Specific Prenylation of Tomato Rab Proteins by Geranylgeranyl Type-II Transferase Requires a Conserved Cysteine-Cysteine Motif.
作者： S. Yalovsky , A. E. Loraine , W. Gruissem
关键词: Geranylgeranyl pyrophosphate 、 Geranylgeranyl Transferase 、 Geranylgeranylation 、 Biochemistry 、 Prenylation 、 RAB1 、 Rab 、 Protein subunit 、 Farnesyl pyrophosphate 、 Biology
摘要: Posttranslational isoprenylation of some small GTP-binding proteins is required for their biological activity. Rab geranylgeranyl transferase (Rab GGTase) uses pyrophosphate to modify proteins, its only known substrates. Geranylgeranylation Rabs believed promote association with target membranes and interaction other proteins. Plants, like eukaryotes, contain Rab-like that are associated intracellular membranes. However, our knowledge, the geranylgeranylation has not yet been characterized from any plant source. This report presents an activity assay allows characterization prenylation in vitro, by protein extracts prepared plants. Tomato Rab1 mammalian Rab1a were modified but farnesyl pyrophosphate. modification a conserved cysteine-cysteine motif. A mutant form lacking motif could be modified, inhibited wild-type homolog. The tomato vitro extract yeast, failed become when was yeast strain containing allele [alpha] subunit GGTase (bet4 ts). These results demonstrate cells, GGTase-like
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