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J. Biol. Chem., Vol. 276, Issue 7, 4564-4569, February 16, 2001
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From the Translation of psbA mRNA in
Chlamydomonas reinhardtii chloroplasts is regulated by a
redox signal(s). RB60 is a member of a protein complex that binds with
high affinity to the 5'-untranslated region of psbA
mRNA. RB60 has been suggested to act as a redox-sensor subunit of
the protein complex regulating translation of chloroplast psbA mRNA. Surprisingly, cloning of RB60 identified
high homology to the endoplasmic reticulum-localized protein disulfide
isomerase, including an endoplasmic reticulum-retention signal at its
carboxyl terminus. Here we show, by in vitro import
studies, that the recombinant RB60 is imported into isolated
chloroplasts of C. reinhardtii and pea in a transit
peptide-dependent manner. Subfractionation of C. reinhardtii chloroplasts revealed that the native RB60 is partitioned between the stroma and the thylakoids. The nature of
association of native RB60, and imported recombinant RB60, with
thylakoids is similar and suggests that RB60 is tightly bound to
thylakoids. The targeting characteristics of RB60 and the potential implications of the association of RB60 with thylakoids are discussed.
The Protein Disulfide Isomerase-like RB60 Is Partitioned
between Stroma and Thylakoids in Chlamydomonas reinhardtii
Chloroplasts*
§,¶,
,, and**
Department of Plant Sciences, Weizmann
Institute of Science and the Department of Agricultural
Botany, The Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
*
This work was supported in part by grants from the Israel
Science Foundation and the Minerva Foundation.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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