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2014 ; 111
(50
): 17827-32
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Direct interactions promote eviction of the Sir3 heterochromatin protein by the
SWI/SNF chromatin remodeling enzyme
#MMPMID25453095
Manning BJ
; Peterson CL
Proc Natl Acad Sci U S A
2014[Dec]; 111
(50
): 17827-32
PMID25453095
show ga
Heterochromatin is a specialized chromatin structure that is central to
eukaryotic transcriptional regulation and genome stability. Despite its globally
repressive role, heterochromatin must also be dynamic, allowing for its repair
and replication. In budding yeast, heterochromatin formation requires silent
information regulators (Sirs) Sir2p, Sir3p, and Sir4p, and these Sir proteins
create specialized chromatin structures at telomeres and silent mating-type loci.
Previously, we found that the SWI/SNF chromatin remodeling enzyme can catalyze
the ATP-dependent eviction of Sir3p from recombinant nucleosomal arrays, and this
activity enhances early steps of recombinational repair in vitro. Here, we show
that the ATPase subunit of SWI/SNF, Swi2p/Snf2p, interacts with the
heterochromatin structural protein Sir3p. Two interaction surfaces are defined,
including an interaction between the ATPase domain of Swi2p and the nucleosome
binding, Bromo-Adjacent-Homology domain of Sir3p. A SWI/SNF complex harboring a
Swi2p subunit that lacks this Sir3p interaction surface is unable to evict Sir3p
from nucleosomes, even though its ATPase and remodeling activities are intact. In
addition, we find that the interaction between Swi2p and Sir3p is key for SWI/SNF
to promote resistance to replication stress in vivo and for establishment of
heterochromatin at telomeres.
|*Models, Molecular
[MESH]
|Adenosine Triphosphatases/*metabolism
[MESH]
|Animals
[MESH]
|Blotting, Western
[MESH]
|Chromatin Assembly and Disassembly/*physiology
[MESH]