Protein geranylgeranyltransferase type II, α- and β-subunit
rat, recombinant, E. coli
For in vitro use only!
Shipping: shipped on dry ice
Storage Conditions: store at -80 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: α: 50 kDa, β: 38 kDa
Accession number: Q08602 / Q08603
Purity: > 90 % (SDS-PAGE)
Form: liquid (Supplied in 50 mM Tris-HCl pH 7.2, 40 mM NaCl and 5 mM DTT and 5 μM ZnCl2)
GGTase-II (Geranylgeranyltransferase-II) catalyzes the transfer of geranylgeranyl moiety onto two C-terminal cysteines of Rab proteins. Composed of an α and β heterodimer (50 and 38 kDa, respectively) and requires Rab escort protein for its catalytic activity. GGTase-II was shown to exhibit higher affinity towards geranylgeranyl pyrophosphate (Kd = 8 nM) than farnesyl pyrophosphate (Kd = 60 nM). Like FTase and GGTase-I, RabGGT functions as a heterodimer. The α subunit has 27% identity to that of CaaX prenylases but contains additional domains, while the β subunit shows 29% identity to that of FTase. The protein substrates of RabGGT have heterogeneous C termini that usually contain two cysteine residues (CXC), both of which are modified by geranylgeranyl groups. Unlike the CaaX prenylases, RabGGT requires specific accessory proteins known as REPs to guide the interaction with its targets. Some farnesyltransferase inhibitors (FTIs) were identified to inhibit RabGGT activity and induce p53 independent apoptosis in C. elegans.
Lackner et al. (2005) Chemical genetics indentifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors. Cancer Cell. 7:325.
Kalinin et al. (2001) Expression of mammalian geranylgeranyltransferase type-II in Escherichia coli and its application for in vitro prenylation of Rab proteins. Protein Expres. Purif. 22:84.
Thomä et al. (2000) Phosphoisoprenoid binding specificity of geranylgeranyltransferase type II. Biochemistry-US 39:12043.
Casey et al. (1996) Protein prenyltransferases. J. Biol. Chem. 271:5289.
Watanabe et al. (2008) Inhibitors of Protein Geranylgeranyltransferase I and Rab Geranylgeranyltransferase Identified from a Library of Allenoate-derived Compounds. J. Biol. Chem. 283 (15):9571-9579.