COP1 E3 ligase protects HYL1 to retain microrna biogenesis

Seok Keun Cho; Samir Ben Chaabane; Pratik Shah; Christian Peter Poulsen; Seong Wook Yang

doi:10.1038/ncomms6867

COP1 E3 ligase protects HYL1 to retain microrna biogenesis

Seok Keun Cho, Samir Ben Chaabane, Pratik Shah, Christian Peter Poulsen, Seong Wook Yang

Research output: Contribution to journal › Article › peer-review

83 Citations (Scopus)

Abstract

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.

Original language	English
Article number	5867
Journal	Nature communications
Volume	5
DOIs	https://doi.org/10.1038/ncomms6867
Publication status	Published - 2014

Bibliographical note

Funding Information:
This work was supported by the Center for Synthetic Biology, funded by the UNIK research initiative of the Danish Ministry of Science, Technology and Innovation (Grant 09-065274). We appreciate Thomas Günther-Pomorski for the use of fluorimeter, which is supported by Carlsbergfondet. We thank Rebecca Louise Neale and Brian Christopher King for the proof-reading of the manuscript.

Publisher Copyright:
© 2014 Macmillan Publishers Limited. All rights reserved.

All Science Journal Classification (ASJC) codes

General
Physics and Astronomy(all)
Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)

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title = "COP1 E3 ligase protects HYL1 to retain microrna biogenesis",

abstract = "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.",

author = "Cho, {Seok Keun} and Chaabane, {Samir Ben} and Pratik Shah and Poulsen, {Christian Peter} and Yang, {Seong Wook}",

note = "Funding Information: This work was supported by the Center for Synthetic Biology, funded by the UNIK research initiative of the Danish Ministry of Science, Technology and Innovation (Grant 09-065274). We appreciate Thomas G{\"u}nther-Pomorski for the use of fluorimeter, which is supported by Carlsbergfondet. We thank Rebecca Louise Neale and Brian Christopher King for the proof-reading of the manuscript. Publisher Copyright: {\textcopyright} 2014 Macmillan Publishers Limited. All rights reserved.",

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doi = "10.1038/ncomms6867",

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AU - Cho, Seok Keun

AU - Chaabane, Samir Ben

AU - Shah, Pratik

AU - Poulsen, Christian Peter

AU - Yang, Seong Wook

N1 - Funding Information: This work was supported by the Center for Synthetic Biology, funded by the UNIK research initiative of the Danish Ministry of Science, Technology and Innovation (Grant 09-065274). We appreciate Thomas Günther-Pomorski for the use of fluorimeter, which is supported by Carlsbergfondet. We thank Rebecca Louise Neale and Brian Christopher King for the proof-reading of the manuscript. Publisher Copyright: © 2014 Macmillan Publishers Limited. All rights reserved.

PY - 2014

Y1 - 2014

N2 - 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.

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.

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COP1 E3 ligase protects HYL1 to retain microrna biogenesis

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