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PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
Published on: July 3, 2010
Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
A Zapun1, S M Petrescu, P M Rudd
1Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
Abstract:
Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. Binding was independent of the conformation of the glycoprotein. Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively as a lectin.
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