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Quantitative proteomic comparison between wild type Col and acinus-2 pinin-1 mutant using 15N metabolic labeling

ABSTRACT: ACINUS and PININ genes regulate transcription and alternative splicing (Bi et al., 2021) and we hypothesize that some proteins should have altered expression in the double mutant. Therefore, MS experiments were designed to identify these altered proteins on a global scale using 15N metabolic labeling.

INSTRUMENT(S): Q Exactive HF

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

TISSUE(S): Plant Cell, Whole Body

SUBMITTER: Shouling Xu

LAB HEAD: Shouling Xu

PROVIDER: PXD030081 | Pride | 2022-02-04

REPOSITORIES: Pride

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			Action	DRS
	Description_of_raw_data.xlsx	Xlsx
	F1_Col-ap_Fw_Protein_Quan_PRIDE.xlsx	Xlsx
	Q20200310_03.pep.xml	Pepxml
	Q20200310_03.raw	Raw
	Q20200310_04.pep.xml	Pepxml

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Project description:AtACINUS protein is involved in regulation of alternative transcription and splicing(AS). Identifying interaction partners and protein complex compositions for AtACINUS can produce valuable information on the mechanisms by which they regulate transcription and AS, as well as post-translational modifications on AtACINUS. A homozygous 35S::AtACINUS-GFP/acinus-2 plant was selected for similar protein expression level to the endogenous AtACINUS protein of wild-type plants using a native α-AtACINUS antibody. We isolated putative AtACINUS interaction partners from young Arabidopsis seedlings using the native α-AtACINUS antibody. Plants expressing TAP-GFP under 35S promoter were used as controls.

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Using targeted quantification (PRM) to quantify proteins between wild type Col and acinus-2 pinin-1 mutant with 15N metabolic labeling

Project description:ACINUS and PININ genes regulate transcription and alternative splicing (Bi et al., 2021) and we hypothesize that some proteins should have altered expression in the double mutant. Therefore, MS experiments were designed to identify these altered proteins on a global scale using 15N metabolic labeling. Some of these altered proteins were subjected to targeted quantification.

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SPY mediates O-fucose modification of hundreds of proteins and sugar-dependent growth in Arabidopsis_(Part 2: EtHCD)

Project description:The recent discovery of SPY-catalyzed protein O-fucosylation reveals a novel mechanism for regulating nucleocytoplasmic protein functions in plants. Genetic evidence indicates important roles of SPY in diverse developmental and physiological processes, however, the upstream signal controlling SPY activity and the downstream substrate proteins O-fucosylated by SPY remain largely unknown. Here, we demonstrate that SPY mediates sugar-dependent growth. We further identify hundreds of O-fucosylated proteins using lectin affinity chromatography followed by mass spectrometry. All the O-fucosylation events quantified in proteomic analyses are undetectable or decreased in the spy mutants and thus likely catalyzed by SPY. The O-fucosylome includes mostly nuclear and cytosolic proteins. Many O-fucosylated proteins function in essential cellular processes, hormone signaling, and developmental programs, consistent with the genetic functions of SPY. The O-fucosylome also includes many proteins modified by O-linked-N-acetylglucosamine (O-GlcNAc) and by phosphorylation downstream of the target of rapamycin (TOR) kinase, revealing the convergence of these nutrient signaling pathways on key regulatory functions such as post-transcriptional/translational regulation and hormonal responses. Our study identifies numerous targets of SPY/O-fucosylation and potential nodes of crosstalk among sugar/nutrient signaling pathways, enabling future dissection of the signaling network that mediates sugar regulation of plant growth and development.

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