Rat tapasin: cDNA cloning and identification as a component of the class I MHC assembly complex View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2001-02

AUTHORS

EV Deverson, SJ Powis, NA Morrice, JA Herberg, J Trowsdale, GW Butcher

ABSTRACT

During the assembly of major histocompatibility complex (MHC) class I molecules transient associations are formed with the endoplasmic reticulum resident chaperones calnexin and calreticulin, ERp57 oxidoreductase, and also with tapasin, the latter mediating binding of the class I molecules to the transporter associated with antigen processing (TAP). We report here the isolation of a cDNA encoding rat tapasin from a DA (RT1av1) library. The cDNA encodes a proline-rich (11.3%) polypeptide of 464 residues with a potential ER-retention KK motif at its COOH-terminus, and a predicted molecular mass of 48 kDa. Matrix-assisted laser-desorption ionisation (MALDI) mass spectrometry of peptides derived from in-gel tryptic digestion of a TAP-associated protein match regions of the predicted translation product. A species of the correct molecular mass and predicted pl was also identified in association with radiolabelled immunoprecipitates of the rat TAP complex analysed by two-dimensional gel electrophoresis. This confirms rat tapasin as a component of the rat MHC class I assembly complex. More... »

PAGES

48

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.gene.6363727

DOI

http://dx.doi.org/10.1038/sj.gene.6363727

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002959576

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11294569


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