Premium
Protein N‐terminal N‐myristoylation at the proteome scale (587.1)
Author(s) -
Meinnel Thierry,
Castrec Benoit,
Traverso Jose,
Majeran Wojtek,
Giglione Carmela
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.587.1
Subject(s) - myristoylation , myr , proteome , context (archaeology) , computational biology , chemistry , biochemistry , biology , genome , gene , paleontology , phosphorylation
N‐Myristoylation (MYR) is a N‐terminal modification, playing a major role in signal transduction pathways. MYR consists in the addition of a myristate to an N‐terminal Glycine, catalyzed by an N‐myristoyl transferase. MYR often acts together with another lipidation located on Cys residues in the close vicinity, S‐palmytoylation. Such lipidations prove most difficult to evidence even with state‐of‐the‐art proteomics approaches and instruments. Although less than 8 residues are enough to define the selectivity of the MYR, the sequence space diversity of MYR is huge (>109). So far, even fine bioinformatics approaches prove limiting to predict this modification. In this context, we have started a comprehensive analysis of this N‐terminal acylation in A. thaliana. With a new high‐throughput in vitro assay and the systematic measurement of catalytic efficiencies, >1200 synthetic octapeptides encoding the N‐terminal part of verified open‐reading frames could be assayed out of the ~2500 possible candidates. It is now possible to better cover the extent of the Myristoylated proteome from A. thaliana using computer modeling and to translate this knowledge to other proteomes including humans. Unexpected new families including thioredoxins for instance could be evidenced. We conclude that MYR is a more frequent modification than initially expected and that its specific recognition motif is extremely complex. Grant Funding Source : CNRS, ANR, ARC