Protein N-acylation overrides differing targeting signals.

TitleProtein N-acylation overrides differing targeting signals.
Publication TypeJournal Article
Year of Publication2011
AuthorsStael, S, Bayer, RG, Mehlmer, N, Teige, M
JournalFEBS Lett
Volume585
Issue3
Pagination517-22
Date Published2011 Feb 4
ISSN1873-3468
KeywordsAcylation, Arabidopsis Proteins, Cell Membrane, Chloroplasts, Ferredoxin-NADP Reductase, Lipoylation, Mutant Proteins, Myristic Acid, Palmitic Acid, Plant Proteins, Protein Kinases, Protein Processing, Post-Translational, Protein Transport, Recombinant Fusion Proteins, Tobacco
Abstract

In a bioinformatics based screen for chloroplast-localized protein kinases we noticed that available protein targeting predictors falsely predicted chloroplast localization. This seems to be due to interference with N-terminal protein acylation, which is of particular importance for protein kinases. Their N-myristoylation was found to be highly overrepresented in the proteome, whereas myristoylation motifs are almost absent in known chloroplast proteins. However, only abolishing their myristoylation was not sufficient to target those kinases to chloroplasts and resulted in nuclear accumulation instead. In contrast, inhibition of N-myristoylation of a calcium-dependent protein kinase was sufficient to alter its localization from the plasma membrane to chloroplasts and chloroplast localization of ferredoxin-NADP+ reductase and Rubisco activase could be efficiently suppressed by artificial introduction of myristoylation and palmitoylation sites.

DOI10.1016/j.febslet.2011.01.001
Alternate JournalFEBS Lett.
Citation Key10.1016/j.febslet.2011.01.001
PubMed ID21219905
PubMed Central IDPMC3971372
Grant ListI 253 / / Austrian Science Fund FWF / Austria