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The C‐terminal tripeptide of glycosomal phosphoglycerate kinase is both necessary and sufficient for import into the glycosomes of Trypanosoma brucei
Author(s) -
Sommer Jürg M.,
Peterson Gregory,
Keller Gilbert-A.,
Parsons Marilyn,
Wang C.C.
Publication year - 1993
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(93)81735-i
Subject(s) - trypanosoma brucei , phosphoglycerate kinase , biochemistry , luciferase , serine , tripeptide , biology , immunoelectron microscopy , chemistry , amino acid , enzyme , gene , genetics , transfection , antibody
Glycosomal phosphoglycerate kinase (gPGK) of Trypanosoma brucei differs from the cytoplasmic isozyme (cPGK) in its higher isoelectric point characterized by clusters of positive charges along the polypeptide chain, and a 20 amino acid C‐terminal extension ending in serine‐serine‐leucine (SSL). While a C‐terminal SSL tripeptide is apparently not capable of directing luciferase to the peroxisomes in mammalian cells [J. Cell Biol. 108 (1989), 1657‐1664], we show here that it is sufficient for the import of luciferase as well as an unrelated protein, β‐glucuronidase, into the glycosomes of T. brucei , as determined by immunoelectron microscopy. The analysis of luciferase‐gPGK fusion proteins indicates that the only targeting signal for import of gPGK into the glycosome resides in this C‐terminal SSL sequence.