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2014 ; 33
(12
): 1397-415
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English Wikipedia
Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase
II-coupled nucleosome recycling
#MMPMID24843044
Rossetto D
; Cramet M
; Wang AY
; Steunou AL
; Lacoste N
; Schulze JM
; Côté V
; Monnet-Saksouk J
; Piquet S
; Nourani A
; Kobor MS
; Côté J
EMBO J
2014[Jun]; 33
(12
): 1397-415
PMID24843044
show ga
The NuA4 histone acetyltransferase complex is required for gene regulation, cell
cycle progression, and DNA repair. Dissection of the 13-subunit complex reveals
that the Eaf7 subunit bridges Eaf5 with Eaf3, a H3K36me3-binding chromodomain
protein, and this Eaf5/7/3 trimer is anchored to NuA4 through Eaf5. This trimeric
subcomplex represents a functional module, and a large portion exists in a native
form outside the NuA4 complex. Gene-specific and genome-wide location analyses
indicate that Eaf5/7/3 correlates with transcription activity and is enriched
over the coding region. In agreement with a role in transcription elongation, the
Eaf5/7/3 trimer interacts with phosphorylated RNA polymerase II and helps its
progression. Loss of Eaf5/7/3 partially suppresses intragenic cryptic
transcription arising in set2 mutants, supporting a role in nucleosome
destabilization. On the other hand, loss of the trimer leads to an increase of
replication-independent histone exchange over the coding region of transcribed
genes. Taken together, these results lead to a model where Eaf5/7/3 associates
with elongating polymerase to promote the disruption of nucleosomes in its path,
but also their refolding in its wake.