The procyclic acidic repetitive proteins of Trypanosoma brucei. Purification and post-translational modification.
The procyclic acidic repetitive protein (PARP) of Trypanosoma brucei was purified by cell fractionation followed by ion-exchange and concanavalin A-Sepharose affinity chromatography. PARP is membrane-bound and comprises about 1% of the total procyclic trypanosome protein or 6 x 10(6) molecules per parasite. The results of NH2-terminal sequencing and amino acid analysis indicate that PARP is processed by removal of an N-terminal signal sequence and the hydrophobic COOH terminus. Metabolic labeling of PARP with [3H] ethanolamine is consistent with attachment of the protein to the membrane via a glycosylphosphatidylinositol anchor. The glycolipid can be removed by base hydrolysis or nitrous acid deamination but is not susceptible to bacterial phosphatidylinositol-specific phospholipase C.
Clayton
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Rockefeller University, New York 10021.
Mowatt
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D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D002458:Cell Fractionation; D006017:Glycolipids / Q000378:metabolism; D017261:Glycosylphosphatidylinositols; D006868:Hydrolysis; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D015800:Protozoan Proteins; D012091:Repetitive Sequences, Nucleic Acid; D013194:Staining and Labeling; D014346:Trypanosoma brucei brucei / Q000032:analysis* / Q000201:enzymology / Q000235:genetics; D010738:Type C Phospholipases
D000953:Antigens, Protozoan; D006017:Glycolipids; D017261:Glycosylphosphatidylinositols; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D010716:Phosphatidylinositols; D015800:Protozoan Proteins; C053277:procyclic acidic repetitive protein, Trypanosoma; D010738:Type C Phospholipases