Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer

FEBS Letters

Gentzsch, Martina¹  Immervoll, Thomas¹  Tanner, Widmar¹ 

[1] Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, 93040 Regensburg, Germany

关键词: Dolichyl phosphate-d-mannose;    Immunoaffinity chromatography;    Glycoprotein;    Protein O-glycosylation;    Mannosyltransferase;    Saccharomyces cerevisiae;    Ac;    acetyl;    Dol-P;    dolichyl phosphate;    Man;    mannose;    PMSF;    phenylmethylsulfonyl fluoride;    Tris;    Tris-hydroxymethylaminomethane;    PAGE;    polyacrylamide gel electrophoresis;    WT;    wild type;   

DOI  :  10.1016/0014-5793(95)01324-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein O-mannosyltransferases Pmt1p and Pmt2p are catalyzing the O-glycosylation of serine and threonine residues in the endoplasmic reticulum of yeast. Deletion of each of these proteins by disruption of the corresponding gene leads to a dramatic decrease of mannosyltransferase activity in vitro. With an anti-Pmt1p immunoaffinity column a complex of Pmt1p and a second protein was purified; this protein turned out to be Pmt2p. Overexpression of Pmt1p or Pmt2p, respectively, does not increase mannosyltransferase activity in vitro. Overexpression of both mannosyltransferases together, however, raises in vitro activity threefold. These data indicate that Pmt1p and Pmt2p function as a complex catalyzing protein O-glycosylation in yeast.

【 授权许可】

Unknown