Plant Molecular Biology 39: 641–645, 1999. © 1999 Kluwer Academic Publishers. Printed in the Netherlands. Mini-review Alexander Caliebe and Jürgen Soill Botanisches Institut, Christian-Albrechts-Universität Kiel, Am Botanischen Garten 1–9, 24118 Kiel, Germany ( author for correspondence) Received 27 October 1998; accepted 2 November 1998 Introduction motif for a cytosolic protein kinase, which phosphory- lates serine or threonine residues. This protein kinase During the co-evolution of ancestor plastids and their speciﬁcally phosphorylates chloroplastidic precursor hosts, the vast majority of genes encoding plastidic proteins, but not mitochondrial and/or peroxisomal proteins were transferred to the genome of the host. precursor proteins . Therefore, systems evolved to mediate the import of The phosphorylated precursor may bind to the Toc nuclear-encoded proteins across two envelope mem- complex, but is arrested in this stage. Before translo- branes into the plastids. This transport system had to cation can resume, it has to be dephosphorylated by be able to distinguish between proteins destined for a not yet identiﬁed phosphatase, which is probably in chloroplasts and other organelles. The challenge was close vicinity to the Toc complex. This cycle of phos- mainly met by the interaction of two protein translo- phorylation/dephosphorylation might be a regulatory cation systems located
Plant Molecular Biology – Springer Journals
Published: Oct 19, 2004
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