SERRATE interacts with the nuclear exosome targeting complex to degrade primary miRNA precursors in Arabidopsis
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)
TISSUE(S): Flower
SUBMITTER: 
Lauriane Kuhn
LAB HEAD: Heike Lange
PROVIDER: PXD014447 | Pride | 2020-04-15
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| 2017_S34_HLange_ColO-1-dil.mgf | Mgf | |||
| 2017_S34_HLange_ColO-1-dil.raw | Raw | |||
| 2017_S34_HLange_ColO-2-dil.mgf | Mgf | |||
| 2017_S34_HLange_ColO-2-dil.raw | Raw | |||
| 2017_S34_HLange_ColO-rep1-dil.mgf | Mgf |
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Publications
SERRATE interacts with the nuclear exosome targeting (NEXT) complex to degrade primary miRNA precursors in Arabidopsis.
Bajczyk Mateusz M Lange Heike H Bielewicz Dawid D Szewc Lukasz L Bhat Susheel S SS Dolata Jakub J Kuhn Lauriane L Szweykowska-Kulinska Zofia Z Gagliardi Dominique D Jarmolowski Artur A
Nucleic acids research 20200701 12
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 id ...[more]
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