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  Intracellular location, complex formation, and function of the transporter associated with antigen processing in yeast

Urlinger, S., Kuchler, K., Meyer, T. H., Uebel, S., & Tampe, R. (1997). Intracellular location, complex formation, and function of the transporter associated with antigen processing in yeast. European Journal of Biochemistry, 245(2), 266-272.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7292-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7293-0
Genre: Journal Article

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 Creators:
Urlinger, S., Author
Kuchler, K., Author
Meyer, T. H., Author
Uebel, S.1, Author              
Tampe, R.2, Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2External Organizations, ou_persistent22              

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Free keywords: Transporter associated with antigen processing; Atp-binding-cassette transporter; Peptide transport; Herpes simplex virus; Endoplasmic reticulum.; Major histocompatibility complex; Class-ii region; Ste6 gene-product; Saccharomyces-cerevisiae; Endoplasmic-reticulum; Abc transporters; Peptide binding; A-factor; Resistance; Proteins.; Biochemistry & biophysics.
 Abstract: Peptide transport across the membrane of the endoplasmic reticulum (ER) gains increasing importance in view of its potential function in selective protein degradation and antigen processing. An example for peptide transport in the ER is the transporter associated with antigen processing (TAP), which supplies peptides for the formation of major-histocompatibility-complex class-I complexes. Here, we have expressed human TAP1 and TAP2 in the yeast Saccharomyces cerevisiae. Expression of both genes resulted in the formation of a stable TAP heterodimer that was localized mainly in the ER. Although a minor fraction of TAP is found in the plasma membrane, TAP is unable to restore a-factor secretion in a mutant cell line that lacks the yeast mating-factor transporter Ste6. Nevertheless, in vitro studies with microsomal vesicles demonstrated that the TAP complex is fully functional in the ER membrane in terms of selective peptide binding, ATP-dependent transport, and specific inhibition by the viral protein of herpes simplex virus ICP47. This offers opportunities for topological, structural and mechanistic studies as well as genetic screenings for TAP functionality. [References: 55]

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 Dates: 1997-04-15
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 318685
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Title: European Journal of Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 245 (2) Sequence Number: - Start / End Page: 266 - 272 Identifier: -