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Published on January 9, 2008; 10.1104/pp.107.107425

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Received August 15, 2007
Accepted January 2, 2008

Farnesylation directs AtIPT3 subcellular localization and modulates cytokinin biosynthesis in Arabidopsis

Arnaud Galichet , Klara Hoyerova , Miroslav Kaminek , and Wilhelm Gruissem *

Institute of Plant Sciences, ETH Zurich, Universitaetsstrasse 2, 8092 Zurich, Switzerland and Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Rozvojova 135, 165 02 Prague 6, Czech Republic

* Corresponding author; email: wgruissem{at}ethz.ch.

Cytokinins regulate cell division and differentiation as well as number of other processes implicated in plant development. The first step of cytokinin biosynthesis in Arabidopsis is catalyzed by adenosine phosphate-isopentenyltransferases (AtIPT). The enzymes are localized in plastids or the cystoplasm where they utilize the intermediate dimethylallyl-diphosphate from the methylerythritolphosphate or mevalonic acid pathways. However, the regulatory mechanisms linking AtIPT activity and cytokinin biosynthesis with cytokinin homeostasis and isoprenoid synthesis are not well understood. Here we demonstrate that expression of AtIPT3, one member of the adenosine AtIPT protein family in Arabidopsis (Arabidopsis thaliana), increased the production of specific isopentenyl-type cytokinins. Moreover, AtIPT3 is a substrate of the protein farnesyl transferase and AtIPT3 farnesylation directed the localization of the protein in the nucleus/cytoplasm whereas the non-farnesylated protein was located in the plastids. AtIPT3 gain-of-function mutant analysis indicated that the different sub-cellular localization of the farnesylated and non-farnesylated protein was closely correlated with either isopentenyl-type or zeatin-type cytokinins biosynthesis. In addition, mutation of the farnesyl acceptor cysteine 333 of AtIPT3 abolishes cytokinin production, suggesting that Cys-333 has a dual and essential role for AtIPT3 farnesylation and catalytic activity.




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