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* Residue conservation analysis
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PDB id:
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Replication/chaperone
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Title:
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Structure of the histone h3-asf1 chaperone interaction
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Structure:
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Anti-silencing protein 1 and histone h3 chimera. Chain: a. Fragment: asf1, residues 2-155 and h3, residues 121-134. Synonym: histone chaperone asf1, anti-silencing function protein 1, yasf1. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: asf1, cia1, yjl115w, j0755, hht1, ybr010w, ybr0201, hht2, sin2, ynl031c, n2749. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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2.20Å
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R-factor:
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0.196
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R-free:
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0.239
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Authors:
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A.J.Antczak,T.Tsubota,P.D.Kaufman,J.M.Berger
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Key ref:
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A.J.Antczak
et al.
(2006).
Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics.
Bmc Struct Biol,
6,
26.
PubMed id:
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Date:
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14-Sep-06
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Release date:
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30-Jan-07
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PROCHECK
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Headers
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References
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Bmc Struct Biol
6:26
(2006)
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PubMed id:
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Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics.
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A.J.Antczak,
T.Tsubota,
P.D.Kaufman,
J.M.Berger.
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ABSTRACT
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BACKGROUND: The histone H3/H4 chaperone Asf1 (anti-silencing function 1) is
required for the establishment and maintenance of proper chromatin structure, as
well as for genome stability in eukaryotes. Asf1 participates in both DNA
replication-coupled (RC) and replication-independent (RI) histone deposition
reactions in vitro and interacts with complexes responsible for both pathways in
vivo. Asf1 is known to directly bind histone H3, however, high-resolution
structural information about the geometry of this interaction was previously
unknown. RESULTS: Here we report the structure of a histone/histone chaperone
interaction. We have solved the 2.2 A crystal structure of the conserved
N-terminal immunoglobulin fold domain of yeast Asf1 (residues 2-155) bound to
the C-terminal helix of yeast histone H3 (residues 121-134). The structure
defines a histone-binding patch on Asf1 consisting of both conserved and
yeast-specific residues; mutation of these residues abrogates H3/H4 binding
affinity. The geometry of the interaction indicates that Asf1 binds to histones
H3/H4 in a manner that likely blocks sterically the H3/H3 interface of the
nucleosomal four-helix bundle. CONCLUSION: These data clarify how Asf1 regulates
histone stoichiometry to modulate epigenetic inheritance. The structure further
suggests a physical model in which Asf1 contributes to interpretation of a
"histone H3 barcode" for sorting H3 isoforms into different deposition pathways.
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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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N.Avvakumov,
A.Nourani,
and
J.Côté
(2011).
Histone chaperones: modulators of chromatin marks.
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Mol Cell,
41,
502-514.
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A.Osakabe,
H.Tachiwana,
T.Matsunaga,
T.Shiga,
R.S.Nozawa,
C.Obuse,
and
H.Kurumizaka
(2010).
Nucleosome formation activity of human somatic nuclear autoantigenic sperm protein (sNASP).
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J Biol Chem,
285,
11913-11921.
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J.C.Hansen,
J.K.Nyborg,
K.Luger,
and
L.A.Stargell
(2010).
Histone chaperones, histone acetylation, and the fluidity of the chromogenome.
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J Cell Physiol,
224,
289-299.
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M.D.Shepherd,
M.K.Kharel,
L.L.Zhu,
S.G.van Lanen,
and
J.Rohr
(2010).
Delineating the earliest steps of gilvocarcin biosynthesis: role of GilP and GilQ in starter unit specificity.
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Org Biomol Chem,
8,
3851-3856.
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S.M.McDonald,
D.Close,
H.Xin,
T.Formosa,
and
C.P.Hill
(2010).
Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.
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Mol Cell,
40,
725-735.
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PDB codes:
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A.De Benedetti
(2009).
Tousled kinase TLK1B counteracts the effect of Asf1 in inhibition of histone H3-H4 tetramer formation.
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BMC Res Notes,
2,
128.
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A.Y.Wang,
J.M.Schulze,
E.Skordalakes,
J.W.Gin,
J.M.Berger,
J.Rine,
and
M.S.Kobor
(2009).
Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation.
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Proc Natl Acad Sci U S A,
106,
21573-21578.
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PDB code:
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N.Dhillon,
J.Raab,
J.Guzzo,
S.J.Szyjka,
S.Gangadharan,
O.M.Aparicio,
B.Andrews,
and
R.T.Kamakaka
(2009).
DNA polymerase epsilon, acetylases and remodellers cooperate to form a specialized chromatin structure at a tRNA insulator.
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EMBO J,
28,
2583-2600.
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S.Takahata,
Y.Yu,
and
D.J.Stillman
(2009).
FACT and Asf1 regulate nucleosome dynamics and coactivator binding at the HO promoter.
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Mol Cell,
34,
405-415.
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A.Galvani,
R.Courbeyrette,
M.Agez,
F.Ochsenbein,
C.Mann,
and
J.Y.Thuret
(2008).
In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells.
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Mol Cell Biol,
28,
3672-3685.
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B.E.Black,
and
E.A.Bassett
(2008).
The histone variant CENP-A and centromere specification.
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Curr Opin Cell Biol,
20,
91.
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J.Fillingham,
J.Recht,
A.C.Silva,
B.Suter,
A.Emili,
I.Stagljar,
N.J.Krogan,
C.D.Allis,
M.C.Keogh,
and
J.F.Greenblatt
(2008).
Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109.
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Mol Cell Biol,
28,
4342-4353.
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N.V.Murzina,
X.Y.Pei,
W.Zhang,
M.Sparkes,
J.Vicente-Garcia,
J.V.Pratap,
S.H.McLaughlin,
T.R.Ben-Shahar,
A.Verreault,
B.F.Luisi,
and
E.D.Laue
(2008).
Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46.
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Structure,
16,
1077-1085.
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PDB codes:
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S.Henikoff
(2008).
Nucleosome destabilization in the epigenetic regulation of gene expression.
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Nat Rev Genet,
9,
15-26.
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T.Stuwe,
M.Hothorn,
E.Lejeune,
V.Rybin,
M.Bortfeld,
K.Scheffzek,
and
A.G.Ladurner
(2008).
The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module.
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Proc Natl Acad Sci U S A,
105,
8884-8889.
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PDB codes:
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Y.J.Park,
and
K.Luger
(2008).
Histone chaperones in nucleosome eviction and histone exchange.
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Curr Opin Struct Biol,
18,
282-289.
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A.Loyola,
and
G.Almouzni
(2007).
Marking histone H3 variants: how, when and why?
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Trends Biochem Sci,
32,
425-433.
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D.Ray-Gallet,
J.P.Quivy,
H.W.Silljé,
E.A.Nigg,
and
G.Almouzni
(2007).
The histone chaperone Asf1 is dispensable for direct de novo histone deposition in Xenopus egg extracts.
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Chromosoma,
116,
487-496.
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E.Bonnefoy,
G.A.Orsi,
P.Couble,
and
B.Loppin
(2007).
The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization.
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PLoS Genet,
3,
1991-2006.
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H.J.Kim,
J.H.Seol,
J.W.Han,
H.D.Youn,
and
E.J.Cho
(2007).
Histone chaperones regulate histone exchange during transcription.
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EMBO J,
26,
4467-4474.
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L.De Koning,
A.Corpet,
J.E.Haber,
and
G.Almouzni
(2007).
Histone chaperones: an escort network regulating histone traffic.
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Nat Struct Mol Biol,
14,
997.
|
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|
|
|
|
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T.Tsubota,
C.E.Berndsen,
J.A.Erkmann,
C.L.Smith,
L.Yang,
M.A.Freitas,
J.M.Denu,
and
P.D.Kaufman
(2007).
Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.
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Mol Cell,
25,
703-712.
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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
codes are
shown on the right.
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Links
