Toc64, a New Component of the Protein Translocon of Chloroplasts

doi:10.1083/jcb.148.6.1213

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COPPER(II) CHLORIDE
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© The Rockefeller University Press, 0021-9525/2000/3/1213/ $5.00
The Journal of Cell Biology, Volume 148, Number 6, March 20, 2000 1213-1222

Original Article

Toc64, a New Component of the Protein Translocon of Chloroplasts

Karen Sohrt^a and Jürgen Soll^a
^a Botanisches Institut, Christian-Albrechts-Universität Kiel, D-24118 Kiel, Germany

Correspondence to: Jürgen Soll, Botanisches Institut, Am Botanischen Garten 1-9, Christian-Albrechts-Universität, D-24118 Kiel, Germany. Tel:49-431-8804210 Fax:49-431-8804222 E-mail:jsoll{at}bot.uni-kiel.de.

A subunit of the preprotein translocon of the outer envelopeof chloroplasts (Toc complex) of 64 kD is described, Toc64.Toc64 copurifies on sucrose density gradients with the isolatedToc complex. Furthermore, it can be cross-linked in intact chloroplaststo a high molecular weight complex containing both Toc and Ticsubunits and a precursor protein. The 0 Å cross-linkerCuCl₂ yields the reversible formation of disulfide bridge(s)between Toc64 and the established Toc complex subunits in purifiedouter envelope membranes. Toc64 contains three tetratricopeptiderepeat motifs that are exposed at the chloroplast cytosol interface.We propose that Toc64 functions early in preprotein translocation,maybe as a docking protein for cytosolic cofactors of the proteinimport into chloroplasts.

Key Words: protein import, Toc complex, chloroplasts, outer envelope, tetratricopeptiderepeat motif

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