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- Title
The consensus motif for N-myristoylation of plant proteins in a wheat germ cell-free translation system.
- Authors
Yamauchi, Seiji; Fusada, Naoki; Hayashi, Hidenori; Utsumi, Toshihiko; Uozumi, Nobuyuki; Endo, Yaeta; Tozawa, Yuzuru
- Abstract
Protein N-myristoylation plays key roles in various cellular functions in eukaryotic organisms. To clarify the relationship between the efficiency of protein N-myristoylation and the amino acid sequence of the substrate in plants, we have applied a wheat germ cell-free translation system with high protein productivity to examine the N-myristoylation of various wild-type and mutant forms of Arabidopsis thaliana proteins. Evaluation of the relationship between removal of the initiating Met and subsequent N -myristoylation revealed that constructs containing Pro at position 3 do not undergo N-myristoylation, primarily because of an inhibitory effect of this amino acid on elimination of the initiating Met by methionyl aminopeptidase. Our analysis of the consensus sequence for N -myristoylation in plants focused on the variability of amino acids at positions 3, 6 and 7 of the motif. We found that not only Ser at position 6 but also Lys at position 7 affects the selectivity for the amino acid at position 3. The results of our analyses allowed us to identify several A. thaliana proteins as substrates for N-myristoylation that had previously been predicted not to be candidates for such modification with a prediction program. We have thus shown that a wheat germ cell-free system is a useful tool for plant N-myristoylome analysis. This in vitro approach will facilitate comprehensive determination of N-myristoylated proteins in plants.
- Subjects
PLANT proteins; WHEAT germ; EUKARYOTIC cells; GENETIC translation; AMINO acid sequence; ARABIDOPSIS thaliana; AMINOPEPTIDASES
- Publication
FEBS Journal, 2010, Vol 277, Issue 17, p3596
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2010.07768.x