Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycosylphosphatidylinositols to proteins

FEBS Letters

Medof, M.Edward¹  Yazaki, Yoshio²  Kudoh, Sumiyo²  Hosoda, Toru²  Mizuno, Takehiko²  Chen, Rui¹  Georgescu, Serban P²  Komuro, Issei²  Hiroi, Yukio² 

[1] Institute of Pathology, Case Western Reserve University, Cleveland, OH, USA;Department of Medicine III, University of Tokyo School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Gaa1;    GPI anchor;    Transamidase;    Glycosylphosphatidylinositol;    Antisense;    Signal sequence trap;    GPI;    glycosylphosphatidylinositol;    Gaa;    GPI anchor attachment;    PIG;    phosphatidyl inositol glycan;   

DOI  :  10.1016/S0014-5793(97)01576-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Anchoring proteins to cell surface membranes by glycosylphosphatidylinositols (GPIs) is important. We have isolated a component of the putative transamidase machinery, hGaa1p (human GPI anchor attachment protein). hGAA1 cDNA is approximately 2 kb in length and codes 621 amino acids. The amino acid sequence of hGaa1p is 25% identical and 57% homologous to that of yeast Gaa1p. Moreover, Kite-Dolittle hydrophobicity plots of both proteins show marked similarity. hGAA1 gene is expressed ubiquitously and mRNA levels are higher in the undifferentiated state. Overexpression of antisense hGAA1 in human K562 cells significantly reduced the production of a reporter GPI-anchored protein.

【 授权许可】

Unknown