Synthesis of a hydrolase for the membrane‐form variant surface glycoprotein is repressed during transformation of Trypanosoma brucei

FEBS Letters

Bülow, Roland¹  Overath, Peter¹ 

[1] Max-Planck-Institut für Biologie, Corrensstrasse 38, 7400 Tübingen, FRG

关键词: Variant surface glycoprotein 1;    2-Dimyristoylglycerol Hydrolase Transformation Trypanosoma brucei;    VSG;    variant surface glycoprotein;    mfVSG;    membrane-form VSG;    sVSG;    soluble VSG;    CR-determinant;    cross-reacting determinant;    DecO(EtO)8H;    decylpolyoxyethylene ether;    ClHgBzS03;    p-chloromercuribenzenesulfonate;    CCA;    citrate plus cis-aconitate;    PMSF;    phenylmethylsulfonyl fluoride;    TLCK;    tosyl-L-lysine chloromethyl ketone;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(85)81223-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A membrane-bound phospholipase C-like hydrolase present in lysates of bloodstream forms of Trypanosoma brucei rapidly converts the membrane form of the variant surface protein to the soluble form and 1,2-dimyristoylglycerol [(1985) M.A.J. Ferguson et al. J.Biol.Chem., 260,4963-4968]. The hydrolase is inhibited by p-chloromercuribenzenesulfonate. The synthesis of the enzyme is rapidly repressed upon differentiation of bloodstream forms to procyclic cells and the enzyme activity declines to an undetectable level during subsequent growth of procyclic forms.

【 授权许可】

Unknown