Publication Information
Bienvenut et al., 2015
No external accession available
Abstract
Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131.
Epub 2012 Jan 5.
Comparative large scale characterization of plant versus mammal proteins reveals
similar and idiosyncratic N-α-acetylation features.
Bienvenut WV(1), Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione
C.
Author information:
(1)CNRS, Centre de Recherche de Gif, Institut des Sciences du Végétal, F-91198
Gif-sur-Yvette cedex, France.
N-terminal modifications play a major role in the fate of proteins in terms of
activity, stability, or subcellular compartmentalization. Such modifications
remain poorly described and badly characterized in proteomic studies, and only a
few comparison studies among organisms have been made available so far. Recent
advances in the field now allow the enrichment and selection of N-terminal
peptides in the course of proteome-wide mass spectrometry analyses. These
targeted approaches unravel as a result the extent and nature of the protein
N-terminal modifications. Here, we aimed at studying such modifications in the
model plant Arabidopsis thaliana to compare these results with those obtained
from a human sample analyzed in parallel. We applied large scale analysis to
compile robust conclusions on both data sets. Our data show strong convergence
of the characterized modifications especially for protein N-terminal methionine
excision, co-translational N-α-acetylation, or N-myristoylation between animal
and plant kingdoms. Because of the convergence of both the substrates and the
N-α-acetylation machinery, it was possible to identify the N-acetyltransferases
involved in such modifications for a small number of model plants. Finally, a
high proportion of nuclear-encoded chloroplast proteins feature
post-translational N-α-acetylation of the mature protein after removal of the
transit peptide. Unlike animals, plants feature in a dedicated pathway for
post-translational acetylation of organelle-targeted proteins. The corresponding
machinery is yet to be discovered.
DOI: 10.1074/mcp.M111.015131
PMCID: PMC3433923
PMID: 22223895 [Indexed for MEDLINE]
