Quantitative proteomics reveals extensive lysine ubiquitination and transcription factor stability states in Arabidopsis.

ABSTRACT: Protein activity, abundance, and stability can be regulated by post-translational modification including ubiquitination. Ubiquitination is conserved among eukaryotes and plays a central role in modulating cellular function; yet, we lack comprehensive catalogs of proteins that are modified by ubiquitin in plants. In this study, we describe an antibody-based approach to enrich ubiquitinated peptides coupled with isobaric labeling to enable quantification of up to 18-multiplexed samples. This approach identified 17,940 ubiquitinated lysine sites arising from 6,453 proteins from Arabidopsis (Arabidopsis thaliana) primary roots, seedlings, and rosette leaves. Gene ontology analysis indicated that ubiquitinated proteins are associated with numerous biological processes including hormone signalin

SUBMITTER: Song G 

PROVIDER: S-EPMC11663597 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature