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A more recent version of this article appeared on October 3, 2003 Originally published In Press as doi:10.1074/jbc.M306367200 on July 23, 2003 Originally published In Press as doi:10.1074/jbc.M306367200 on July 21, 2003
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Papers In Press, published online ahead of print July 23, 2003
J. Biol. Chem, 10.1074/jbc.M306367200
Submitted on June 16, 2003
Revised on July 21, 2003
Accepted on July 21, 2003

atTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts

Takehito Inaba, Ming Li, Mayte Alvarez-Huerta, Felix Kessler, and Danny J. Schnell

Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003

Corresponding Author: dschnell{at}biochem.umass.edu

The translocon of the inner envelope membrane of chloroplasts (Tic) mediates the late events in the translocation of nucleus-encoded preproteins into chloroplasts. Tic110 is a major integral membrane component of active Tic complexes and has been proposed to function as a docking site for translocation-associated stromal factors and as a component of the protein-conducting channel. To investigate the various proposed functions of Tic110, we have investigated the structure, topology and activities of a 97.5 kDa fragment of Arabidopsis Tic110, atTic110, lacking only the amino-terminal transmembrane segments. The protein was expressed both in E. coli and Arabidopsis as a stable, soluble protein with a high alpha-helical content. Binding studies demonstrate that a region of the atTic110 soluble domain selectively associates with chloroplast preproteins at the late stages of membrane translocation. These data support the hypothesis that the bulk of Tic110 extends into the chloroplast stroma and suggest that the domain forms a docking site for preproteins as they emerge from the Tic translocon.


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