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Topology Studies of the Chloroplast Protein Import Channel Toc75

  • N. Sveshnikova , R. Grimm , J. Soll and E. Schleiff
Published/Copyright: July 5, 2005
Biological Chemistry
From the journal Volume 381 Issue 8

Abstract

A major goal in understanding protein transport across membranes is the investigation of the structure and regulation of the translocon subunits. We analysed Toc75, a pore-forming subunit of the translocon of the outer envelope of chloroplasts. Toc75 was over-expressed and reconstituted into liposomes. Immunoprecipitation of liposome-reconstituted Toc75 indicates an Nin-Cin orientation of Toc75. Limited proteolytic digestion of Toc75 present in outer envelope vesicles with specific proteases combined with amino acid sequencing was used to study the topology of Toc75. Finally, computer modelling based on known protein structures indicates that Toc75 traverses the outer envelope with 16 amphiphilic beta sheets and the topology model is presented.

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Published Online: 2005-07-05
Published in Print: 2000-08-06

Copyright (c) 2000 by Walter de Gruyter GmbH & Co. KG

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