Publication Information
Marejan et al., 2018
No external accession available
Abstract
Plant Cell. 2018 Mar;30(3):543-562. doi: 10.1105/tpc.17.00523. Epub 2018 Feb 16.
Targeted Profiling of Arabidopsis thaliana Subproteomes Illuminates Co- and
Posttranslationally N-Terminal Myristoylated Proteins.
Majeran W(1), Le Caer JP(2), Ponnala L(3), Meinnel T(4), Giglione C(4).
Author information:
(1)Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université
Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France.
(2)Institut de Chimie des Substances Naturelles, CNRS, Université Paris-Sud,
Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France.
(3)Computational Biology Service Unit, Cornell University, Ithaca, New York
14850 carmela.giglione@i2bc.paris-saclay.fr
thierry.meinnel@i2bc.paris-saclay.fr.
(4)Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université
Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France
carmela.giglione@i2bc.paris-saclay.fr thierry.meinnel@i2bc.paris-saclay.fr.
N-terminal myristoylation, a major eukaryotic protein lipid modification, is
difficult to detect in vivo and challenging to predict in silico. We developed a
proteomics strategy involving subfractionation of cellular membranes, combined
with separation of hydrophobic peptides by mass spectrometry-coupled liquid
chromatography to identify the Arabidopsis thaliana myristoylated proteome. This
approach identified a starting pool of 8837 proteins in all analyzed cellular
fractions, comprising 32% of the Arabidopsis proteome. Of these, 906 proteins
contain an N-terminal Gly at position 2, a prerequisite for myristoylation, and
214 belong to the predicted myristoylome (comprising 51% of the predicted
myristoylome of 421 proteins). We further show direct evidence of myristoylation
in 72 proteins; 18 of these myristoylated proteins were not previously
predicted. We found one myristoylation site downstream of a predicted initiation
codon, indicating that posttranslational myristoylation occurs in plants. Over
half of the identified proteins could be quantified and assigned to a
subcellular compartment. Hierarchical clustering of protein accumulation
combined with myristoylation and S-acylation data revealed that N-terminal
double acylation influences redirection to the plasma membrane. In a few cases,
MYR function extended beyond simple membrane association. This study identified
hundreds of N-acylated proteins for which lipid modifications could control
protein localization and expand protein function.
© 2018 American Society of Plant Biologists. All rights reserved.
DOI: 10.1105/tpc.17.00523
PMCID: PMC5894833
PMID: 29453228 [Indexed for MEDLINE]
