title: Protein S-Acyltransferase 14: A Specific Role for Palmitoylation in Leaf Senescence in Arabidopsis.
abstract: The Asp-His-His-Cys-Cys-rich domain-containing Protein S-Acyl Transferases (PATs) are multipass transmembrane proteins that catalyze S-acylation (commonly known as S-palmitoylation), the reversible posttranslational lipid modification of proteins. Palmitoylation enhances the hydrophobicity of proteins, contributes to their membrane association, and plays roles in protein trafficking and signaling. In Arabidopsis (Arabidopsis thaliana), there are at least 24 PATs; previous studies on two PATs established important roles in growth, development, and stress responses. In this study, we identified a, to our knowledge, novel PAT, AtPAT14, in Arabidopsis. Complementation studies in yeast (Saccharomyces cerevisiae) and Arabidopsis demonstrate that AtPAT14 possesses PAT enzyme activity. Disruption of AtPAT14 by T-DNA insertion resulted in an accelerated senescence phenotype. This coincided with increased transcript levels of some senescence-specific and pathogen-resistant marker genes. We show that early senescence of pat14 does not involve the signaling molecules jasmonic acid and abscisic acid, or autophagy, but associates with salicylic acid homeostasis and signaling. This strongly suggests that AtPAT14 plays a pivotal role in regulating senescence via salicylic acid pathways. Senescence is a complex process required for normal plant growth and development and requires the coordination of many genes and signaling pathways. However, precocious senescence results in loss of biomass and seed production. The negative regulation of leaf senescence by AtPAT14 in Arabidopsis highlights, to our knowledge for the first time, a specific role for palmitoylation in leaf senescence.
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom (Y.L., R.S., J.D., B.Q.); andCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, United Kingdom (M.G.).
authors.forename: Yaxiao
authors.initials: Y
authors.lastname: Li
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom (Y.L., R.S., J.D., B.Q.); andCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, United Kingdom (M.G.).
authors.forename: Rod
authors.initials: R
authors.lastname: Scott
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom (Y.L., R.S., J.D., B.Q.); andCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, United Kingdom (M.G.).
authors.forename: James
authors.initials: J
authors.lastname: Doughty
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom (Y.L., R.S., J.D., B.Q.); andCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, United Kingdom (M.G.).
authors.forename: Murray
authors.initials: M
authors.lastname: Grant
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom (Y.L., R.S., J.D., B.Q.); andCollege of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, United Kingdom (M.G.) bssbq@bath.ac.uk.
authors.forename: Baoxiu
authors.identifier: http://orcid.org/0000-0002-9425-935X
authors.initials: B
authors.lastname: Qi
mesh_terms: D000040:Abscisic Acid / Q000378:metabolism / Q000494:pharmacology; D000217:Acyltransferases / Q000235:genetics / Q000378:metabolism*; D017360:Arabidopsis / Q000187:drug effects / Q000254:growth & development / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001343:Autophagy / Q000502:physiology; D003517:Cyclopentanes / Q000378:metabolism / Q000494:pharmacology; D018506:Gene Expression Regulation, Plant; D055786:Gene Knockout Techniques; D006056:Golgi Apparatus / Q000378:metabolism; D054878:Lipoylation; D009154:Mutation; D054883:Oxylipins / Q000378:metabolism / Q000494:pharmacology; D018515:Plant Leaves / Q000502:physiology*; D030821:Plants, Genetically Modified; D020156:Salicylic Acid / Q000378:metabolism / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; D003517:Cyclopentanes; D054883:Oxylipins; C011006:jasmonic acid; D000040:Abscisic Acid; D000217:Acyltransferases; C000609136:PAT14 protein, Arabidopsis; D020156:Salicylic Acid