Two homologous protein S-acyltransferases, PAT13 and PAT14, cooperatively regulate leaf senescence in Arabidopsis
© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
| Veröffentlicht in: | Journal of experimental botany. - 1985. - 66(2015), 20 vom: 10. Okt., Seite 6345-53 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2015
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| Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana S-acylation S-acyltransferase. S-palmitoylation leaf senescence protein modification subcellular localization Arabidopsis Proteins mehr... |
| Zusammenfassung: | © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. 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 |
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| Beschreibung: | Date Completed 19.07.2016 Date Revised 01.10.2015 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1460-2431 |
| DOI: | 10.1093/jxb/erv347 |