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==Publications== {{medline-entry |title=The dependence of leaf senescence on the balance between 1-aminocyclopropane-1-carboxylate acid synthase 1 (ACS1)-catalysed ACC generation and nitric oxide-associated 1 (NOS1)-dependent NO accumulation in Arabidopsis. |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/30734982 |abstract=Ethylene and nitric oxide (NO) act as endogenous regulators during leaf senescence. Levels of ethylene or its precursor 1-aminocyclopropane-1-carboxylate acid (ACC) depend on the activity of ACC synthases (ACS), and NO production is controlled by NO-associated 1 ([[NOA1]]). However, the integration mechanisms of ACS and [[NOA1]] activity still need to be explored during leaf senescence. Here, using experimental techniques, such as physiological and molecular detection, liquid chromatography-tandem mass spectrometry and fluorescence measurement, we investigated the relevant mechanisms. Our observations showed that the loss-of-function acs1-1 mutant ameliorated age- or dark-induced leaf senescence syndrome, such as yellowing and loss of chlorophyll, that acs1-1 reduced ACC accumulation mainly in mature leaves and that acs1-1-promoted [[NOA1]] expression and NO accumulation mainly in juvenile leaves, when compared with the wild type (WT). But the leaf senescence promoted by the NO-deficient noa1 mutant was not involved in ACS1 expression. There was a similar sharp reduction of ACS1 and [[NOA1]] expression with the increase in WT leaf age, and this inflection point appeared in mature leaves and coincided with the onset of leaf senescence. These findings suggest that [[NOA1]]-dependent NO accumulation blocked the ACS1-induced onset of leaf senescence, and that ACS1 activity corresponds to the onset of leaf senescence in Arabidopsis. |mesh-terms=* Amino Acids, Cyclic * Arabidopsis * Arabidopsis Proteins * Chlorophyll * Glucuronidase * Lyases * Nitric Oxide * Nitric Oxide Synthase * Plant Leaves * Transcriptome |keywords=* ACC * NO * ACS1 * NOA1 * leaf senescence |full-text-url=https://sci-hub.do/10.1111/plb.12970 }} {{medline-entry |title=Low concentrations of salicylic acid delay methyl jasmonate-induced leaf senescence by up-regulating nitric oxide synthase activity. |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27440938 |abstract=In plants, extensive efforts have been devoted to understanding the crosstalk between salicylic acid (SA) and jasmonic acid (JA) signaling in pathogen defenses, but this crosstalk has scarcely been addressed during senescence. In this study, the effect of SA application on methyl jasmonate (MeJA)-induced leaf senescence was assessed. We found that low concentrations of SA (1-50 μM) played a delayed role against the senescence promoted by MeJA. Furthermore, low concentrations of SA enhanced plant antioxidant defenses and restricted reactive oxygen species (ROS) accumulation in MeJA-treated leaves. When applied simultaneously with MeJA, low concentrations of SA triggered a nitric oxide (NO) burst, and the elevated NO levels were linked to the nitric oxide associated 1 ([[NOA1]])-dependent pathway via nitric oxide synthase (NOS) activity. The ability of SA to up-regulate plant antioxidant defenses, reduce ROS accumulation, and suppress leaf senescence was lost in NO-deficient Atnoa1 plants. In a converse manner, exogenous addition of NO donors increased the plant antioxidant capacity and lowered the ROS levels in MeJA-treated leaves. Taken together, the results indicate that SA at low concentrations counteracts MeJA-induced leaf senescence through [[NOA1]]-dependent NO signaling and strengthening of the antioxidant defense. |mesh-terms=* Acetates * Aging * Arabidopsis * Chlorophyll * Cyclopentanes * Lipid Peroxidation * Nitric Oxide Synthase * Oxylipins * Plant Growth Regulators * Plant Leaves * Real-Time Polymerase Chain Reaction * Salicylic Acid * Up-Regulation |keywords=* Jasmonic acid * leaf senescence * nitric oxide * nitric oxide synthase * reactive oxygen species * salicylic acid. |full-text-url=https://sci-hub.do/10.1093/jxb/erw280 }} {{medline-entry |title=Two homologous protein S-acyltransferases, PAT13 and PAT14, cooperatively regulate leaf senescence in Arabidopsis. |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/26160582 |abstract=Lipid modification on the cysteine residues of proteins, known as S-palmitoylation or S-acylation, regulates the subcellular localization and the function of proteins. S-acylation is catalysed by a group of protein acyltransferases (PATs) with a conserved Asp-His-His-Cys (DHHC) motif. The molecular function of S-acylation has been studied in details in yeast and mammalian cells, but its role in plant cells remains unclear. Here it is reported that the expression of two homologous protein acyltransferases- PAT13 and PAT14 -was moderately increased in the older leaves of Arabidopsis. The double mutant of PAT13 and PAT14 displayed a severely early leaf senescence phenotype. The phenotype was complemented by PAT13 or PAT14 overexpression in the double mutant, confirming the roles of PAT13 and PAT14 in this process. Furthermore, the levels of reactive oxygen species (ROS) and cell death were dramatically induced in the double mutant. To investigate the molecular functions of PAT13 and PAT14, their potential S-acylation substrates were predicted by bioinformatics methods. The subcellular localization and S-acylation of a candidate substrate NITRIC OXIDE ASSOCIATED 1 ([[NOA1]]), which also plays a role in leaf senescence control, were partially disrupted in the protoplasts of the double mutant. Impairment of S-acylation on [[NOA1]] affected its subcellular localization and its function in leaf senescence regulation. Conclusively, protein S-acyltransferases PAT13 and PAT14 are involved in leaf senescence control- possibly via [[NOA1]] S-acylation-, providing a new sight into the regulation mechanism of S-acylation in leaf senescence. |mesh-terms=* Acyltransferases * Arabidopsis * Arabidopsis Proteins * Gene Expression Regulation, Developmental * Gene Expression Regulation, Plant * Nitric Oxide Synthase * Plant Leaves |keywords=* Arabidopsis thaliana * S-acylation * S-acyltransferase. * S-palmitoylation * leaf senescence * protein modification * subcellular localization |full-text-url=https://sci-hub.do/10.1093/jxb/erv347 }}
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