Publication Information
Kumar et al., 2022
Abstract
Nat Plants. 2022 Jun;8(6):670-681. doi: 10.1038/s41477-022-01164-4. Epub 2022
Jun 9.
An atlas of Arabidopsis protein S-acylation reveals its widespread role in plant
cell organization and function.
Kumar M(1), Carr P(1)(2), Turner SR(3).
Author information:
(1)Faculty of Biology, Medicine and Health, University of Manchester,
Manchester, UK.
(2)Holiferm, Manchester, UK.
(3)Faculty of Biology, Medicine and Health, University of Manchester,
Manchester, UK. simon.turner@manchester.ac.uk.
S-acylation is the addition of a fatty acid to a cysteine residue of a protein.
While this modification may profoundly alter protein behaviour, its effects on
the function of plant proteins remains poorly characterized, largely as a result
of the lack of basic information regarding which proteins are S-acylated and
where in the proteins the modification occurs. To address this gap in our
knowledge, we used an optimized acyl-resin-assisted capture assay to perform a
comprehensive analysis of plant protein S-acylation from six separate tissues.
In our high- and medium-confidence groups, we identified 1,849 cysteines
modified by S-acylation, which were located in 1,640 unique peptides from 1,094
different proteins. This represents around 6% of the detectable Arabidopsis
proteome and suggests an important role for S-acylation in many essential
cellular functions including trafficking, signalling and metabolism. To
illustrate the potential of this dataset, we focus on cellulose synthesis and
confirm the S-acylation of a number of proteins known to be involved in
cellulose synthesis and trafficking of the cellulose synthase complex. In the
secondary cell walls, cellulose synthesis requires three different catalytic
subunits (CESA4, CESA7 and CESA8) that all exhibit striking sequence similarity
and are all predicted to possess a RING-type zinc finger at their amino terminus
composed of eight cysteines. For CESA8, we find evidence for S-acylation of
these cysteines that is incompatible with any role in coordinating metal ions.
We show that while CESA7 may possess a RING-type domain, the same region of
CESA8 appears to have evolved a very different structure. Together, the data
suggest that this study represents an atlas of S-acylation in Arabidopsis that
will facilitate the broader study of this elusive post-translational
modification in plants as well as demonstrating the importance of further work
in this area.
© 2022. The Author(s), under exclusive licence to Springer Nature Limited.
DOI: 10.1038/s41477-022-01164-4
PMID: 35681017 [Indexed for MEDLINE]
