The Endoplasmic Reticulum Chaperone Cosmc Directly Promotes in Vitro Folding of T-synthase |
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Authors: | Rajindra P. Aryal Tongzhong Ju Richard D. Cummings |
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Affiliation: | From the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322 |
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Abstract: | The T-synthase is the key β3-galactosyltransferase essential for biosynthesis of core 1 O-glycans (Galβ1–3GalNAcα1-Ser/Thr) in animal cell glycoproteins. Here we describe the novel ability of an endoplasmic reticulum-localized molecular chaperone termed Cosmc to specifically interact with partly denatured T-synthase in vitro to cause partial restoration of activity. By contrast, a mutated form of Cosmc observed in patients with Tn syndrome has reduced chaperone function. The chaperone activity of Cosmc is specific, does not require ATP in vitro, and is effective toward T-synthase but not another β-galactosyltransferase. Cosmc represents the first ER chaperone identified to be required for folding of a glycosyltransferase. |
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Keywords: | Chaperones/Protein Folding Cosmc Endoplasmic Reticulum Galactosyltransferase Molecular Chaperone T-synthase |
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