Plant Cell Advance Online Publication
Published on March 8, 2002; 10.1105/tpc.010336
Received August 8, 2001
Accepted November 12, 2001
In Vivo Analysis of the Role of atTic20 in Protein Import into Chloroplasts
Xuejun Chen 1, Matthew D. Smith 1, Lynda Fitzpatrick 2, and Danny J. Schnell 1*
1
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst,
Massachusetts 01003
2
Michigan State University--Department of Energy Plant Research Laboratory and
Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824
* To whom correspondence should be addressed. E-mail: dschnell{at}biochem.umass.edu.
The import of nucleus-encoded preproteins into plastids requires the coordinated
activities of membrane protein complexes that facilitate the translocation of polypeptides
across the envelope double membrane. Tic20 was identified previously as a component
of the import machinery of the inner envelope membrane by covalent cross-linking
studies with trapped preprotein import intermediates. To investigate the role of
Tic20 in preprotein import, we altered the expression of the Arabidopsis Tic20 ortholog
(atTic20) by antisense expression. Several antisense lines exhibited pronounced chloroplast
defects exemplified by pale leaves, reduced accumulation of plastid proteins, and
significant growth defects. The severity of the phenotypes correlated directly with
the reduction in levels of atTic20 expression. In vitro import studies with plastids
isolated from control and antisense plants indicated that the antisense plastids
are defective specifically in protein translocation across the inner envelope membrane.
These data suggest that Tic20 functions as a component of the protein-conducting
channel at the inner envelope membrane.
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