Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features

Bienvenut, W.V., Sumpton, D., Martinez, A., Lilla, S., Espagne, C., Meinnel, T. and Giglione, C. (2012) Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features. Molecular and Cellular Proteomics, 11(6), M111.015131. (doi: 10.1074/mcp.M111.015131)

Abstract

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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Bienvenut, Dr Willy and Sumpton, Mr David and Lilla, Dr Sergio
• Authors: Bienvenut, W.V., Sumpton, D., Martinez, A., Lilla, S., Espagne, C., Meinnel, T., and Giglione, C.
• College/School: College of Medical Veterinary and Life Sciences > School of Cancer Sciences
• Journal Name: Molecular and Cellular Proteomics
• ISSN: 1535-9476
• Published Online: 05 January 2012