SERRATE interacts with the nuclear exosome targeting (NEXT) complex to degrade primary miRNA precursors in Arabidopsis
Open Access
- 9 July 2020
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 48 (12), 6839-6854
- https://doi.org/10.1093/nar/gkaa373
Abstract
SERRATE/ARS2 is a conserved RNA effector protein involved in transcription, processing and export of different types of RNAs. In Arabidopsis, the best-studied function of SERRATE (SE) is to promote miRNA processing. Here, we report that SE interacts with the nuclear exosome targeting (NEXT) complex, comprising the RNA helicase HEN2, the RNA binding protein RBM7 and one of the two zinc-knuckle proteins ZCCHC8A/ZCCHC8B. The identification of common targets of SE and HEN2 by RNA-seq supports the idea that SE cooperates with NEXT for RNA surveillance by the nuclear exosome. Among the RNA targets accumulating in absence of SE or NEXT are miRNA precursors. Loss of NEXT components results in the accumulation of pri-miRNAs without affecting levels of miRNAs, indicating that NEXT is, unlike SE, not required for miRNA processing. As compared to se-2, se-2 hen2-2 double mutants showed increased accumulation of pri-miRNAs, but partially restored levels of mature miRNAs and attenuated developmental defects. We propose that the slow degradation of pri-miRNAs caused by loss of HEN2 compensates for the poor miRNA processing efficiency in se-2 mutants, and that SE regulates miRNA biogenesis through its double contribution in promoting miRNA processing but also pri-miRNA degradation through the recruitment of the NEXT complex.Funding Information
- National Science Centre (UMO-2014/13/N/NZ1/00049, UMO-2018/28/T/NZ1/00392, UMO-2013/10/NZ1/00557, UMO-2016/23/D/NZ1/00152)
- Centre National de la Recherche Scientifique
- Agence Nationale de la Recherche (ANR-17-EURE-0023,, ANR-10-LABX-0036_NETRNA)
- Adam Mickiewicz University
This publication has 73 references indexed in Scilit:
- mirEX: a platform for comparative exploration of plant pri-miRNA expression dataNucleic Acids Research, 2011
- Putative Arabidopsis THO/TREX mRNA export complex is involved in transgene and endogenous siRNA biosynthesisProceedings of the National Academy of Sciences, 2010
- BEDTools: a flexible suite of utilities for comparing genomic featuresBioinformatics, 2010
- Ars2 Links the Nuclear Cap-Binding Complex to RNA Interference and Cell ProliferationCell, 2009
- The RNA-binding proteins HYL1 and SE promote accurate in vitro processing of pri-miRNA by DCL1Proceedings of the National Academy of Sciences, 2008
- Dual roles of the nuclear cap-binding complex and SERRATE in pre-mRNA splicing and microRNA processing in Arabidopsis thalianaProceedings of the National Academy of Sciences, 2008
- Identification of Nuclear Dicing Bodies Containing Proteins for MicroRNA Biogenesis in Living Arabidopsis PlantsCurrent Biology, 2007
- SERRATE: a new player on the plant microRNA sceneEMBO Reports, 2006
- SERRATE coordinates shoot meristem function and leaf axial patterning in ArabidopsisNature, 2005
- Expression of Arabidopsis MIRNA GenesPlant Physiology, 2005