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Synthesis of a hydrolase for the membrane‐form variant surface glycoprotein is repressed during transformation of Trypanosoma brucei
Author(s) -
Bülow Roland,
Overath Peter
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81223-0
Subject(s) - trypanosoma brucei , hydrolase , glycoprotein , enzyme , biochemistry , transformation (genetics) , chemistry , biology , phospholipase , gene
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.