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A more recent version of this article appeared on December 1, 2002
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Submitted on April 11, 2002
Revised on July 23, 2002
Accepted on September 9, 2002
1 School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT, United Kingdom (present address: European Patent Office, Landsbergerstrasse 30, 80339 München, Germany)
2 School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT, United Kingdom
* Corresponding author. E-mail address: stephen.high{at}man.ac.uk.
We have been studying the insertion of the seven transmembrane domain protein opsin in order to gain insights into how the multiple transmembrane domains (TMs) of polytopic proteins are integrated at the endoplasmic reticulum (ER). We find that the ER components associated with the first and second TMs of the nascent opsin polypeptide chain are clearly distinct. The first TM (TM1) is adjacent to the 
and ß subunits of the Sec61 complex, and a novel component, PAT-10. The most striking characteristic of PAT-10 is that it remains adjacent to TM1 throughout the biogenesis and membrane integration of the full-length opsin polypeptide. TM2 is also found to be adjacent to Sec61 and Sec61ß during its membrane integration. However, TM2 does not form any adducts with PAT-10, rather, a transient association with the TRAM protein is observed. We show that the association of PAT-10 with opsin TM1 does not require the N-glycosylation of the nascent chain, and occurs irrespective of the amino acid sequence and transmembrane topology of TM1. We conclude that the precise make up of the ER membrane insertion site can be distinct for the different transmembrane domains of a polytopic protein. We find that the environment of a particular TM can be influenced by both the "stage" of nascent chain biosynthesis reached, and the TM's relative location within the polypeptide.
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