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Chromosomal protein
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PDB id
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1ghc
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Contents |
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* Residue conservation analysis
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PDB id:
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Chromosomal protein
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Title:
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Homo-and heteronuclear two-dimensional nmr studies of the globular domain of histone h1: full assignment, tertiary structure, and comparison with the globular domain of histone h5
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Structure:
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Gh1. Chain: a. Engineered: yes
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Cell_line: h5
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NMR struc:
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14 models
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Authors:
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C.Cerf,G.Lippens,V.Ramakrishnan,S.Muyldermans,A.Segers, L.Wyns,S.J.Wodak,K.Hallenga
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Key ref:
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C.Cerf
et al.
(1994).
Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5.
Biochemistry,
33,
11079-11086.
PubMed id:
DOI:
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Date:
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16-May-94
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Release date:
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31-Aug-94
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PROCHECK
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Headers
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References
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P08287
(H11L_CHICK) -
Histone H1.11L
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Seq:
Struc:
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225 a.a.
75 a.a.*
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Key: |
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PfamA domain |
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PfamB domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Gene Ontology (GO) functional annotation
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Cellular component
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nucleus
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2 terms
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Biological process
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nucleosome assembly
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1 term
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Biochemical function
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DNA binding
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1 term
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DOI no:
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Biochemistry
33:11079-11086
(1994)
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PubMed id:
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Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: full assignment, tertiary structure, and comparison with the globular domain of histone H5.
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C.Cerf,
G.Lippens,
V.Ramakrishnan,
S.Muyldermans,
A.Segers,
L.Wyns,
S.J.Wodak,
K.Hallenga.
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ABSTRACT
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The globular domain of chicken histone H1 (GH1) has been studied by 1H
homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. After the full
assignment of the proton and 15N resonances, the tertiary structure of GH1 was
determined by an iterative procedure using distance geometry and restrained
simulated annealing. The secondary structure elements of GH1, three helices
(S5-A16, S24-A34, N42-K56) followed by a beta-hairpin (L59-L73), are folded in a
manner very similar to the corresponding parts of the globular domain of chicken
histone H5 (GH5) [Clore et al. (1987) EMBO J. 6, 1833-1842; Ramakrishnan et al.
(1993) Nature 362, 219-223]. However, subtle differences are detected between
the two structures and between the electrostatic potentials surrounding the
molecules. The most important differences are located in the loop between the
second and third helices, a region that could be responsible for the different
affinity for DNA. The most positively charged regions are not found in exactly
the same position in GH1 and GH5. Nevertheless, their location seems to agree
with the model where nucleosome binding takes place through contact points
located at one DNA terminus and close to the dyad axis of the nucleosome
[Schwabe & Travers (1993) Curr. Biol. 3, 628-630].
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Hayashihara,
S.Uchiyama,
S.Shimamoto,
S.Kobayashi,
M.Tomschik,
H.Wakamatsu,
D.No,
H.Sugahara,
N.Hori,
M.Noda,
T.Ohkubo,
J.Zlatanova,
S.Matsunaga,
and
K.Fukui
(2010).
The middle region of an HP1-binding protein, HP1-BP74, associates with linker DNA at the entry/exit site of nucleosomal DNA.
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J Biol Chem, 285,
6498-6507.
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PDB code:
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S.H.Syed,
D.Goutte-Gattat,
N.Becker,
S.Meyer,
M.S.Shukla,
J.J.Hayes,
R.Everaers,
D.Angelov,
J.Bednar,
and
S.Dimitrov
(2010).
Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome.
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Proc Natl Acad Sci U S A, 107,
9620-9625.
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S.J.McBryant,
X.Lu,
and
J.C.Hansen
(2010).
Multifunctionality of the linker histones: an emerging role for protein-protein interactions.
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Cell Res, 20,
519-528.
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S.Kohler,
and
L.A.Cirillo
(2010).
Stable chromatin binding prevents FoxA acetylation, preserving FoxA chromatin remodeling.
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J Biol Chem, 285,
464-472.
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A.Levy,
M.Eyal,
G.Hershkovits,
M.Salmon-Divon,
M.Klutstein,
and
D.J.Katcoff
(2008).
Yeast linker histone Hho1p is required for efficient RNA polymerase I processivity and transcriptional silencing at the ribosomal DNA.
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Proc Natl Acad Sci U S A, 105,
11703-11708.
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V.Galius,
C.Leontiou,
T.Richmond,
and
G.Wider
(2008).
Projected [(1)H, (15)N]-HMQC-[ (1)H, (1)H]-NOESY for large molecular systems: application to a 121 kDa protein-DNA complex.
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J Biomol NMR, 40,
175-181.
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A.Ramaswamy,
and
I.Ioshikhes
(2007).
Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone.
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BMC Struct Biol, 7,
76.
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T.Kawamura,
L.U.Le,
H.Zhou,
and
F.W.Dahlquist
(2007).
Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation.
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J Mol Biol, 365,
1130-1142.
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PDB code:
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W.Goebel,
N.Obermeyer,
N.Bleicher,
M.Kratzmeier,
H.J.Eibl,
D.Doenecke,
and
W.Albig
(2007).
Apoptotic DNA fragmentation is not related to the phosphorylation state of histone H1.
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Biol Chem, 388,
197-206.
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L.Fan,
and
V.A.Roberts
(2006).
Complex of linker histone H5 with the nucleosome and its implications for chromatin packing.
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Proc Natl Acad Sci U S A, 103,
8384-8389.
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A.C.Harvey,
and
J.A.Downs
(2004).
What functions do linker histones provide?
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Mol Microbiol, 53,
771-775.
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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.
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Ann N Y Acad Sci, 1030,
644-655.
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|
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K.Ono,
O.Kusano,
S.Shimotakahara,
M.Shimizu,
T.Yamazaki,
and
H.Shindo
(2003).
The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
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Nucleic Acids Res, 31,
7199-7207.
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PDB code:
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L.C.Trotman,
N.Mosberger,
M.Fornerod,
R.P.Stidwill,
and
U.F.Greber
(2001).
Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1.
|
| |
Nat Cell Biol, 3,
1092-1100.
|
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|
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A.Travers
(1999).
The location of the linker histone on the nucleosome.
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| |
Trends Biochem Sci, 24,
4-7.
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|
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L.A.Cirillo,
and
K.S.Zaret
(1999).
An early developmental transcription factor complex that is more stable on nucleosome core particles than on free DNA.
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Mol Cell, 4,
961-969.
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H.G.Patterton,
C.C.Landel,
D.Landsman,
C.L.Peterson,
and
R.T.Simpson
(1998).
The biochemical and phenotypic characterization of Hho1p, the putative linker histone H1 of Saccharomyces cerevisiae.
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J Biol Chem, 273,
7268-7276.
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J.P.Schneider,
A.Lombardi,
and
W.F.DeGrado
(1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
|
| |
Fold Des, 3,
R29-R40.
|
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J.Widom
(1998).
Structure, dynamics, and function of chromatin in vitro.
|
| |
Annu Rev Biophys Biomol Struct, 27,
285-327.
|
|
|
|
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|
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K.Zaret
(1998).
Early liver differentiation: genetic potentiation and multilevel growth control.
|
| |
Curr Opin Genet Dev, 8,
526-531.
|
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|
|
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|
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L.A.Cirillo,
C.E.McPherson,
P.Bossard,
K.Stevens,
S.Cherian,
E.Y.Shim,
K.L.Clark,
S.K.Burley,
and
K.S.Zaret
(1998).
Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome.
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EMBO J, 17,
244-254.
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|
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A.Travers,
and
H.Drew
(1997).
DNA recognition and nucleosome organization.
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Biopolymers, 44,
423-433.
|
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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.
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| |
Mol Cell Biol, 17,
1189-1200.
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D.T.Brown,
A.Gunjan,
B.T.Alexander,
and
D.B.Sittman
(1997).
Differential effect of H1 variant overproduction on gene expression is due to differences in the central globular domain.
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| |
Nucleic Acids Res, 25,
5003-5009.
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J.G.Omichinski,
P.V.Pedone,
G.Felsenfeld,
A.M.Gronenborn,
and
G.M.Clore
(1997).
The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode.
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Nat Struct Biol, 4,
122-132.
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PDB codes:
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V.Ramakrishnan
(1997).
Histone structure and the organization of the nucleosome.
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Annu Rev Biophys Biomol Struct, 26,
83.
|
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F.A.Goytisolo,
L.C.Packman,
and
J.O.Thomas
(1996).
Photoaffinity labelling of a DNA-binding site on the globular domain of histone H5.
|
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Eur J Biochem, 242,
619-626.
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F.A.Goytisolo,
S.E.Gerchman,
X.Yu,
C.Rees,
V.Graziano,
V.Ramakrishnan,
and
J.O.Thomas
(1996).
Identification of two DNA-binding sites on the globular domain of histone H5.
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EMBO J, 15,
3421-3429.
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K.Kondili,
O.Tsolas,
and
T.Papamarcaki
(1996).
Selective interaction between parathymosin and histone H1.
|
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Eur J Biochem, 242,
67-74.
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M.McArthur,
and
J.O.Thomas
(1996).
A preference of histone H1 for methylated DNA.
|
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EMBO J, 15,
1705-1714.
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V.Ramakrishnan
(1995).
The histone fold: evolutionary questions.
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Proc Natl Acad Sci U S A, 92,
11328-11330.
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S.Muyldermans,
J.De Jonge,
L.Wyns,
and
A.A.Travers
(1994).
Differential association of linker histones H1 and H5 with telomeric nucleosomes in chicken erythrocytes.
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Nucleic Acids Res, 22,
5635-5639.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
