Characterization of the translocon of the outer envelope of chloroplasts

doi:10.1083/jcb.200210060

Published 18 February 2003. doi:10.1083/jcb.200210060

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© The Rockefeller University Press, 0021-9525/2003/2/541 $5.00
The Journal of Cell Biology, Volume 160, Number 4, 541-551

Article

Characterization of the translocon of the outer envelope of chloroplasts

Enrico Schleiff¹, Jürgen Soll¹, Michael Küchler¹, Werner Kühlbrandt² and Roswitha Harrer²

¹ Botanisches Institut, Ludwig Maximilian Universität München, 80638 München, Germany
² Max-Planck-Institut für Biophysik, 60528 Frankfurt am Main, Germany

Address correspondence to Enrico Schleiff, Botanisches Institut, LMU München, Menzinger Str. 67, 80638 München, Germany. Tel.: 49-89-17861-182. Fax: 49-89-17861-185. E-mail: schleiff{at}botanik.biologie.uni-muenchen.de

The protein translocon of the outer envelope of chloroplasts(Toc) consists of the core subunits Toc159, Toc75, and Toc34.To investigate the molecular structure, the core complex waspurified. This core complex has an apparent molecular mass of $~$ 500 kD and a molecular stoichiometry of 1:4:4–5 betweenToc159, Toc75, and Toc34. The isolated translocon recognizesboth transit sequences and precursor proteins in a GTP-dependentmanner, suggesting its functional integrity. The complex isembedded by the lipids phosphatidylcholine and digalactosyldiacylglyceride.Two-dimensional structural analysis by EM revealed roughly circularparticles consistent with the formation of a stable core complex.The particles show a diameter of $~$ 130 Å with a solid ringand a less dense interior structure. A three-dimensional mapobtained by random conical tilt reconstruction of electron micrographssuggests that a "finger"-like central region separates fourcurved translocation channels within one complex.

Key Words: complex structure; protein translocation; complex composition; preprotein recognition; membrane complex purification

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