Characterization of two components of the chloroplastic Tic complex Dissertation der Fakultät für Biologie der Ludwig-Maximilians-Universität München vorgelegt von Johan Philipp Benz aus Bremen München 2009 Erstgutachter: Prof. Dr. J. Soll Zweitgutachter: Prof. Dr. U.C. Vothknecht Tag der mündlichen Prüfung: 22.06.2009 LITTERIS ET FLORIBUS Summary Summary Translocation of nuclear-encoded preproteins across the inner envelope of chloroplasts is catalyzed by the multi-subunit Tic translocon. This machinery can be considered a bottleneck in the pathway of preproteins from the cytosol into the chloroplast. It is therefore perfectly situated to receive signals from inside of the organelle and implement regulatory control over the import process. Seven components have been identified as Tic subunits so far, two of which have been implicated in channel function: Tic110, the central protein of the translocon, and Tic20, a putative alternative channel protein. Another component, Tic62, is part of the so called “redox regulon” of the complex and was proposed to act as a redox sensor, in part because of its specific interaction with the photosynthetic protein ferredoxin-NADP(H) oxidoreductase (FNR) and its redox-dependent shuttling behavior between envelope and stroma.