PMID- 25532508
OWN - NLM
STAT- MEDLINE
DCOM- 20151117
LR  - 20190806
IS  - 2041-1723 (Electronic)
IS  - 2041-1723 (Linking)
VI  - 5
DP  - 2014 Dec 23
TI  - COP1 E3 ligase protects HYL1 to retain microRNA biogenesis.
PG  - 5867
LID - 10.1038/ncomms6867 [doi]
AB  - Constitutive photomorphogenic 1 (COP1) is a RING-finger E3 ligase that plays a 
      central role in photomorphogenesis by destabilizing many light-regulated 
      transcription factors and photoreceptors. Here, we reveal a novel function for 
      COP1 E3 ligase in controlling global miRNA biogenesis in Arabidopsis thaliana. In 
      cop1 mutants, the level of miRNAs is dramatically reduced because of the 
      diminution of HYPONASTIC LEAVES 1 (HYL1), an RNA-binding protein required for 
      precise miRNA processing. HYL1 is destabilized by an unidentified protease, which 
      we tentatively call protease X, that specifically cleaves the N-terminal region 
      from HYL1, thus neutralizing its function. Our results further show that the 
      cytoplasmic partitioning of COP1 under light is essential to protect HYL1 against 
      protease X. Taken together, we suggest a novel regulatory network involving HYL1, 
      protease X, COP1 and light signalling that is indispensable for miRNA biogenesis 
      in Arabidopsis thaliana.
FAU - Cho, Seok Keun
AU  - Cho SK
AD  - Laboratory of Plant Biochemistry, Department of Plant and Environmental Sciences, 
      Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, 
      Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
FAU - Ben Chaabane, Samir
AU  - Ben Chaabane S
AD  - Laboratory of Plant Biochemistry, Department of Plant and Environmental Sciences, 
      Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, 
      Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
FAU - Shah, Pratik
AU  - Shah P
AD  - Laboratory of Plant Biochemistry, Department of Plant and Environmental Sciences, 
      Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, 
      Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
FAU - Poulsen, Christian Peter
AU  - Poulsen CP
AD  - Laboratory of Plant Biochemistry, Department of Plant and Environmental Sciences, 
      Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, 
      Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
FAU - Yang, Seong Wook
AU  - Yang SW
AD  - Laboratory of Plant Biochemistry, Department of Plant and Environmental Sciences, 
      Center for UNIK Synthetic Biology, Faculty of Science, University of Copenhagen, 
      Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20141223
PL  - England
TA  - Nat Commun
JT  - Nature communications
JID - 101528555
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (HYL1 protein, Arabidopsis)
RN  - 0 (MicroRNAs)
RN  - 0 (RNA, Plant)
RN  - 0 (RNA-Binding Proteins)
RN  - EC 2.3.2.27 (AT2G32950 protein, Arabidopsis)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 3.4.- (Peptide Hydrolases)
SB  - IM
MH  - Arabidopsis/*enzymology/genetics/metabolism/radiation effects
MH  - Arabidopsis Proteins/genetics/*metabolism
MH  - Gene Expression Regulation, Plant/radiation effects
MH  - Light
MH  - MicroRNAs/genetics/*metabolism
MH  - Peptide Hydrolases/genetics/metabolism
MH  - Plant Leaves/enzymology/genetics/metabolism/radiation effects
MH  - RNA Processing, Post-Transcriptional
MH  - RNA, Plant/genetics/*metabolism
MH  - RNA-Binding Proteins/genetics/*metabolism
MH  - Ubiquitin-Protein Ligases/genetics/*metabolism
EDAT- 2014/12/24 06:00
MHDA- 2015/11/18 06:00
CRDT- 2014/12/24 06:00
PHST- 2014/04/05 00:00 [received]
PHST- 2014/11/14 00:00 [accepted]
PHST- 2014/12/24 06:00 [entrez]
PHST- 2014/12/24 06:00 [pubmed]
PHST- 2015/11/18 06:00 [medline]
AID - ncomms6867 [pii]
AID - 10.1038/ncomms6867 [doi]
PST - epublish
SO  - Nat Commun. 2014 Dec 23;5:5867. doi: 10.1038/ncomms6867.