (2006) de FACTo nucleosome dynamics. J. Biol. Chem. 281, 23297-23301
    • (2006) J. Biol. Chem , vol.281 , pp. 23297-23301
    • Reinberg, D.1    Sims 3rd, R.J.2
  • 110
    • 0942290537 scopus 로고    scopus 로고
    • Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo
    • Fyodorov, D. V., Blower, M. D., Karpen, G. H., and Kadonaga, J. T. (2004) Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo. Genes Dev. 18, 170-183
    • (2004) Genes Dev , vol.18 , pp. 170-183
    • Fyodorov, D.V.1    Blower, M.D.2    Karpen, G.H.3    Kadonaga, J.T.4
  • 111
    • 16844366808 scopus 로고    scopus 로고
    • Histone release during transcription: Displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress
    • Levchenko, V., Jackson, B., and Jackson, V. (2005) Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress. Biochemistry 44, 5357-5372
    • (2005) Biochemistry , vol.44 , pp. 5357-5372
    • Levchenko, V.1    Jackson, B.2    Jackson, V.3
  • 112
    • 1542267778 scopus 로고    scopus 로고
    • Histone release during transcription: Nap1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome
    • Levchenko, V., and Jackson, V. (2004) Histone release during transcription: Nap1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome. Biochemistry 43, 2359-2372
    • (2004) Biochemistry , vol.43 , pp. 2359-2372
    • Levchenko, V.1    Jackson, V.2
  • 113
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu, L. F., and Wang, J. C. (1987) Supercoiling of the DNA template during transcription. Proc. Natl. Acad. Sci. U. S. A. 84, 7024-7027
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 114
    • 7544242666 scopus 로고    scopus 로고
    • The dynamic response of upstream DNA to transcription-generated torsional stress
    • Kouzine, F., Liu, J., Sanford, S., Chung, H. J., and Levens, D. (2004) The dynamic response of upstream DNA to transcription-generated torsional stress. Nat. Struct. Mol. Biol. 11, 1092-1100
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1092-1100
    • Kouzine, F.1    Liu, J.2    Sanford, S.3    Chung, H.J.4    Levens, D.5
  • 116
    • 0035959633 scopus 로고    scopus 로고
    • DNA topoisomerase IIα is required for RNA polymerase II transcription on chromatin templates
    • Mondal, N., and Parvin, J. D. (2001) DNA topoisomerase IIα is required for RNA polymerase II transcription on chromatin templates. Nature 413, 435-438
    • (2001) Nature , vol.413 , pp. 435-438
    • Mondal, N.1    Parvin, J.D.2
  • 117
    • 0035200324 scopus 로고    scopus 로고
    • Transcriptional consequences of topoisomerase inhibition
    • Collins, I., Weber, A., and Levens, D. (2001) Transcriptional consequences of topoisomerase inhibition. Mol. Cell Biol. 21, 8437-8451
    • (2001) Mol. Cell Biol , vol.21 , pp. 8437-8451
    • Collins, I.1    Weber, A.2    Levens, D.3


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