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Volumn 7, Issue 1, 1997, Pages 94-102

Histone-like transcription factors in eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; TRANSCRIPTION FACTOR;

EID: 0031049523     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80012-7     Document Type: Article
Times cited : (39)

References (47)
  • 1
    • 0016211838 scopus 로고
    • Chromatin structure: Oligomers of the histones
    • Kornberg RD, Thomas JO. Chromatin structure: oligomers of the histones. Science. 184:1974;865-868.
    • (1974) Science , vol.184 , pp. 865-868
    • Kornberg, R.D.1    Thomas, J.O.2
  • 2
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • Kornberg RD. Chromatin structure: a repeating unit of histones and DNA. Science. 184:1974;868-871.
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 3
    • 0019200870 scopus 로고
    • A low resolution structure for the histone core of the nucleosome
    • Klug A, Rhodes D, Smith J, Finch JT, Thomas JO. A low resolution structure for the histone core of the nucleosome. Nature. 287:1980;509-516.
    • (1980) Nature , vol.287 , pp. 509-516
    • Klug, A.1    Rhodes, D.2    Smith, J.3    Finch, J.T.4    Thomas, J.O.5
  • 5
    • 0021760689 scopus 로고
    • Structure of the nucleosome core particle at 7Å resolution
    • Richmond TJ, Finch JT, Rushton B, Rhodes D, Klug A. Structure of the nucleosome core particle at 7Å resolution. Nature. 311:1984;532-537.
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.3    Rhodes, D.4    Klug, A.5
  • 6
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents G, Burlingame RW, Wang B-C, Love WE, Moudrianakis EN. The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc Natl Acad Sci USA. 88:1991;10148-10152.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.-C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 7
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch JT, Klug A. Solenoidal model for superstructure in chromatin. Proc Natl Acad Sci USA. 73:1976;1897-1901.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1897-1901
    • Finch, J.T.1    Klug, A.2
  • 8
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt dependent superstructures of chromatin
    • Thoma F, Losa R, Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt dependent superstructures of chromatin. J Cell Biol. 83:1979;403-427.
    • (1979) J Cell Biol , vol.83 , pp. 403-427
    • Thoma, F.1    Losa, R.2    Klug, A.3
  • 9
    • 0028314834 scopus 로고
    • Histone H1 is located in the interior of the chromatin 30 nm filament
    • Graziano V, Gerchman SE, Schneider DK, Ramakrishnan V. Histone H1 is located in the interior of the chromatin 30 nm filament. Nature. 368:1994;351-354.
    • (1994) Nature , vol.368 , pp. 351-354
    • Graziano, V.1    Gerchman, S.E.2    Schneider, D.K.3    Ramakrishnan, V.4
  • 10
    • 0027402969 scopus 로고
    • Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan V, Finch J, Graziano V, Sweet R. Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature. 362:1993;219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.2    Graziano, V.3    Sweet, R.4
  • 11
    • 0016259652 scopus 로고
    • A histone cross-complexing pattern
    • D'Anna JA, Isenberg I. A histone cross-complexing pattern. Biochemistry. 13:1974;4992-4997.
    • (1974) Biochemistry , vol.13 , pp. 4992-4997
    • D'Anna, J.A.1    Isenberg, I.2
  • 12
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • of outstanding interest. This paper reports the first detailed characterization of the histone fold at high resolution.
    • Arents G, Moudrianakis E. The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. of outstanding interest Proc Natl Acad Sci USA. 92:1995;11170-11174 This paper reports the first detailed characterization of the histone fold at high resolution.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.2
  • 13
    • 0029869460 scopus 로고    scopus 로고
    • Structural similarity between TAFs and the heterotetrameric core of the histone octamer
    • of outstanding interest. The first high-resolution X-ray crystal structures of TBP-associated factors and proof of their structural similarity to core histone proteins H3 and H4 are presented.
    • Xie X, Kokubo T, Cohen SL, Hoffmann A, Chait BT, Roeder RG, Nakatani Y, Burley SK. Structural similarity between TAFs and the heterotetrameric core of the histone octamer. of outstanding interest Nature. 380:1996;316-322 The first high-resolution X-ray crystal structures of TBP-associated factors and proof of their structural similarity to core histone proteins H3 and H4 are presented.
    • (1996) Nature , vol.380 , pp. 316-322
    • Xie, X.1    Kokubo, T.2    Cohen, S.L.3    Hoffmann, A.4    Chait, B.T.5    Roeder, R.G.6    Nakatani, Y.7    Burley, S.K.8
  • 14
    • 0029924193 scopus 로고    scopus 로고
    • NMR structure of HMfB from the hyperthermophile, methanothermus fervidus, confirms that this archael protein is a histone
    • of special interest. This paper presents the first NMR study of an archael histone protein, and proof of its structural similarity to core histone proteins.
    • Starich MR, Sandman K, Reeve JN, Summers MF. NMR structure of HMfB from the hyperthermophile, methanothermus fervidus, confirms that this archael protein is a histone. of special interest J Mol Biol. 255:1996;187-203 This paper presents the first NMR study of an archael histone protein, and proof of its structural similarity to core histone proteins.
    • (1996) J Mol Biol , vol.255 , pp. 187-203
    • Starich, M.R.1    Sandman, K.2    Reeve, J.N.3    Summers, M.F.4
  • 15
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA
    • Arents G, Moudrianakis E. Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA. Proc Natl Acad Sci USA. 90:1993;10489-10493.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.2
  • 16
    • 0030026726 scopus 로고    scopus 로고
    • Thermodynamic studies of the core histones: PH and ionic strength effects on the stability of the (H3-H4)/(H3-H4)2 system
    • 2 heterotetramer are reported.
    • 2 heterotetramer are reported.
    • (1996) Biochemistry , vol.35 , pp. 2037-2046
    • Karantza, V.1    Friere, E.2    Moudrianakis, E.3
  • 17
    • 0029011919 scopus 로고
    • The p150 and p60 subunits of chromatin assembly factor 1: A molecular link between newly synthesized histones and DNA replication
    • Kaufman PD, Kobayashi R, Kessler N, Stillman B. The p150 and p60 subunits of chromatin assembly factor 1: a molecular link between newly synthesized histones and DNA replication. Cell. 81:1995;1105-1114.
    • (1995) Cell , vol.81 , pp. 1105-1114
    • Kaufman, P.D.1    Kobayashi, R.2    Kessler, N.3    Stillman, B.4
  • 18
    • 0022230224 scopus 로고
    • DNA bending and its relation to nucleosome positioning
    • Drew H, Travers A. DNA bending and its relation to nucleosome positioning. J Mol Biol. 186:1985;773-790.
    • (1985) J Mol Biol , vol.186 , pp. 773-790
    • Drew, H.1    Travers, A.2
  • 19
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosomal core DNA
    • Satchwell S, Drew H, Travers A. Sequence periodicities in chicken nucleosomal core DNA. J Mol Biol. 191:1986;659-679.
    • (1986) J Mol Biol , vol.191 , pp. 659-679
    • Satchwell, S.1    Drew, H.2    Travers, A.3
  • 20
    • 0030013203 scopus 로고    scopus 로고
    • Biochemistry and structural biology of transcription factor IID
    • of special interest. A comprehensive review on the structure and function of transcription factor IID.
    • Burley SK, Roeder RG. Biochemistry and structural biology of transcription factor IID. of special interest Annu Rev Biochem. 65:1996;769-799 A comprehensive review on the structure and function of transcription factor IID.
    • (1996) Annu Rev Biochem , vol.65 , pp. 769-799
    • Burley, S.K.1    Roeder, R.G.2
  • 21
    • 0029917840 scopus 로고    scopus 로고
    • Repression and activation by multiprotein complexes that alter chromatin structure
    • of special interest. A useful review on the interplay between transcription and DNA packaging.
    • Kingston RE, Bunker CA, Imbalzano AN. Repression and activation by multiprotein complexes that alter chromatin structure. of special interest Genes Dev. 10:1996;905-920 A useful review on the interplay between transcription and DNA packaging.
    • (1996) Genes Dev , vol.10 , pp. 905-920
    • Kingston, R.E.1    Bunker, C.A.2    Imbalzano, A.N.3
  • 22
    • 0023661185 scopus 로고
    • Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II
    • Workman JL, Roeder RG. Binding of transcription factor TFIID to the major late promoter during in vitro nucleosome assembly potentiates subsequent initiation by RNA polymerase II. Cell. 51:1987;613-622.
    • (1987) Cell , vol.51 , pp. 613-622
    • Workman, J.L.1    Roeder, R.G.2
  • 23
    • 0025647724 scopus 로고
    • Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay
    • Meisterernst M, Horikoshi M, Roeder RG. Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay. Proc Natl Acad Sci USA. 87:1990;9153-9157.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9153-9157
    • Meisterernst, M.1    Horikoshi, M.2    Roeder, R.G.3
  • 25
    • 0029115323 scopus 로고
    • Evolutionary conservation of human TBP-associated factors TAF31 and TAF80 and interactions of TAF80 with other TAFs and with general transcription factors
    • Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder R. Evolutionary conservation of human TBP-associated factors TAF31 and TAF80 and interactions of TAF80 with other TAFs and with general transcription factors. Proc Natl Acad Sci USA. 92:1995;8195-8199.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8195-8199
    • Hisatake, K.1    Ohta, T.2    Takada, R.3    Guermah, M.4    Horikoshi, M.5    Nakatani, Y.6    Roeder, R.7
  • 26
    • 0029887687 scopus 로고    scopus 로고
    • A histone octamer-like structure within TFIID
    • of outstanding interest. This paper presents results of biochemical studies that complement the X-ray crystallographic work described in reference [13] and provides further evidence of a histone octamer-like structure within transcription factor IID.
    • Hoffmann A, Chiang C-M, Oelgeschlager T, Xie X, Burley SK, Nakatani Y, Roeder RG. A histone octamer-like structure within TFIID. of outstanding interest Nature. 380:1996;356-359 This paper presents results of biochemical studies that complement the X-ray crystallographic work described in reference [13] and provides further evidence of a histone octamer-like structure within transcription factor IID.
    • (1996) Nature , vol.380 , pp. 356-359
    • Hoffmann, A.1    Chiang, C.-M.2    Oelgeschlager, T.3    Xie, X.4    Burley, S.K.5    Nakatani, Y.6    Roeder, R.G.7
  • 27
    • 0028987948 scopus 로고
    • Cloning and characterization of hTAFII18, hTAF1120 and hTAFII28: Three subunits of the human transcription factor TFIID
    • Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I. Cloning and characterization of hTAFII18, hTAF1120 and hTAFII28: Three subunits of the human transcription factor TFIID. EMBO J. 14:1995;1520-1531.
    • (1995) EMBO J , vol.14 , pp. 1520-1531
    • Mengus, G.1    May, M.2    Jacq, X.3    Staub, A.4    Tora, L.5    Chambon, P.6    Davidson, I.7
  • 28
    • 0029127222 scopus 로고
    • A variety of DNA-binding and multimeric proteins contain the histone fold motif
    • Baxevanis A, Arents G, Moudrianakis E, Landsman D. A variety of DNA-binding and multimeric proteins contain the histone fold motif. Nucleic Acids Res. 23:1995;2685-2691.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2685-2691
    • Baxevanis, A.1    Arents, G.2    Moudrianakis, E.3    Landsman, D.4
  • 29
    • 0028861437 scopus 로고
    • Elusive affinities
    • Janin J. Elusive affinities. Proteins. 21:1995;30-39.
    • (1995) Proteins , vol.21 , pp. 30-39
    • Janin, J.1
  • 30
    • 0022374891 scopus 로고
    • Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region
    • Sawadogo M, Roeder RG. Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region. Cell. 43:1985;165-175.
    • (1985) Cell , vol.43 , pp. 165-175
    • Sawadogo, M.1    Roeder, R.G.2
  • 31
    • 0029808220 scopus 로고    scopus 로고
    • Topology and reorganization of a human TFIID-promoter complex
    • of outstanding interest. The authors report the results of DNA - protein photocrosslinking studies of transcription factor IID and provide the first evidence for negative super-coiling of closed circular DNA by transcription factor IID under standard nucleosome assembly conditions.
    • Oelgeschlager T, Chiang C-M, Roeder RG. Topology and reorganization of a human TFIID-promoter complex. of outstanding interest Nature. 382:1996;735-738 The authors report the results of DNA - protein photocrosslinking studies of transcription factor IID and provide the first evidence for negative super-coiling of closed circular DNA by transcription factor IID under standard nucleosome assembly conditions.
    • (1996) Nature , vol.382 , pp. 735-738
    • Oelgeschlager, T.1    Chiang, C.-M.2    Roeder, R.G.3
  • 32
    • 0027974851 scopus 로고
    • 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG
    • Kim JL, Burley SK. 1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG. Nat Struct Biol. 1:1994;638-653.
    • (1994) Nat Struct Biol , vol.1 , pp. 638-653
    • Kim, J.L.1    Burley, S.K.2
  • 33
    • 0025993737 scopus 로고
    • Family of proteins that interact with TFIID and regulate promoter activity
    • Meisterernst M, Roeder RG. Family of proteins that interact with TFIID and regulate promoter activity. Cell. 67:1991;557-567.
    • (1991) Cell , vol.67 , pp. 557-567
    • Meisterernst, M.1    Roeder, R.G.2
  • 34
    • 0026742095 scopus 로고
    • Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription
    • Inostroza JA, Mermelstein FH, Ha I, Lane WS, Reinberg D. Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. Cell. 70:1992;477-489.
    • (1992) Cell , vol.70 , pp. 477-489
    • Inostroza, J.A.1    Mermelstein, F.H.2    Ha, I.3    Lane, W.S.4    Reinberg, D.5
  • 35
    • 0029977801 scopus 로고    scopus 로고
    • A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains
    • of special interest. The authors report their discovery that NC2, a negative regulator of RNA polymerase II transcription initiation, is an H2A/H2B-like heterodimer. Similar findings are reported in [36].
    • Goppelt A, Stelzer G, Lottspeich F, Meisterernst M. A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains. of special interest EMBO J. 15:1996;3105-3116 The authors report their discovery that NC2, a negative regulator of RNA polymerase II transcription initiation, is an H2A/H2B-like heterodimer. Similar findings are reported in [36].
    • (1996) EMBO J , vol.15 , pp. 3105-3116
    • Goppelt, A.1    Stelzer, G.2    Lottspeich, F.3    Meisterernst, M.4
  • 37
    • 0030943821 scopus 로고    scopus 로고
    • Eukaryotic transcription factor-DNA complexes
    • of special interest A useful, comprehensive review of all high-resolution X-ray crystallographic and NMR structures of eukaryotic transcription factor/DNA complexes published before August 1996
    • Patikoglou G, Burley SK. Eukaryotic transcription factor-DNA complexes. of special interest Annu Rev Biophys Biomolec Struct. 26:1997; A useful, comprehensive review of all high-resolution X-ray crystallographic and NMR structures of eukaryotic transcription factor/DNA complexes published before August 1996.
    • (1997) Annu Rev Biophys Biomolec Struct , vol.26
    • Patikoglou, G.1    Burley, S.K.2
  • 38
    • 0025914242 scopus 로고
    • Crystal structure of a CAP - DNA complex: The DNA is bent by 90°
    • Schultz SC, Shields GC, Steitz TA. Crystal structure of a CAP - DNA complex: the DNA is bent by 90° Science. 253:1991;1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 39
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark KL, Halay ED, Lai E, Burley SK. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature. 364:1993;412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 40
    • 0027482831 scopus 로고
    • Hepatocyte nuclear factor 3/fork head or 'winged helix' proteins: A family of transcription factors of diverse biological function
    • Lai E, Clark KL, Burley S, James E, Darnell J. Hepatocyte nuclear factor 3/fork head or 'winged helix' proteins: a family of transcription factors of diverse biological function. Proc Natl Acad Sci USA. 90:1993;10421-10423.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10421-10423
    • Lai, E.1    Clark, K.L.2    Burley, S.3    James, E.4    Darnell, J.5
  • 41
    • 0026666377 scopus 로고
    • E. coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains
    • Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. E. coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin-and DNA-binding domains. Proc Natl Acad Sci USA. 89:1992;9257-9261.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 42
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and structural meaning of sequence alignment
    • Sander C, Schneider R. Database of homology-derived protein structures and structural meaning of sequence alignment. Proteins. 9:1991;56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 43
    • 0030016336 scopus 로고    scopus 로고
    • Identification of two DNA-binding sites on the globular domain of histone H5
    • of special interest. This paper reports further characterization of the DNA-binding properties of the linker histone H5, which builds on earlier work in [10].
    • Goytisolo FA, Gerchman S-E, Yu X, Rees C, Graziano V, Ramakrishnan V, Thomas JO. Identification of two DNA-binding sites on the globular domain of histone H5. of special interest EMBO J. 15:1996;3421-3429 This paper reports further characterization of the DNA-binding properties of the linker histone H5, which builds on earlier work in [10].
    • (1996) EMBO J , vol.15 , pp. 3421-3429
    • Goytisolo, F.A.1    Gerchman, S.-E.2    Yu, X.3    Rees, C.4    Graziano, V.5    Ramakrishnan, V.6    Thomas, J.O.7
  • 44
    • 0026089359 scopus 로고
    • Extracellular signals that regulate liver transcription factors during hepatic differentiation in vitro
    • Liu J-K, DiPersio CM, Zaret KS. Extracellular signals that regulate liver transcription factors during hepatic differentiation in vitro. Mol Cell Biol. 11:1991;773-784.
    • (1991) Mol Cell Biol , vol.11 , pp. 773-784
    • Liu, J.-K.1    Dipersio, C.M.2    Zaret, K.S.3
  • 45
    • 0027507894 scopus 로고
    • An active tissue-specific enhancer and bound transcription factors existing in a precisely position nucleosomal array
    • McPherson C, Shin E-Y, Friedman D, Zaret K. An active tissue-specific enhancer and bound transcription factors existing in a precisely position nucleosomal array. Cell. 75:1993;387-398.
    • (1993) Cell , vol.75 , pp. 387-398
    • McPherson, C.1    Shin, E.-Y.2    Friedman, D.3    Zaret, K.4
  • 46
    • 0029867161 scopus 로고    scopus 로고
    • Nucleosome positioning properties of the albumin transcriptional enhancer
    • of special interest. The authors report further characterization of the nucleosome-phasing properties of the linker histone-like transcription factor HNF-3α, which builds on earlier work in [45].
    • McPherson CE, Horowitz R, Woodcock CL, Jiang C, Zaret KS. Nucleosome positioning properties of the albumin transcriptional enhancer. of special interest Nucleic Acids Res. 24:1996;397-404 The authors report further characterization of the nucleosome-phasing properties of the linker histone-like transcription factor HNF-3α, which builds on earlier work in [45].
    • (1996) Nucleic Acids Res , vol.24 , pp. 397-404
    • McPherson, C.E.1    Horowitz, R.2    Woodcock, C.L.3    Jiang, C.4    Zaret, K.S.5
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst. 24:1991;946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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