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Identification of proteins associated with the decapping complex and the endonuclease DNE1 in Arabidopsis

ABSTRACT: In this work, we used an unbiased approach coupling immunoprecipitations (IPs) and mass spectrometry to define the interactome of the decapping activator DCP1 and the decapping enzyme DCP2. In addition we unravel the interactome of the endonuclease DNE1 harboring an endoribonuclease domain of the NYN family.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Flower Bud

SUBMITTER: Lauriane Kuhn

LAB HEAD: Damien Garcia

PROVIDER: PXD020780 | Pride | 2021-11-16

REPOSITORIES: Pride

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			Action	DRS
	2016_S24_CChicois_pAPMS_14062016_Flower-GFPbeads-CFP-HA_dil10x.mgf	Mgf
	2016_S24_CChicois_pAPMS_14062016_Flower-GFPbeads-CFP-HA_dil10x.raw	Raw
	2016_S24_CChicois_pAPMS_14062016_Flower-GFPbeads-GFP1_dil10x.mgf	Mgf
	2016_S24_CChicois_pAPMS_14062016_Flower-GFPbeads-GFP1_dil10x.raw	Raw
	2016_S24_CChicois_pAPMS_14062016_Flower-GFPbeads-GFP2_dil10x.mgf	Mgf

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The TUTase URT1 connects decapping activators and prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis

Project description:Uridylation is a widespread modification destabilizing eukaryotic mRNAs. Yet, molecular mechanisms underlying TUTase-mediated mRNA degradation remain mostly unresolved. Here, we report that the Arabidopsis TUTase URT1 participates in a molecular network connecting several translational repressors/decapping activators. URT1 directly interacts with DECAPPING 5 (DCP5), the Arabidopsis ortholog of human LSM14 and yeast Scd6, and this interaction connects URT1 to additional decay factors like DDX6/Dhh1-like RNA helicases. Nanopore direct RNA sequencing reveals a global role of URT1 in shaping poly(A) tail length, notably by preventing the accumulation of excessively deadenylated mRNAs. Based on in vitro and in planta data, we propose a model that explains how URT1 could reduce the accumulation of oligo(A)-tailed mRNAs both by favoring their degradation and because 3’ terminal uridines intrinsically hinder deadenylation. Importantly, preventing the accumulation of excessively deadenylated mRNAs avoids the biogenesis of illegitimate siRNAs that silence endogenous mRNAs and perturb Arabidopsis growth and development.

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Project description:Uridylation is a widespread modification destabilizing eukaryotic mRNAs. Yet, molecular mechanisms underlying TUTase-mediated mRNA degradation remain mostly unresolved. Here, we report that the Arabidopsis TUTase URT1 participates in a molecular network connecting several translational repressors/decapping activators including DECAPPING 5 (DCP5), the Arabidopsis ortholog of human LSM14 and yeast Scd6. A conserved Helical Leucine-rich Motif (HLM) within an intrinsically disordered region of URT1 binds to the LSm domain of DCP5. This interaction connects URT1 to additional decay factors like DDX6/Dhh1-like RNA helicases. The combination of in planta and in vitro analyses supports a model that explains how URT1 reduces the accumulation of oligo(A)-tailed mRNAs: first, by connecting decapping factors and second, because 3’ terminal uridines can intrinsically hinder deadenylation. Importantly, preventing the accumulation of excessively deadenylated mRNAs in Arabidopsis avoids the biogenesis of illegitimate siRNAs that silence endogenous mRNAs and perturb plant growth and development.

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