TY  - JOUR
A1  - Delbarre, Erwan
A1  - Ivanauskiene, Kristina
A1  - Küntziger, Thomas
A1  - Collas, Philippe
T1  - DAXX-dependent supply of soluble (H3.3-H4) dimers into PML bodies pending deposition into chromatin
Y1  - 2012/12/05 
JF  - Genome Research 
JO  - Genome Research 
DO  - 10.1101/gr.142703.112 
SP  - gr.142703.112 
UR  - http://genome.cshlp.org/content/early/2012/12/05/gr.142703.112.abstract 
N2  - Replication-independent chromatin deposition of histone variant H3.3 is mediated by several chaperones. We report a multi-step targeting of newly synthesized epitope-tagged H3.3 to chromatin via PML bodies. H3.3 is recruited to PML bodies in a DAXX--dependent manner, a process facilitated by ASF1A. DAXX is required for enrichment of ATRX, but not ASF1A or HIRA, with PML. Nonetheless, the chaperones co-localize with H3.3 at PML bodies and are found in one or more complexes with PML. Both DAXX and PML are necessary to prevent accumulation of a soluble, non-incorporated, pool of H3.3. H3.3 targeting to PML is enhanced with an (H3.3-H4)2 tetramerization mutant of H3.3, suggesting H3.3 recruitment to PML as an (H3.3-H4) dimer rather than as a tetramer. Our data support a model of DAXX-mediated recruitment of (H3.3-H4) dimers to PML bodies, which may function as triage centers for H3.3 deposition into chromatin by distinct chaperones. 
ER  -