A Rab1 homologue with a novel isoprenylation signal provides insight into the secretory pathway of Theileria parva.

作者: Rozmin Janoo , Anthony Musoke , Clive Wells , Richard Bishop

DOI: 10.1016/S0166-6851(99)00093-6

关键词: GTP-binding protein regulatorsBiologyGTP'RabVesicular transport proteinSecretory pathwayPrenylationEndoplasmic reticulumGeranylgeranyl pyrophosphateBiochemistry

摘要: Abstract As a first step in developing compartment-specific markers for protein trafficking within Theileria parva, we have isolated cDNAs encoding homologues of the small GTP binding proteins Rab1 and Rab4. The T. parva homologue (TpRab1), which regulates vesicular transport between endoplasmic reticulum cis golgi other organisms, was unusual that it contained unique 17 amino acid C-terminal extension. motif sequence KCT (XCX) contrasted with CXC or XCC motifs act as signals isoprenylation by geranylgeranyl most Rab proteins, including all known homologues, containing only single cysteine. [C14]mevalonic lactone [H3]geranylgeranyl pyrophosphate were specifically incorporated into recombinant TpRab1 vitro, demonstrating novel functional isoprenylation. Recombinant bound radiolabeled GTP, this inhibited excess unlabeled GDP also partially ATP. gene four short (34–67 bp) introns distinct pattern occurrence compared to lower eukaryote genes. Immunofluorescence microscopy using antiserum specific peptide combination labelling cells nucleic acid-staining dye DAPI, indicated located vicinity schizont nucleus infected lymphocyte.

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