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

被引：41

作者：

Hiroi, Y

Komuro, I

Chen, R

Hosoda, T

Mizuno, T

Kudoh, S

Georgescu, SP

Medof, ME

Yazaki, Y

机构：

[1] Univ Tokyo, Sch Med, Dept Med 3, Bunkyo Ku, Tokyo 113, Japan

[2] Case Western Reserve Univ, Inst Pathol, Cleveland, OH 44106 USA

来源：

FEBS LETTERS | 1998年 / 421卷 / 03期

关键词：

Gaa1; GPI anchor; transamidase; glycosylphosphatidylinositol; antisense; signal sequence trap;

D O I：

10.1016/S0014-5793(97)01576-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：252 / 258

页数：7