Document Detail


High-throughput profiling of N-Myristoylation substrate specificity across species including pathogens.
MedLine Citation:
PMID:  23165749     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
One of the most critical modifications affecting the N-terminus of proteins is N-Myristoylation. This irreversible modification affects the membrane binding properties of crucial proteins involved in signal transduction cascades. This cotranslational modification, catalyzed by N-myristoyl transferase, occurs both in lower and higher Eukaryotes and is a validated therapeutic target for several pathologies. However, this lipidation proves very difficult to evidence in vivo even with state-of-the-art proteomics approaches or bioinformatics tools. A large part of N-Myristoylated proteins remains to be discovered and the rules of substrate specificity need to be established in each organism. Because the peptide substrate recognition occurs around the first 8 residues, short peptides are used for modeling the reaction in vitro. Here, we provide a novel approach including a dedicated peptide array for high-throughput profiling protein N-myristoylation specificity. We show that Myristoylation predictive tools need to be fine-tuned to organisms and that their poor accuracy should be significantly enhanced. This should lead to strongly improved knowledge of the number and function of myristoylated proteins occurring in any proteome.
Authors:
José A Traverso; Carmela Giglione; Thierry Meinnel
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-20
Journal Detail:
Title:  Proteomics     Volume:  -     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Affiliation:
CNRS, Centre de Recherche de Gif, Institut des Sciences du Végétal, Bâtiment 23A, 1 avenue de la Terrasse, F-91198, Gif-sur-Yvette cedex, France.
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