PXD031348-1

PXD031348 is an original dataset announced via ProteomeXchange.

Title	An atlas of Arabidopsis protein S-Acylation reveals its widespread role in plant cell organisation of and function.
Description	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 characterised, largely as a result to the lack of basic information regarding which proteins are S-acylated and where in the proteins the modification occurs. In order to address this gap in our knowledge, we have performed a comprehensive analysis of plant protein S-acylation from 6 separate tissues. In our high and medium confidence groups, we identified 1849 cysteines modified by S-acylation, which were located in 1640 unique peptides from 1094 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 for the first time 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 N-terminus composed of 8 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 suggests 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 demonstrates the importance of undertaking further work in this area.
HostingRepository	PRIDE
AnnounceDate	2022-06-26
AnnouncementXML	Submission_2022-06-26_05:41:51.027.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD031348
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Manoj Kumar
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	S-carboxamidoethyl-L-cysteine; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2022-01-31 00:57:27	ID requested
⏵ 1	2022-06-26 05:41:51	announced

Dataset with its publication pending

submitter keyword: Arabidopsis, Acylome, Cellulose Synthesis

Simon Turner
contact affiliation	Faculty of Biology, Medicine and Health University of Manchester
contact email	simon.turner@manchester.ac.uk
lab head
Manoj Kumar
contact affiliation	University of Manchester
contact email	manoj.kumar@manchester.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD031348
     1. Label: PRIDE project
     2. Name: An atlas of Arabidopsis protein S-Acylation reveals its widespread role in plant cell organisation of and function.