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A Golgi and tonoplast localized S-acyl transferase is involved in cell expansion, cell division, vascular patterning and fertility in Arabidopsis

Qi, B, Doughty, J and Hooley, R (2013) A Golgi and tonoplast localized S-acyl transferase is involved in cell expansion, cell division, vascular patterning and fertility in Arabidopsis. New Phytologist, 200 (2). pp. 444-456. ISSN 0028-646X

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Abstract

S‐acylation of eukaryotic proteins is the reversible attachment of palmitic or stearic acid to cysteine residues, catalysed by protein S‐acyl transferases that share an Asp‐His‐His‐Cys (DHHC) motif. Previous evidence suggests that in Arabidopsis S‐acylation is involved in the control of cell size, polarity and the growth of pollen tubes and root hairs.
Using a combination of yeast genetics, biochemistry, cell biology and loss of function genetics the roles of a member of the protein S‐acyl transferase PAT family, AtPAT10 (At3g51390), have been explored.
In keeping with its role as a PAT, AtPAT10 auto‐S‐acylates, and partially complements the yeast akr1 PAT mutant, and this requires Cys192 of the DHHC motif. In Arabidopsis AtPAT10 is localized in the Golgi stack, trans‐Golgi network/early endosome and tonoplast. Loss‐of‐function mutants have a pleiotropic phenotype involving cell expansion and division, vascular patterning, and fertility that is rescued by wild‐type AtPAT10 but not by catalytically inactive AtPAT10C192A. This supports the hypothesis that AtPAT10 is functionally independent of the other Arabidopsis PATs.
Our findings demonstrate a growing importance of protein S‐acylation in plants, and reveal a Golgi and tonoplast located S‐acylation mechanism that affects a range of events during growth and development in Arabidopsis.

Item Type: Article
Uncontrolled Keywords: 06 Biological Sciences, 07 Agricultural and Veterinary Sciences
Subjects: R Medicine > RM Therapeutics. Pharmacology
R Medicine > RS Pharmacy and materia medica
Divisions: Pharmacy & Biomolecular Sciences
Publisher: Wiley
Related URLs:
Date Deposited: 06 Mar 2020 11:23
Last Modified: 06 Mar 2020 11:30
DOI or Identification number: 10.1111/nph.12385
URI: http://researchonline.ljmu.ac.uk/id/eprint/12417

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