Both male and female gametogenesis require a fully functional protein S-acyl transferase 21 in Arabidopsis thaliana

The Plant Journal : for Cell and Molecular Biology
Yaxiao LiBaoxiu Qi

Abstract

S-Acylation is a reversible post-translational lipid modification in which a long chain fatty acid covalently attaches to specific cysteine(s) of proteins via a thioester bond. It enhances the hydrophobicity of proteins, contributes to their membrane association and plays roles in protein trafficking, stability and signalling. A family of Protein S-Acyl Transferases (PATs) is responsible for this reaction. PATs are multi-pass transmembrane proteins that possess a catalytic Asp-His-His-Cys cysteine-rich domain (DHHC-CRD). In Arabidopsis, there are currently 24 such PATs, five having been characterized, revealing their important roles in growth, development, senescence and stress responses. Here, we report the functional characterization of another PAT, AtPAT21, demonstrating the roles it plays in Arabidopsis sexual reproduction. Loss-of-function mutation by T-DNA insertion in AtPAT21 results in the complete failure of seed production. Detailed studies revealed that the sterility of the mutant is caused by defects in both male and female sporogenesis and gametogenesis. To determine if the sterility observed in atpat21-1 was caused by upstream defects in meiosis, we assessed meiotic progression in pollen mother cells and found mas...Continue Reading

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Citations

Apr 3, 2020·Biochemical Society Transactions·Piers A Hemsley
May 14, 2021·Nature Communications·Dongqin ChenGary Stacey

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