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The Acidic A-Domain of Arabidopsis Toc159 Occurs as a Hyperphosphorylated Protein
Auteur(s)
Agne, Birgit
Andrès, Charles
Montandon, Cyril
Christ, Bastien
Ertan, Anouk
Jung, Friederike
Infanger, Sibylle
Bischof, Sylvain
Baginsky, Sacha
In
Plant Physiology, American Society of Plant Biologists, 2010/53/3/1016-1030
Résumé
The translocon at the outer membrane of the chloroplast assists the import of a large class of preproteins with amino-terminal transit sequences. The preprotein receptors Toc159 and Toc33 in Arabidopsis (<i>Arabidopsis thaliana</i>) are specific for the accumulation of abundant photosynthetic proteins. The receptors are homologous GTPases known to be regulated by phosphorylation within their GTP-binding domains. In addition to the central GTP-binding domain, Toc159 has an acidic N-terminal domain (A-domain) and a C-terminal membrane-anchoring domain (M-domain). The A-domain of Toc159 is dispensable for its in vivo activity in Arabidopsis and prone to degradation in pea (<i>Pisum sativum</i>). Therefore, it has been suggested to have a regulatory function. Here, we show that in Arabidopsis, the A-domain is not simply degraded but that it accumulates as a soluble, phosphorylated protein separated from Toc159. However, the physiological relevance of this process is unclear. The data show that the A-domain of Toc159 as well as those of its homologs Toc132 and Toc120 are targets of a casein kinase 2-like activity.
Identifiants
Type de publication
journal article
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