Proteomics

Dataset Information

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Impact of alternative splicing on Arabidopsis proteome (Part II, TMT MS2, batch I)


ABSTRACT: Alternative splicing (AS) is an important regulatory process in eukaryotes and, in plants, is influenced by various stressors and developmental stages. Despite its significance, the impact of AS on proteome diversity in plants has not been fully explored. To address this gap, we investigated isoform-specific peptides in wild-type (WT) plants and acinus pinin double mutants. ACINUS and PININ are evolutionarily conserved splicing factors, and their disruption induces splicing events resembling those triggered by diverse abiotic and biotic stressors. We generated extensively fractionated samples from a pooled peptide mix containing five replicates each of WT and acinus pinin, labeled with TMT11. This dataset was integrated with additional data generated using the alternative protease AspN, as well as mined data from the Arabidopsis Proteome Draft (Mergner et al., 2020, Nature), to enhance isoform-specific peptide detection. Using in-house algorithms and tailored filtering steps, this approach enabled identification of isoform-specific peptides, both annotated and previously unannotated. Our findings demonstrate that alternative splicing contributes substantially to proteome diversity in plants.

INSTRUMENT(S):

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

TISSUE(S): Whole Body

SUBMITTER: Shouling Xu  

LAB HEAD: Shouling Xu

PROVIDER: PXD068589 | Pride | 2026-06-08

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MSFragger_protein.tsv Tabular
ProteinProspector_protein.txt Txt
Q20230117_01.raw Raw
Q20230117_02.raw Raw
Q20230117_03.raw Raw
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Publications

Impact of alternative splicing on Arabidopsis proteome.

Reyes Andres V AV   Zhang Christopher C   Karunadasa Sumudu S SS   Shrestha Ruben R   Grismer TaraBryn S TS   Byun Danbi D   Xu Shou-Ling SL  

Nucleic acids research 20260401 8


Limited proteomic evidence makes it unclear to what extent alternative splicing (AS) isoforms are translated and functionally relevant in eukaryotes. Here, we present a comprehensive proteomic analysis in plants using large-scale data mining, extensive fractionation of AspN- and trypsin-digested proteomes, and both label-free and TMT labeling. In total, we identified 471 196 peptides from 22 479 proteins by searching against Araport11, revealing 32 110 isoform-specific peptides. Using an integra  ...[more]

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