PMID- 20651253
OWN - NLM
STAT- MEDLINE
DCOM- 20100907
LR  - 20211020
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 107
IP  - 32
DP  - 2010 Aug 10
TI  - Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in 
      replication-independent chromatin assembly at telomeres.
PG  - 14075-80
LID - 10.1073/pnas.1008850107 [doi]
AB  - The histone variant H3.3 is implicated in the formation and maintenance of 
      specialized chromatin structure in metazoan cells. H3.3-containing nucleosomes 
      are assembled in a replication-independent manner by means of dedicated chaperone 
      proteins. We previously identified the death domain associated protein (Daxx) and 
      the alpha-thalassemia X-linked mental retardation protein (ATRX) as 
      H3.3-associated proteins. Here, we report that the highly conserved N terminus of 
      Daxx interacts directly with variant-specific residues in the H3.3 core. 
      Recombinant Daxx assembles H3.3/H4 tetramers on DNA templates, and the ATRX-Daxx 
      complex catalyzes the deposition and remodeling of H3.3-containing nucleosomes. 
      We find that the ATRX-Daxx complex is bound to telomeric chromatin, and that both 
      components of this complex are required for H3.3 deposition at telomeres in 
      murine embryonic stem cells (ESCs). These data demonstrate that Daxx functions as 
      an H3.3-specific chaperone and facilitates the deposition of H3.3 at 
      heterochromatin loci in the context of the ATRX-Daxx complex.
FAU - Lewis, Peter W
AU  - Lewis PW
AD  - Laboratory of Chromatin Biology and Epigenetics, Rockefeller University, 1230 
      York Ave, New York, NY 10065, USA.
FAU - Elsaesser, Simon J
AU  - Elsaesser SJ
FAU - Noh, Kyung-Min
AU  - Noh KM
FAU - Stadler, Sonja C
AU  - Stadler SC
FAU - Allis, C David
AU  - Allis CD
LA  - eng
GR  - R37 GM053512/GM/NIGMS NIH HHS/United States
GR  - GM53512/GM/NIGMS NIH HHS/United States
GR  - GM53122/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20100722
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Carrier Proteins)
RN  - 0 (Co-Repressor Proteins)
RN  - 0 (Daxx protein, mouse)
RN  - 0 (Heterochromatin)
RN  - 0 (Histone Chaperones)
RN  - 0 (Histones)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Nucleosomes)
RN  - EC 3.6.4.- (DNA Helicases)
RN  - EC 3.6.4.12 (Atrx protein, mouse)
RN  - EC 3.6.4.12 (X-linked Nuclear Protein)
SB  - IM
MH  - Animals
MH  - Carrier Proteins/metabolism/*physiology
MH  - *Chromatin Assembly and Disassembly
MH  - Co-Repressor Proteins
MH  - DNA Helicases/*metabolism
MH  - Embryonic Stem Cells
MH  - Heterochromatin
MH  - Histone Chaperones/*metabolism
MH  - Histones/*metabolism
MH  - Intracellular Signaling Peptides and Proteins/metabolism/*physiology
MH  - Mice
MH  - Molecular Chaperones
MH  - Multiprotein Complexes
MH  - Nuclear Proteins/*metabolism/*physiology
MH  - Nucleosomes/metabolism
MH  - Protein Binding
MH  - *Telomere
MH  - X-linked Nuclear Protein
PMC - PMC2922592
COIS- The authors declare no conflict of interest.
EDAT- 2010/07/24 06:00
MHDA- 2010/09/09 06:00
PMCR- 2010/07/22
CRDT- 2010/07/24 06:00
PHST- 2010/07/24 06:00 [entrez]
PHST- 2010/07/24 06:00 [pubmed]
PHST- 2010/09/09 06:00 [medline]
PHST- 2010/07/22 00:00 [pmc-release]
AID - 1008850107 [pii]
AID - 201008850 [pii]
AID - 10.1073/pnas.1008850107 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14075-80. doi: 
      10.1073/pnas.1008850107. Epub 2010 Jul 22.