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THE PLANT CELL, Vol 2, Issue 5 479-494, Copyright © 1990 by American Society of Plant Biologists
Protein Import into and Sorting inside the Chloroplast Are Independent Processes
J. Hageman, C. Baecke, M. Ebskamp, R. Pilon, S. Smeekens and P. Weisbeek
Department of Molecular Cell Biology and Institute of Molecular Biology, University of Utrecht, Padualaan 8, NL 3584 CH Utrecht, The Netherlands
Plastocyanin is a nuclear-encoded chloroplast thylakoid lumen protein that
is synthesized in the cytoplasm with a large N-terminal extension (66 amino
acids). Transport of plastocyanin involves two steps: import across the
chloroplast envelope into the stroma, followed by transfer across the
thylakoid membrane into the lumen. During transport the N-terminal
extension is removed in two parts by two different processing proteases. In
this study we examined the functions of the two cleaved parts, C1 and C2,
in the transport pathway of plastocyanin. The results show that C1 mediates
import into the chloroplast. C1 is sufficient to direct chloroplast import
of mutant proteins that lack C2. It is also sufficient to direct import of
a nonplastid protein and can be replaced functionally by the transit
peptide of an imported stromal protein. C2 is a prerequisite for
intraorganellar routing but is not required for chloroplast import.
Deletions in C2 result in accumulation of intermediates in the stroma or on
the outside of the thylakoids. The fact that C1 is functionally equivalent
to a stromal-targeting transit peptide shows that plastocyanin is imported
into the chloroplast by way of the same mechanism as stromal proteins, and
that import into and routing inside the chloroplasts are independent
processes.
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