The Acidic A-Domain of Arabidopsis Toc159 Occurs as a Hyperphosphorylated Protein

Author:

Agne Birgit1,Andrès Charles1,Montandon Cyril1,Christ Bastien1,Ertan Anouk1,Jung Friederike1,Infanger Sibylle1,Bischof Sylvain1,Baginsky Sacha1,Kessler Felix1

Affiliation:

1. Laboratoire de Physiologie Végétale, Université de Neuchâtel, CH–2009 Neuchatel, Switzerland (B.A., C.A., C.M., F.J., S.I., F.K.); University of Zürich, CH–8008 Zurich, Switzerland (B.C.); Philip Morris International Research and Development, CH–2000 Neuchatel, Switzerland (A.E.); Department of Biology, Eidgenössische Technische Hochschule Zürich, 8092 Zurich, Switzerland (S. Bischof, S. Baginsky

Abstract

Abstract 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 (Arabidopsis thaliana) 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 (Pisum sativum). 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.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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