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Originally published In Press as doi:10.1074/jbc.M006417200 on December 18, 2000

J. Biol. Chem., Vol. 276, Issue 11, 7985-7991, March 16, 2001
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Diatom Fucoxanthin Chlorophyll a/c-binding Protein (FCP) and Land Plant Light-harvesting Proteins Use a Similar Pathway for Thylakoid Membrane Insertion*

Markus Lang and Peter G. KrothDagger

From the Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Germany

The light-harvesting proteins in plastids of different lineages including algae and land plants represent a superfamily of chlorophyll-binding proteins that seem to be phylogenetically related, although some of the light-harvesting complex (LHC) proteins bind different carotenoids. LHCs can be divided into chlorophyll a/b-binding proteins found in green algae, euglenoids, and higher plants and into chlorophyll a/c-binding proteins of various algal taxa. LHC proteins from diatoms are named fucoxanthin-chlorophyll a/c-binding proteins (FCP). In contrast to chlorophyll a/b-binding proteins, there is no information so far about the way FCPs integrate into thylakoid membranes. The diatom FCP preproteins have a bipartite presequence that is necessary to enable transport into the four membrane-bound diatom plastids, but similar to chlorophyll a/b-binding proteins there is apparently no presequence present for targeting to the thylakoid membrane. By establishing an in vitro import assay for diatom thylakoids, we demonstrated that thylakoid integration of diatom FCP depends on the presence of stromal factors and GTP. This indicates that a pathway involving signal recognition particles (SRP) is involved in membrane integration just as shown for LHCs in higher plants. We also demonstrate integration of diatom FCP into thylakoids of higher plants and vice versa SRP-dependent targeting of LHCs from pea and Arabidopsis into diatom thylakoids. The similar SRP-dependent modes of thylakoid integration of land plant LHCs and FCPs support recent analyses indicating a common origin of chlorophyll a/b- and a/c-binding proteins.


* This work was supported by grants from the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 189 Project B3 (to P. G. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Institut für Biochemie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Germany. Tel.: 49-211-811-2343; Fax: 49-211-811-3706; E-mail: Peter.Kroth@uni-duesseldorf.de.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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