Current views on chloroplast protein import and hypotheses on the origin of the transport mechanism |
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Authors: | E. Kathleen Archer Kenneth Keegstra |
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Affiliation: | (1) Department of Biology, Trinity College, 06106 Hartford, Connecticut;(2) Department of Botany, University of Wisconsin, Birge Hall, 430 Lincoln Drive, 53703 Madison, Wisconsin |
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Abstract: | Most chloroplastic proteins are synthesized as precursors in the cytosol prior to their transport into chloroplasts. These precursors are generally synthesized in a form that is larger than the mature form found inside chloroplasts. The extra amino acids, called transit peptides, are present at the amino terminus. The transit peptide is necessary and sufficient to recognize the chloroplast and induce movement of the attached protein across the envelope membranes. In this review, we discuss the primary and secondary structure of transit peptides, describe what is known about the import process, and present some hypotheses on the evolutionary origin of the import mechanism.Abbreviations DHFR dihydrofolate reductase - EPSP synthase 5-enolpyrovylshikimate-3-phosphate synthase; hsp heat-shock protein - LHCP II light-harvesting chlorophylla/b binding protein - OEE 16, 23, and 33 the 16-, 23-, and 33-kDa proteins of the oxygen-evolving complex - pr precursor - rubisco ribulose-1,5-bisphosphate carboxylase/oxygenase - SS rubisco small subunit |
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Keywords: | Chloroplast import protein evolutionary origin binding translocation |
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