S-acylation is a common yet poorly understood fatty acid-based post-translational modification of proteins in all eukaryotes, including plants. While exact roles for S-acylation in protein function are largely unknown the reversibility of S-acylation indicates that it is likely able to play a regulatory role. As more studies reveal the roles of S-acylation within the cell it is becoming apparent that how S-acylation affects proteins is conceptually different from other reversible modifications such as phosphorylation or ubiquitination; a new mind-set is therefore required to fully integrate these data into our knowledge of plant biology. This review aims to highlight recent advances made in the function and enzymology of S-acylation in plants, highlights current and emerging technologies for its study and suggests future avenues for investigation.
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April 2020
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Cover Image
The cover shows a metaphorical representation of the anti-CRISPR AcrIIA6, represented as handcuffs, sequestering two Streptococcus thermophilus CRISPR1-Cas9 (St1Cas9) molecules at a time and preventing conformational changes associated with DNA recognition and binding. In the absence of AcrIIA6, St1Cas9 tightly binds to its target DNA, and can proceed to target cleavage. For further information, see the article by Hardouin and Goulet in this issue (pp. 507–516). This cover artwork has been made by Beata Edyta Mierzwa (www.BeataScienceArt.com).
Review Article|
April 02 2020
S-acylation in plants: an expanding field
Piers A. Hemsley
1Division of Plant Sciences, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
2Cell and Molecular Sciences, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, U.K.
Correspondence: Piers A. Hemsley (p.a.hemsley@dundee.ac.uk)
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Biochem Soc Trans (2020) 48 (2): 529–536.
Article history
Received:
January 22 2020
Revision Received:
March 10 2020
Accepted:
March 11 2020
Citation
Piers A. Hemsley; S-acylation in plants: an expanding field. Biochem Soc Trans 29 April 2020; 48 (2): 529–536. doi: https://doi.org/10.1042/BST20190703
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