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J. Biol. Chem., Vol. 278, Issue 44, 43418-43429, October 31, 2003

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Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote^*

Bertrand Boisson, Carmela Giglione, and Thierry Meinnel

From the Protein Maturation Group, Institut des Sciences du Végétal, UPR2355, Centre National de la Recherche Scientifique, Bâtiment 23, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France

N-Myristoylation is an irreversible modification that affects the membrane binding properties of crucial cytoplasmic proteins from signal transduction cascades. We characterized the two putative N-myristoyltransferases of Arabidopsis thaliana as a means of investigating the entire N-myristoylation proteome (N-myristoylome) in a higher eukaryote. AtNMT1 compensated for the nmt1 defect in yeast, whereas AtNMT2 and chimeras of the two genes did not. Only AtNMT1 modified known N-myristoylated proteins in vitro. AtNMT1 is therefore responsible for the A. thaliana N-myristoylome, whereas AtNMT2 does not seem to have usual myristoylation activity. We began with the whole set of N-myristoylated G proteins in the A. thaliana proteome. We then used a reiterative approach, based on the in vitro N-myristoylation of more than 60 different polypeptides, to determine the substrate specificity of AtNMT1. We found that the positive charge on residue 7 of the substrate was particularly important in substrate recognition. The A. thaliana N-myristoylome consists of 437 proteins, accounting for 1.7% of the complete proteome. We demonstrated the N-myristoylation of several unexpected protein families, including innate immunity proteins, thioredoxins, components of the protein degradation pathway, transcription factors, and a crucial regulatory enzyme of glycolysis. The role of N-myristoylation is discussed in each case; in particular, this process may underlie the "guard" hypothesis of innate immunity.

Received for publication, July 9, 2003 , and in revised form, August 11, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF250956 and AF250957

^* This work was supported in part by an Action Thématique et Incitative sur Programme grant from the CNRS (to T. M.) and by Grant 4477 from the Association pour la Recherche sur le Cancer (Villejuif, France). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Table s1 and Figure s1.

Recipient of a Ph.D. studentship from the Fondation pour la Recherche Médicale.

To whom all correspondence should be addressed. Tel.: 33-1-69-82-36-12; Fax: 33-1-69-82-36-07; E-mail: meinnel{at}isv.cnrs-gif.fr.

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