Genome-wide identification, structural analysis, and heterologous functional inference of FvPAT10, a protein S-acyl transferase in woodland strawberry (Fragaria vesca).

backgroundProtein S-acyl transferases (PATs) mediate S-acylation, a reversible post-translational modification that attaches long-chain lipids, typically palmitate, to cysteine residues, thereby impacting protein trafficking, membrane association, stability, signaling, and stress responses in plants.

resultsThis study characterizes 22 FvPAT genes, focusing on FvPAT9 and FvPAT10 in woodland strawberry (Fragaria vesca), a diploid model species of the Rosaceae family, regarding their genomic organization, structure, and expression, with heterologous functional validation of FvPAT9 and FvPAT10. Using yeast (akr1 mutant) and Arabidopsis (atpat10 mutant) complementation, we confirmed FvPAT10 (FvH4_1g10780) restores growth in atpat10 mutants via its protein's conserved DHHC cysteine, unlike FvPAT9 (FvH4_6g14950), which complemented yeast but not Arabidopsis, revealing functional divergence. This cross-species validation uniquely elucidates FvPAT10's specificity, distinguishing it from FvPAT9 and confirming its homology to AtPAT10, implicated in cell expansion, division, vascular patterning, and fertility. Genome-wide in silico analysis identified 22 FvPAT genes across seven chromosomes. These genes were named after Arabidopsis homologs, and their proteins contained a conserved DHHC domain and predominantly localized to the endomembrane system. Phylogenetic and structural analyses highlighted diverse gene architectures, while qRT-PCR revealed tissue-specific expression, with FvPAT10 prominent in ripe fruit, suggesting a potential role in fruit development.

conclusionsThis work establishes a foundation for understanding the functions of FvPAT genes in F. vesca, providing insights for molecular breeding and a robust framework for future PAT gene studies in fruit crops.