Drosha regulates gene expression independently of RNA cleavage function
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Drosha regulates gene expression independently of RNA cleavage function. / Gromak, Natalia; Dienstbier, Martin; Macias, Sara; Plass, Mireya; Eyras, Eduardo; Cáceres, Javier F.; Proudfoot, Nicholas J.
In: Cell Reports, Vol. 5, No. 6, 2013, p. 1499-510.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Drosha regulates gene expression independently of RNA cleavage function
AU - Gromak, Natalia
AU - Dienstbier, Martin
AU - Macias, Sara
AU - Plass, Mireya
AU - Eyras, Eduardo
AU - Cáceres, Javier F.
AU - Proudfoot, Nicholas J.
N1 - Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved.
PY - 2013
Y1 - 2013
N2 - Drosha is the main RNase III-like enzyme involved in the process of microRNA (miRNA) biogenesis in the nucleus. Using whole-genome ChIP-on-chip analysis, we demonstrate that, in addition to miRNA sequences, Drosha specifically binds promoter-proximal regions of many human genes in a transcription-dependent manner. This binding is not associated with miRNA production or RNA cleavage. Drosha knockdown in HeLa cells downregulated nascent gene transcription, resulting in a reduction of polyadenylated mRNA produced from these gene regions. Furthermore, we show that this function of Drosha is dependent on its N-terminal protein-interaction domain, which associates with the RNA-binding protein CBP80 and RNA Polymerase II. Consequently, we uncover a previously unsuspected RNA cleavage-independent function of Drosha in the regulation of human gene expression.
AB - Drosha is the main RNase III-like enzyme involved in the process of microRNA (miRNA) biogenesis in the nucleus. Using whole-genome ChIP-on-chip analysis, we demonstrate that, in addition to miRNA sequences, Drosha specifically binds promoter-proximal regions of many human genes in a transcription-dependent manner. This binding is not associated with miRNA production or RNA cleavage. Drosha knockdown in HeLa cells downregulated nascent gene transcription, resulting in a reduction of polyadenylated mRNA produced from these gene regions. Furthermore, we show that this function of Drosha is dependent on its N-terminal protein-interaction domain, which associates with the RNA-binding protein CBP80 and RNA Polymerase II. Consequently, we uncover a previously unsuspected RNA cleavage-independent function of Drosha in the regulation of human gene expression.
U2 - 10.1016/j.celrep.2013.11.032
DO - 10.1016/j.celrep.2013.11.032
M3 - Journal article
C2 - 24360955
VL - 5
SP - 1499
EP - 1510
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 6
ER -
ID: 106792465