In vitro biosynthesis and membrane translocation of the serine rich protein of Plasmodium falciparum.
The serine-rich protein (SERP) of Plasmodium falciparum is found within the parasitophorous vacuole. Exons 1 and 2 of the SERP gene were combined to a continuous open reading frame and expressed in a cell free translation/translocation system to study translocation of the protein across membranes. The protein was found to be translocated co-translationally across canine pancreatic microsomes. This process required the presence of the signal recognition particle, and it was accompanied by cleavage of a signal peptide. We conclude that the authentic SERP is exported from the parasite cell via the endoplasmic reticulum.
Ragge
K
K
Fraunhofer Institute of Toxicology, Gene Technology Group, Hamburg, F.R.G.
Arnold
H H
HH
Tümmler
M
M
Knapp
B
B
Hundt
E
E
Lingelbach
K
K
D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D003001:Cloning, Molecular; D016054:DNA, Protozoan / Q000096:biosynthesis*; D010963:Plasmodium falciparum / Q000378:metabolism*; D014176:Protein Biosynthesis; D021382:Protein Sorting Signals / Q000235:genetics* / Q000378:metabolism; D015800:Protozoan Proteins / Q000378:metabolism*; D012694:Serine / Q000378:metabolism*
D002352:Carrier Proteins; D016054:DNA, Protozoan; D021382:Protein Sorting Signals; D015800:Protozoan Proteins; D012694:Serine