Abstract
Argonaute (AGO) proteins have a well-established role in post-transcriptional regulation of gene expression as key component of the RNA silencing pathways. Recent evidence involves AGO proteins in mammalian nuclear processes such as transcription and splicing, though the mechanistic aspects of AGO nuclear functions remain largely elusive. Here, by SILAC-based interaction proteomics, we identify the chromatin-remodelling complex SWI/SNF as a novel AGO2 interactor in human cells. Moreover, we show that nuclear AGO2 is loaded with a novel class of Dicer-dependent short RNAs (sRNAs), that we called swiRNAs, which map nearby the Transcription Start Sites (TSSs) bound by SWI/SNF. The knockdown of AGO2 decreases nucleosome occupancy at the first nucleosome located downstream of TSSs in a swiRNA-dependent manner. Our findings indicate that in human cells AGO2 binds SWI/SNF and a novel class of sRNAs to establish nucleosome occupancy on target TSSs.
| Original language | English |
|---|---|
| Pages (from-to) | 1498-1512 |
| Number of pages | 15 |
| Journal | Nucleic Acids Research |
| Volume | 43 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2015 |
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- Genetics
Cite this
ARGONAUTE2 cooperates with SWI/SNF complex to determine nucleosome occupancy at human Transcription Start Sites. / Carissimi, Claudia; Laudadio, Ilaria; Cipolletta, Emanuela; Gioiosa, Silvia; Mihailovich, Marija; Bonaldi, Tiziana; Macino, Giuseppe; Fulci, Valerio.
In: Nucleic Acids Research, Vol. 43, No. 3, 2015, p. 1498-1512.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ARGONAUTE2 cooperates with SWI/SNF complex to determine nucleosome occupancy at human Transcription Start Sites
AU - Carissimi, Claudia
AU - Laudadio, Ilaria
AU - Cipolletta, Emanuela
AU - Gioiosa, Silvia
AU - Mihailovich, Marija
AU - Bonaldi, Tiziana
AU - Macino, Giuseppe
AU - Fulci, Valerio
PY - 2015
Y1 - 2015
N2 - Argonaute (AGO) proteins have a well-established role in post-transcriptional regulation of gene expression as key component of the RNA silencing pathways. Recent evidence involves AGO proteins in mammalian nuclear processes such as transcription and splicing, though the mechanistic aspects of AGO nuclear functions remain largely elusive. Here, by SILAC-based interaction proteomics, we identify the chromatin-remodelling complex SWI/SNF as a novel AGO2 interactor in human cells. Moreover, we show that nuclear AGO2 is loaded with a novel class of Dicer-dependent short RNAs (sRNAs), that we called swiRNAs, which map nearby the Transcription Start Sites (TSSs) bound by SWI/SNF. The knockdown of AGO2 decreases nucleosome occupancy at the first nucleosome located downstream of TSSs in a swiRNA-dependent manner. Our findings indicate that in human cells AGO2 binds SWI/SNF and a novel class of sRNAs to establish nucleosome occupancy on target TSSs.
AB - Argonaute (AGO) proteins have a well-established role in post-transcriptional regulation of gene expression as key component of the RNA silencing pathways. Recent evidence involves AGO proteins in mammalian nuclear processes such as transcription and splicing, though the mechanistic aspects of AGO nuclear functions remain largely elusive. Here, by SILAC-based interaction proteomics, we identify the chromatin-remodelling complex SWI/SNF as a novel AGO2 interactor in human cells. Moreover, we show that nuclear AGO2 is loaded with a novel class of Dicer-dependent short RNAs (sRNAs), that we called swiRNAs, which map nearby the Transcription Start Sites (TSSs) bound by SWI/SNF. The knockdown of AGO2 decreases nucleosome occupancy at the first nucleosome located downstream of TSSs in a swiRNA-dependent manner. Our findings indicate that in human cells AGO2 binds SWI/SNF and a novel class of sRNAs to establish nucleosome occupancy on target TSSs.
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UR - http://www.scopus.com/inward/citedby.url?scp=84930859040&partnerID=8YFLogxK
U2 - 10.1093/nar/gku1387
DO - 10.1093/nar/gku1387
M3 - Article
C2 - 25605800
AN - SCOPUS:84930859040
VL - 43
SP - 1498
EP - 1512
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 3
ER -