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Characterization of the ternary complex between Rab7, REP-1 and Rab geranylgeranyl transferase by Kirill Alexandrov; Iris Simon; Vyacheslav Yurchenko; Andrei Iakovenko; Elena Rostkova; Axel J. Scheidig; Roger S. Goody is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Characterization of the ternary complex between Rab7, REP-1 and Rab geranylgeranyl transferase about?
Geranylgeranylation is a post‐translational modification of Rab GTPases that enables them to associate reversibly with intracellular membranes. Geranylgeranylation of Rab proteins is critical for their activity in controlling intracellular membrane transport. According to the currently accepted model for their action, newly synthesized Rab proteins are recruited by Rab escort protein (REP) and are presented to the Rab geranylgeranyl transferase (RabGGTase) which covalentely modifies the Rab protein with two geranylgeranyl moieties. After prenylation, the Rab protein remains in complex with REP and is delivered to the target membrane by the latter. In this work, we show that RabGGTase can form a stable complex with Rab7–REP in the absence of its lipid substrate geranylgeranyl pyrophosphate. In order to characterize this interaction, we developed three fluorescence assays reporting on the interaction of RabGGTase with the Rab7–REP complex. For this interaction we determined a __K__~d~ value of about 120 nm. Association of RabGGTase with the Rab7–REP complex occurs with a rate constant of ≈ 10^8^ m^−1^·s^−1^. We demonstrate that the state of the nucleotide bound to Rab7 does not influ
Who reads Characterization of the ternary complex between Rab7, REP-1 and Rab geranylgeranyl transferase?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Kirill Alexandrov; Iris Simon; Vyacheslav Yurchenko; Andrei Iakovenko; Elena Rostkova; Axel J. Scheidig; Roger S. Goody
- Publisher
- John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)
- Published
- 1999
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)