Meta-Analysis of Rice Phosphoproteomics Data to Understand Variation in Cell Signaling Across the Rice Pan-Genome.

Publication Title

Journal of proteome research

Document Type

Article

Publication Date

7-5-2024

Keywords

washington; isb; Oryza; Proteomics; Phosphoproteins; Plant Proteins; Genome, Plant; Signal Transduction; Phosphorylation; Protein Processing, Post-Translational; Phosphopeptides; Databases, Protein; Amino Acid Motifs; Mass Spectrometry

Abstract

Phosphorylation is the most studied post-translational modification, and has multiple biological functions. In this study, we have reanalyzed publicly available mass spectrometry proteomics data sets enriched for phosphopeptides from Asian rice (Oryza sativa). In total we identified 15,565 phosphosites on serine, threonine, and tyrosine residues on rice proteins. We identified sequence motifs for phosphosites, and link motifs to enrichment of different biological processes, indicating different downstream regulation likely caused by different kinase groups. We cross-referenced phosphosites against the rice 3,000 genomes, to identify single amino acid variations (SAAVs) within or proximal to phosphosites that could cause loss of a site in a given rice variety and clustered the data to identify groups of sites with similar patterns across rice family groups. The data has been loaded into UniProt Knowledge-Base-enabling researchers to visualize sites alongside other data on rice proteins, e.g., structural models from AlphaFold2, PeptideAtlas, and the PRIDE database-enabling visualization of source evidence, including scores and supporting mass spectra.

Specialty

Institute for Systems Biology

DOI

10.1021/acs.jproteome.4c00187

Link to Full Text

PSJH Full Text

Share

COinS