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PDBsum entry 5ejo
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Nuclear protein
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PDB id
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5ejo
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PDB id:
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| Name: |
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Nuclear protein
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Title:
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Crystal structure of the winged helix domain in chromatin assembly factor 1 subunit p90
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Structure:
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Chromatin assembly factor 1 subunit p90. Chain: a. Fragment: unp residues 519-606. Synonym: caf-1 90 kda subunit,rap1 localization factor 2. Engineered: yes
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Source:
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Saccharomyces cerevisiae s288c. Baker's yeast. Organism_taxid: 559292. Strain: s288c. Gene: rlf2, cac1, ypr018w, yp9531.12. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.75Å
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R-factor:
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0.200
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R-free:
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0.230
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Authors:
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K.Zhang,Y.Gao,J.Li,R.Burgess,J.Han,H.Liang,Z.Zhang,Y.Liu
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Key ref:
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K.Zhang
et al.
(2016).
A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks.
Nucleic Acids Res,
44,
5083-5094.
PubMed id:
DOI:
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Date:
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02-Nov-15
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Release date:
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16-Mar-16
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PROCHECK
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Headers
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References
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Q12495
(RLF2_YEAST) -
Chromatin assembly factor 1 subunit A from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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606 a.a.
79 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Nucleic Acids Res
44:5083-5094
(2016)
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PubMed id:
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A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks.
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K.Zhang,
Y.Gao,
J.Li,
R.Burgess,
J.Han,
H.Liang,
Z.Zhang,
Y.Liu.
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ABSTRACT
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Chromatin assembly factor 1 (CAF-1) is a histone H3-H4 chaperone that deposits
newly synthesized histone (H3-H4)2 tetramers during replication-coupled
nucleosome assembly. However, how CAF-1 functions in this process is not yet
well understood. Here, we report the crystal structure of C terminus of Cac1
(Cac1C), a subunit of yeast CAF-1, and the function of this domain in
stabilizing CAF-1 at replication forks. We show that Cac1C forms a winged helix
domain (WHD) and binds DNA in a sequence-independent manner. Mutations in Cac1C
that abolish DNA binding result in defects in transcriptional silencing and
increased sensitivity to DNA damaging agents, and these defects are exacerbated
when combined with Cac1 mutations deficient in PCNA binding. Similar phenotypes
are observed for corresponding mutations in mouse CAF-1. These results reveal a
mechanism conserved in eukaryotic cells whereby the ability of CAF-1 to bind DNA
is important for its association with the DNA replication forks and subsequent
nucleosome assembly.
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Links
