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PDBsum entry 1hio

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protein links
Chromosomal protein PDB id
1hio
Jmol
Contents
Protein chains
95 a.a.* *
90 a.a.* *
93 a.a.* *
76 a.a.* *
* Residue conservation analysis
* C-alpha coords only
PDB id:
1hio
Name: Chromosomal protein
Title: Histone octamer (chicken), chromosomal protein, alpha carbons only
Structure: Histone h2a. Chain: a. Histone h2b. Chain: b. Histone h3. Chain: c. Histone h4. Chain: d
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: thymus. Organ: thymus
Resolution:
3.10Å     R-factor:   0.255    
Authors: G.Arents,E.N.Moudrianakis
Key ref:
G.Arents et al. (1991). The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc Natl Acad Sci U S A, 88, 10148-10152. PubMed id: 1946434 DOI: 10.1073/pnas.88.22.10148
Date:
19-Sep-91     Release date:   25-Nov-98    
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02263  (H2A4_CHICK) -  Histone H2A-IV
Seq:
Struc:
129 a.a.
95 a.a.
Protein chain
Pfam   ArchSchema ?
P0C1H5  (H2B7_CHICK) -  Histone H2B 7
Seq:
Struc:
126 a.a.
90 a.a.*
Protein chain
Pfam   ArchSchema ?
P84229  (H32_CHICK) -  Histone H3.2
Seq:
Struc:
136 a.a.
93 a.a.*
Protein chain
Pfam   ArchSchema ?
P62801  (H4_CHICK) -  Histone H4
Seq:
Struc:
103 a.a.
76 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   2 terms 
  Biological process     nucleosome assembly   1 term 
  Biochemical function     DNA binding     2 terms  

 

 
    reference    
 
 
DOI no: 10.1073/pnas.88.22.10148 Proc Natl Acad Sci U S A 88:10148-10152 (1991)
PubMed id: 1946434  
 
 
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
G.Arents, R.W.Burlingame, B.C.Wang, W.E.Love, E.N.Moudrianakis.
 
  ABSTRACT  
 
The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A. The histone octamer is a tripartite assembly in which a centrally located (H3-H4)2 tetramer is flanked by two H2A-H2B dimers. It has a complex outer surface; depending on the perspective, the structure appears as a wedge or as a flat disk. The disk represents the planar projection of a left-handed proteinaceous superhelix with approximately 28 A pitch. The diameter of the particle is 65 A and the length is 60 A at its maximum and approximately 10 A at its minimum extension; these dimensions are in agreement with those reported earlier by Klug et al. [Klug, A., Rhodes, D., Smith, J., Finch, J. T. & Thomas, J. O. (1980) Nature (London) 287, 509-516]. The folded histone chains are elongated rather than globular and are assembled in a characteristic "handshake" motif. The individual polypeptides share a common central structural element of the helix-loop-helix type, which we name the histone fold.
 
  Selected figure(s)  
 
Figure 3.
FIG. 3. Three orthogonal of the histone octamer. (a) View showing the tripartite nature of the histone looking down the molecular twofold axis with the superhelical axis running hori- zontally from left to right. We refer to this as the front view. (b) Protein wedge as it appears by looking down at a plane containing the twofold and the superhelical axes, with the twofold axis running from top to bottom. The apex of the wedge is formed by the tetramer, while the H2A-H2B dimers form the lobes of the wedge. (c) View showing the histone octamer as a disk, looking down into the superhelical axis with the twofold axis Protrusions from the curved surface are due to the termini of H2A, H2B, and H3. Surfaces were calculated from a-carbon positions at twice the van der Waals radius. The H2A-H2B dimers dark and the tetramer is white.
Figure 5.
FIG. 5. Stereo pair of the H2A-H2B and H3-H4 dimer domains within the histone octamer, viewed approximately down the superhelical axis so as to optimize visualization of the four chains and the histone fold. For reasons of clarity, only one of each histone pair is shown. The amino end of each chain in the model is marked by an arrow.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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PDB code: 3aad
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17028330 R.E.Baker, and K.Rogers (2006).
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16802969 W.Li, S.X.Dou, P.Xie, and P.Y.Wang (2006).
Brownian dynamics simulation of directional sliding of histone octamers caused by DNA bending.
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16287087 Y.Qiu, V.Tereshko, Y.Kim, R.Zhang, F.Collart, M.Yousef, A.Kossiakoff, and A.Joachimiak (2006).
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  Proteins, 62, 8.
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15624215 A.Ramaswamy, I.Bahar, and I.Ioshikhes (2005).
Structural dynamics of nucleosome core particle: comparison with nucleosomes containing histone variants.
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16242031 B.D.Silverman (2005).
Asymmetry in the burial of hydrophobic residues along the histone chains of eukarya, archaea and a transcription factor.
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High-resolution structure of the native histone octamer.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 541-545.
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Prediction of unfolded segments in a protein sequence based on amino acid composition.
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16277689 P.L.Carl, B.R.Temple, and P.L.Cohen (2005).
Most nuclear systemic autoantigens are extremely disordered proteins: implications for the etiology of systemic autoimmunity.
  Arthritis Res Ther, 7, R1360-R1374.  
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  Eur J Biochem, 271, 1153-1162.  
15096635 D.D.Banks, and L.M.Gloss (2004).
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome.
  Protein Sci, 13, 1304-1316.  
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Functional complementation of human centromere protein A (CENP-A) by Cse4p from Saccharomyces cerevisiae.
  Mol Cell Biol, 24, 6620-6630.  
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  Biol Reprod, 70, 1843-1851.  
15659848 J.M.Nicholson, C.M.Wood, C.D.Reynolds, A.Brown, S.J.Lambert, L.Chantalat, and J.P.Baldwin (2004).
Histone structures: targets for modifications by molecular assemblies.
  Ann N Y Acad Sci, 1030, 644-655.  
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Phylogenomics of the nucleosome.
  Nat Struct Biol, 10, 882-891.  
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Conformation of reconstituted mononucleosomes and effect of linker histone H1 binding studied by scanning force microscopy.
  Biophys J, 85, 4012-4022.  
12672489 K.Luger (2003).
Structure and dynamic behavior of nucleosomes.
  Curr Opin Genet Dev, 13, 127-135.  
12876341 L.Chantalat, J.M.Nicholson, S.J.Lambert, A.J.Reid, M.J.Donovan, C.D.Reynolds, C.M.Wood, and J.P.Baldwin (2003).
Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A resolution.
  Acta Crystallogr D Biol Crystallogr, 59, 1395-1407.
PDB code: 1hq3
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Global and specific transcriptional repression by the histone H3 amino terminus in yeast.
  Proc Natl Acad Sci U S A, 100, 4084-4089.  
12743713 P.B.Hebbar, and T.K.Archer (2003).
Chromatin remodeling by nuclear receptors.
  Chromosoma, 111, 495-504.  
12917342 P.W.Hsiao, C.J.Fryer, K.W.Trotter, W.Wang, and T.K.Archer (2003).
BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.
  Mol Cell Biol, 23, 6210-6220.  
12866056 S.A.Sullivan, and D.Landsman (2003).
Characterization of sequence variability in nucleosome core histone folds.
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11940675 D.B.Kirschner, E.vom Baur, C.Thibault, S.L.Sanders, Y.G.Gangloff, I.Davidson, P.A.Weil, and L.Tora (2002).
Distinct mutations in yeast TAF(II)25 differentially affect the composition of TFIID and SAGA complexes as well as global gene expression patterns.
  Mol Cell Biol, 22, 3178-3193.  
12150903 E.M.Bradbury (2002).
Chromatin structure and dynamics: state-of-the-art.
  Mol Cell, 10, 13-19.  
12438377 F.T.Papageorgiou, and K.P.Soteriadou (2002).
Expression of a novel Leishmania gene encoding a histone H1-like protein in Leishmania major modulates parasite infectivity in vitro.
  Infect Immun, 70, 6976-6986.  
11988475 J.C.Hansen (2002).
Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions.
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12230577 J.Castillo, A.Zúñiga, L.Franco, and M.I.Rodrigo (2002).
A chromatin-associated protein from pea seeds preferentially binds histones H3 and H4.
  Eur J Biochem, 269, 4641-4648.  
11854477 J.J.Hayes, and J.C.Hansen (2002).
New insights into unwrapping DNA from the nucleosome from a single-molecule optical tweezers method.
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12086617 K.Ahmad, and S.Henikoff (2002).
The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly.
  Mol Cell, 9, 1191-1200.  
  12426116 P.E.Carrington, F.Al-Mjeni, M.A.Zoroddu, M.Costa, and M.J.Maroney (2002).
Use of XAS for the elucidation of metal structure and function: applications to nickel biochemistry, molecular toxicology, and carcinogenesis.
  Environ Health Perspect, 110, 705-708.  
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Identification and characterization of the genes encoding the core histones and histone variants of Neurospora crassa.
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11752331 S.Sullivan, D.W.Sink, K.L.Trout, I.Makalowska, P.M.Taylor, A.D.Baxevanis, and D.Landsman (2002).
The Histone Database.
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11983172 W.An, V.B.Palhan, M.A.Karymov, S.H.Leuba, and R.G.Roeder (2002).
Selective requirements for histone H3 and H4 N termini in p300-dependent transcriptional activation from chromatin.
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11707409 A.E.de la Barre, D.Angelov, A.Molla, and S.Dimitrov (2001).
The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation.
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11447119 A.Eberharter, S.Ferrari, G.Längst, T.Straub, A.Imhof, P.Varga-Weisz, M.Wilm, and P.B.Becker (2001).
Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome remodelling.
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Prodos is a conserved transcriptional regulator that interacts with dTAF(II)16 in Drosophila melanogaster.
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Adaptive evolution of Cid, a centromere-specific histone in Drosophila.
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Trajectory of nucleosomal linker DNA studied by fluorescence resonance energy transfer.
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Constraints, histones, and the 30-nm spiral.
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  Mol Cell, 8, 841-853.
PDB code: 1k5j
11295558 Y.G.Gangloff, C.Romier, S.Thuault, S.Werten, and I.Davidson (2001).
The histone fold is a key structural motif of transcription factor TFIID.
  Trends Biochem Sci, 26, 250-257.  
10654937 A.E.de la Barre, V.Gerson, S.Gout, M.Creaven, C.D.Allis, and S.Dimitrov (2000).
Core histone N-termini play an essential role in mitotic chromosome condensation.
  EMBO J, 19, 379-391.  
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Negative constrained DNA supercoiling in archaeal nucleosomes.
  Mol Microbiol, 35, 341-349.  
10655499 E.V.Howman, K.J.Fowler, A.J.Newson, S.Redward, A.C.MacDonald, P.Kalitsis, and K.H.Choo (2000).
Early disruption of centromeric chromatin organization in centromere protein A (Cenpa) null mice.
  Proc Natl Acad Sci U S A, 97, 1148-1153.  
11026679 J.Ausió (2000).
Analytical ultracentrifugation and the characterization of chromatin structure.
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10759838 J.Castillo, M.I.Rodrigo, J.A.Márquez, A.Zúñiga, and L.Franco (2000).
A pea nuclear protein that is induced by dehydration belongs to the vicilin superfamily.
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11000274 J.D.Jackson, and M.A.Gorovsky (2000).
Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants.
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Asymmetries in the nucleosome core particle at 2.5 A resolution.
  Acta Crystallogr D Biol Crystallogr, 56, 1513-1534.
PDB code: 1eqz
11123932 J.T.Millard, and E.E.Wilkes (2000).
cis- and trans-diamminedichloroplatinum(II) interstrand cross-linking of a defined sequence nucleosomal core particle.
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10891506 L.Glowczewski, P.Yang, T.Kalashnikova, M.S.Santisteban, and M.M.Smith (2000).
Histone-histone interactions and centromere function.
  Mol Cell Biol, 20, 5700-5711.  
11081628 M.S.Santisteban, T.Kalashnikova, and M.M.Smith (2000).
Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes.
  Cell, 103, 411-422.  
11057899 P.Cheung, C.D.Allis, and P.Sassone-Corsi (2000).
Signaling to chromatin through histone modifications.
  Cell, 103, 263-271.  
10592260 S.A.Sullivan, L.Aravind, I.Makalowska, A.D.Baxevanis, and D.Landsman (2000).
The histone database: a comprehensive WWW resource for histones and histone fold-containing proteins.
  Nucleic Acids Res, 28, 320-322.  
10982840 V.Morales, and H.Richard-Foy (2000).
Role of histone N-terminal tails and their acetylation in nucleosome dynamics.
  Mol Cell Biol, 20, 7230-7237.  
10618382 Y.Cui, and C.Bustamante (2000).
Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure.
  Proc Natl Acad Sci U S A, 97, 127-132.  
10983971 Y.Dou, and M.A.Gorovsky (2000).
Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch.
  Mol Cell, 6, 225-231.  
10594036 Y.G.Gangloff, S.Werten, C.Romier, L.Carré, O.Poch, D.Moras, and I.Davidson (2000).
The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.
  Mol Cell Biol, 20, 340-351.  
10399912 A.Hamiche, R.Sandaltzopoulos, D.A.Gdula, and C.Wu (1999).
ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF.
  Cell, 97, 833-842.  
10029546 C.Logie, C.Tse, J.C.Hansen, and C.L.Peterson (1999).
The core histone N-terminal domains are required for multiple rounds of catalytic chromatin remodeling by the SWI/SNF and RSC complexes.
  Biochemistry, 38, 2514-2522.  
10361708 D.Bernhard (1999).
Several highly divergent histone H3 genes are present in the hypotrichous ciliate Stylonychia lemnae.
  FEMS Microbiol Lett, 175, 45-50.  
  10454532 D.Vermaak, P.A.Wade, P.L.Jones, Y.B.Shi, and A.P.Wolffe (1999).
Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte.
  Mol Cell Biol, 19, 5847-5860.  
10628834 H.Zhao, Y.Zhang, S.B.Zhang, C.Jiang, Q.Y.He, M.Q.Li, and R.L.Qian (1999).
The structure of the nucleosome core particle of chromatin in chicken erythrocytes visualized by using atomic force microscopy.
  Cell Res, 9, 255-260.  
10422263 J.Pérez-Martín (1999).
Chromatin and transcription in Saccharomyces cerevisiae.
  FEMS Microbiol Rev, 23, 503-523.  
9878065 J.Recht, and M.A.Osley (1999).
Mutations in both the structured domain and N-terminus of histone H2B bypass the requirement for Swi-Snf in yeast.
  EMBO J, 18, 229-240.  
  10454560 K.C.Keith, R.E.Baker, Y.Chen, K.Harris, S.Stoler, and M.Fitzgerald-Hayes (1999).
Analysis of primary structural determinants that distinguish the centromere-specific function of histone variant Cse4p from histone H3.
  Mol Cell Biol, 19, 6130-6139.  
10462418 K.van Holde, and J.Zlatanova (1999).
The nucleosome core particle: does it have structural and physiologic relevance?
  Bioessays, 21, 776-780.  
10077600 M.Goldberg, A.Harel, M.Brandeis, T.Rechsteiner, T.J.Richmond, A.M.Weiss, and Y.Gruenbaum (1999).
The tail domain of lamin Dm0 binds histones H2A and H2B.
  Proc Natl Acad Sci U S A, 96, 2852-2857.  
10458604 R.D.Kornberg, and Y.Lorch (1999).
Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome.
  Cell, 98, 285-294.  
10353812 S.P.Chandler, D.Guschin, N.Landsberger, and A.P.Wolffe (1999).
The methyl-CpG binding transcriptional repressor MeCP2 stably associates with nucleosomal DNA.
  Biochemistry, 38, 7008-7018.  
9421495 A.I.Slesarev, G.I.Belova, S.A.Kozyavkin, and J.A.Lake (1998).
Evidence for an early prokaryotic origin of histones H2A and H4 prior to the emergence of eukaryotes.
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9636058 A.Taquet, R.Labarbe, and C.Houssier (1998).
Calorimetric investigation of ethidium and netropsin binding to chicken erythrocyte chromatin.
  Biochemistry, 37, 9119-9126.  
9427644 A.Verreault, P.D.Kaufman, R.Kobayashi, and B.Stillman (1998).
Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase.
  Curr Biol, 8, 96.  
9695952 C.Birck, O.Poch, C.Romier, M.Ruff, G.Mengus, A.C.Lavigne, I.Davidson, and D.Moras (1998).
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.
  Cell, 94, 239-249.
PDB codes: 1bh8 1bh9
  9502778 C.Mohan, E.Alas, L.Morel, P.Yang, and E.K.Wakeland (1998).
Genetic dissection of SLE pathogenesis. Sle1 on murine chromosome 1 leads to a selective loss of tolerance to H2A/H2B/DNA subnucleosomes.
  J Clin Invest, 101, 1362-1372.  
9628724 D.Guschin, S.Chandler, and A.P.Wolffe (1998).
Asymmetric linker histone association directs the asymmetric rearrangement of core histone interactions in a positioned nucleosome containing a thyroid hormone response element.
  Biochemistry, 37, 8629-8636.  
9482742 H.L.Lee, and T.K.Archer (1998).
Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter.
  EMBO J, 17, 1454-1466.  
9759497 J.L.Workman, and R.E.Kingston (1998).
Alteration of nucleosome structure as a mechanism of transcriptional regulation.
  Annu Rev Biochem, 67, 545-579.  
9556343 J.R.Daban, and A.Bermúdez (1998).
Interdigitated solenoid model for compact chromatin fibers.
  Biochemistry, 37, 4299-4304.  
9646870 J.Widom (1998).
Structure, dynamics, and function of chromatin in vitro.
  Annu Rev Biophys Biomol Struct, 27, 285-327.  
9591681 J.Zlatanova, S.H.Leuba, and K.van Holde (1998).
Chromatin fiber structure: morphology, molecular determinants, structural transitions.
  Biophys J, 74, 2554-2566.  
9628723 K.M.Lee, and J.J.Hayes (1998).
Linker DNA and H1-dependent reorganization of histone-DNA interactions within the nucleosome.
  Biochemistry, 37, 8622-8628.  
9635737 S.H.Leuba, C.Bustamante, K.van Holde, and J.Zlatanova (1998).
Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.
  Biophys J, 74, 2830-2839.  
10384268 S.K.Burley (1998).
X-ray crystallographic studies of eukaryotic transcription factors.
  Cold Spring Harb Symp Quant Biol, 63, 33-40.  
  9632749 T.Sera, and A.P.Wolffe (1998).
Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genes.
  Mol Cell Biol, 18, 3668-3680.  
  9774646 V.Mutskov, D.Gerber, D.Angelov, J.Ausio, J.Workman, and S.Dimitrov (1998).
Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding.
  Mol Cell Biol, 18, 6293-6304.  
9705517 W.An, K.van Holde, and J.Zlatanova (1998).
Linker histone protection of chromatosomes reconstituted on 5S rDNA from Xenopus borealis:a reinvestigation.
  Nucleic Acids Res, 26, 4042-4046.  
9520377 W.An, S.H.Leuba, K.van Holde, and J.Zlatanova (1998).
Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner.
  Proc Natl Acad Sci U S A, 95, 3396-3401.  
9336172 A.Leforestier, and F.Livolant (1997).
Liquid crystalline ordering of nucleosome core particles under macromolecular crowding conditions: evidence for a discotic columnar hexagonal phase.
  Biophys J, 73, 1771-1776.  
9138593 A.Prunell (1997).
Linker histones' role revisited.
  Biophys J, 72, 983-984.  
9332970 B.Hassan, and H.Vaessin (1997).
Daughterless is required for the expression of cell cycle genes in peripheral nervous system precursors of Drosophila embryos.
  Dev Genet, 21, 117-122.  
  9032246 B.Mandl, W.F.Brandt, G.Superti-Furga, P.G.Graninger, M.L.Birnstiel, and M.Busslinger (1997).
The five cleavage-stage (CS) histones of the sea urchin are encoded by a maternally expressed family of replacement histone genes: functional equivalence of the CS H1 and frog H1M (B4) proteins.
  Mol Cell Biol, 17, 1189-1200.  
9033581 C.M.Read, and P.C.Driscoll (1997).
GAGA over the nucleosome.
  Nat Struct Biol, 4, 87-89.  
8990153 D.B.Nikolov, and S.K.Burley (1997).
RNA polymerase II transcription initiation: a structural view.
  Proc Natl Acad Sci U S A, 94, 15-22.  
9166766 E.Ballestar, and L.Franco (1997).
Use of the transglutaminase reaction to study the dissociation of histone N-terminal tails from DNA in nucleosome core particles.
  Biochemistry, 36, 5963-5969.  
9096360 E.L.Gadbois, D.M.Chao, J.C.Reese, M.R.Green, and R.A.Young (1997).
Functional antagonism between RNA polymerase II holoenzyme and global negative regulator NC2 in vivo.
  Proc Natl Acad Sci U S A, 94, 3145-3150.  
9396628 G.B.Fogel, and C.F.Brunk (1997).
Expression of Tetrahymena histone H4 in yeast.
  Biochim Biophys Acta, 1354, 116-126.  
  9121454 G.Prelich (1997).
Saccharomyces cerevisiae BUR6 encodes a DRAP1/NC2alpha homolog that has both positive and negative roles in transcription in vivo.
  Mol Cell Biol, 17, 2057-2065.  
9315878 H.F.Peng, and V.Jackson (1997).
Measurement of the frequency of histone displacement during the in vitro transcription of nucleosomes: RNA is a competitor for these histones.
  Biochemistry, 36, 12371-12382.  
  9372928 H.Kurumizaka, and A.P.Wolffe (1997).
Sin mutations of histone H3: influence on nucleosome core structure and function.
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9368751 J.Widom (1997).
Chromatin: the nucleosome unwrapped.
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9384590 J.Wong, Q.Li, B.Z.Levi, Y.B.Shi, and A.P.Wolffe (1997).
Structural and functional features of a specific nucleosome containing a recognition element for the thyroid hormone receptor.
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9356434 J.Zlatanova (1997).
Archaeal chromatin: virtual or real?
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9256417 K.M.Lee, and J.J.Hayes (1997).
The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.
  Proc Natl Acad Sci U S A, 94, 8959-8964.  
9155034 M.A.Wechser, M.P.Kladde, J.A.Alfieri, and C.L.Peterson (1997).
Effects of Sin- versions of histone H4 on yeast chromatin structure and function.
  EMBO J, 16, 2086-2095.  
9171362 M.S.Santisteban, G.Arents, E.N.Moudrianakis, and M.M.Smith (1997).
Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression.
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CCAAT-binding factor NF-Y and RFX are required for in vivo assembly of a nucleoprotein complex that spans 250 base pairs: the invariant chain promoter as a model.
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9303316 P.T.Georgel, T.Tsukiyama, and C.Wu (1997).
Role of histone tails in nucleosome remodeling by Drosophila NURF.
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9024683 R.D.Shelby, O.Vafa, and K.F.Sullivan (1997).
Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sites.
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9351811 R.N.Dutnall, and V.Ramakrishnan (1997).
Twists and turns of the nucleosome: tails without ends.
  Structure, 5, 1255-1259.  
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Histone-like transcription factors in eukaryotes.
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9129808 T.C.Bishop, D.Kosztin, and K.Schulten (1997).
How hormone receptor-DNA binding affects nucleosomal DNA: the role of symmetry.
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Histone structure and the organization of the nucleosome.
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8594591 A.D.Baxevanis, and D.Landsman (1996).
Histone Sequence Database: a compilation of highly-conserved nucleoprotein sequences.
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A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains.
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8948634 A.Goppelt, and M.Meisterernst (1996).
Characterization of the basal inhibitor of class II transcription NC2 from Saccharomyces cerevisiae.
  Nucleic Acids Res, 24, 4450-4455.  
8755519 A.Hamiche, V.Carot, M.Alilat, F.De Lucia, M.F.O'Donohue, B.Revet, and A.Prunell (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.  
8552683 A.Nakanishi, J.Clever, M.Yamada, P.P.Li, and H.Kasamatsu (1996).
Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA.
  Proc Natl Acad Sci U S A, 93, 96.  
8919875 C.A.Ouzounis, and N.C.Kyrpides (1996).
Parallel origins of the nucleosome core and eukaryotic transcription from Archaea.
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8995050 C.A.Ouzounis, and N.C.Kyrpides (1996).
The core histone fold: limits to functional versatility.
  J Mol Evol, 43, 541-542.  
  8670902 F.Lenfant, R.K.Mann, B.Thomsen, X.Ling, and M.Grunstein (1996).
All four core histone N-termini contain sequences required for the repression of basal transcription in yeast.
  EMBO J, 15, 3974-3985.  
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Role of amino-terminal histone domains in chromatin replication.
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  8754798 I.S.Kim, S.Sinha, B.de Crombrugghe, and S.N.Maity (1996).
Determination of functional domains in the C subunit of the CCAAT-binding factor (CBF) necessary for formation of a CBF-DNA complex: CBF-B interacts simultaneously with both the CBF-A and CBF-C subunits to form a heterotrimeric CBF molecule.
  Mol Cell Biol, 16, 4003-4013.  
  8703085 J.H.Waterborg, and A.J.Robertson (1996).
Common features of analogous replacement histone H3 genes in animals and plants.
  J Mol Evol, 43, 194-206.  
  8649361 J.Recht, B.Dunn, A.Raff, and M.A.Osley (1996).
Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae.
  Mol Cell Biol, 16, 2545-2553.  
8831284 K.van Holde, and J.Zlatanova (1996).
Chromatin architectural proteins and transcription factors: a structural connection.
  Bioessays, 18, 697-700.  
8855215 K.van Holde, and J.Zlatanova (1996).
What determines the folding of the chromatin fiber?
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8917496 L.Freeman, H.Kurumizaka, and A.P.Wolffe (1996).
Functional domains for assembly of histones H3 and H4 into the chromatin of Xenopus embryos.
  Proc Natl Acad Sci U S A, 93, 12780-12785.  
  8622646 M.M.Smith, P.Yang, M.S.Santisteban, P.W.Boone, A.T.Goldstein, and P.C.Megee (1996).
A novel histone H4 mutant defective in nuclear division and mitotic chromosome transmission.
  Mol Cell Biol, 16, 1017-1026.  
  8844144 P.A.Compagnone-Post, and M.A.Osley (1996).
Mutations in the SPT4, SPT5, and SPT6 genes alter transcription of a subset of histone genes in Saccharomyces cerevisiae.
  Genetics, 143, 1543-1554.  
9112224 R.W.Burlingame, and R.L.Rubin (1996).
Autoantibody to the nucleosome subunit (H2A-H2B)-DNA is an early and ubiquitous feature of lupus-like conditions.
  Mol Biol Rep, 23, 159-166.  
  8524312 S.Sinha, I.S.Kim, K.Y.Sohn, B.de Crombrugghe, and S.N.Maity (1996).
Three classes of mutations in the A subunit of the CCAAT-binding factor CBF delineate functional domains involved in the three-step assembly of the CBF-DNA complex.
  Mol Cell Biol, 16, 328-337.  
8639689 V.Karantza, E.Freire, and E.N.Moudrianakis (1996).
Thermodynamic studies of the core histones: pH and ionic strength effects on the stability of the (H3-H4)/(H3-H4)2 system.
  Biochemistry, 35, 2037-2046.  
7651829 A.D.Baxevanis, G.Arents, E.N.Moudrianakis, and D.Landsman (1995).
A variety of DNA-binding and multimeric proteins contain the histone fold motif.
  Nucleic Acids Res, 23, 2685-2691.  
7748166 D.Pruss, J.J.Hayes, and A.P.Wolffe (1995).
Nucleosomal anatomy--where are the histones?
  Bioessays, 17, 161-170.  
7479959 G.Arents, and E.N.Moudrianakis (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.  
8522597 J.Bednar, R.A.Horowitz, J.Dubochet, and C.L.Woodcock (1995).
Chromatin conformation and salt-induced compaction: three-dimensional structural information from cryoelectron microscopy.
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A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects in vivo.
  Mol Cell Biol, 15, 1999-2009.  
7479703 S.Vijay-Kumar, N.Chandra, C.Dharia, and J.R.Pehrson (1995).
Crystallization and preliminary X-ray crystallographic studies of nonhistone region of macroH2A.1.
  Proteins, 22, 290-292.  
  7836329 T.J.Darcy, K.Sandman, and J.N.Reeve (1995).
Methanobacterium formicicum, a mesophilic methanogen, contains three HFo histones.
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8524779 V.Ramakrishnan (1995).
The histone fold: evolutionary questions.
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Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex.
  Protein Sci, 4, 187-197.
PDB code: 1gpv
7922373 A.P.Wolffe (1994).
Transcriptional activation. Switched-on chromatin.
  Curr Biol, 4, 525-528.  
  8306969 C.Gutiérrez, R.Freire, M.Salas, and J.M.Hermoso (1994).
Assembly of phage phi 29 genome with viral protein p6 into a compact complex.
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8016088 D.Pruss, F.D.Bushman, and A.P.Wolffe (1994).
Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core.
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Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.
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The central role of chromatin in autoimmune responses to histones and DNA in systemic lupus erythematosus.
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Issues in searching molecular sequence databases.
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Rearrangement of the histone H2A C-terminal domain in the nucleosome.
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Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA.
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Mutations that suppress the deletion of an upstream activating sequence in yeast: involvement of a protein kinase and histone H3 in repressing transcription in vivo.
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Nucleosome-specific antibody from an autoimmune MRL/Mp-lpr/lpr mouse.
  Arthritis Rheum, 36, 552-560.  
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Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome.
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Dynamics of interaction of RNA polymerase II with nucleosomes. I. Effect of salts.
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8473512 R.W.Burlingame, R.L.Rubin, R.S.Balderas, and A.N.Theofilopoulos (1993).
Genesis and evolution of antichromatin autoantibodies in murine lupus implicates T-dependent immunization with self antigen.
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  1498368 A.van Daal, and S.C.Elgin (1992).
A histone variant, H2AvD, is essential in Drosophila melanogaster.
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1365915 J.J.Hayes, and A.P.Wolffe (1992).
The interaction of transcription factors with nucleosomal DNA.
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Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci.
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Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo.
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Autoantibodies associated with lupus induced by diverse drugs target a similar epitope in the (H2A-H2B)-DNA complex.
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