[8] Coupled translation/ prenylation of rab proteins in Vitro
作者： Amy L. Wilson , William A. Maltese
DOI: 10.1016/0076-6879(95)50064-2
关键词:
摘要: Publisher Summary This chapter discusses the determination of rab protein in vitro by coupled translation/prenylation. All known mammalian prenyltransferases are found cytosolic compartment cell. Rabbit reticulocyte lysates contain farnesyltransferase (FTase) and geranylgeranyltransferase (GGTase) activities directed toward proteins ending with each different cysteine motifs. Because also translational machinery needed to synthesize polypeptide chains from exogenously supplied mRNAs, a translation/prenylation assay can be devised test ability specific serve as substrate for one or more prenyltransferases. Translation/prenylation reactions started adding mRNA encoding interest. To minimize secondary structure, RNA is first preincubated at 67 ° C 10 minutes. The endogenous occasionally detected some lots lysate that incorporate radiolabeled isoprenoid precursors. Liquid scintillation counting may used obtain direct measurements radioactivity region dried gel containing translation product.
sci-hub.se 参考文章(33)
T Giannakouros, C.M. Newman, M.W. Craighead, J Armstrong, A.I. Magee, Post-translational processing of Schizosaccharomyces pombe YPT5 protein. In vitro and in vivo analysis of processing mutants. Journal of Biological Chemistry. ,vol. 268, pp. 24467- 24474 ,(1993) , 10.1016/S0021-9258(20)80549-3
J.C. Sanford, Y Pan, M Wessling-Resnick, Prenylation of Rab5 is dependent on guanine nucleotide binding. Journal of Biological Chemistry. ,vol. 268, pp. 23773- 23776 ,(1993) , 10.1016/S0021-9258(20)80449-9
K. Vorburger, G.T. Kitten, E.A. Nigg, Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif The EMBO Journal. ,vol. 8, pp. 4007- 4013 ,(1989) , 10.1002/J.1460-2075.1989.TB08583.X
Regulation of Isopentenoid Metabolism American Chemical Society. ,(1992) , 10.1021/BK-1992-0497
M.C. Seabra, J.L. Goldstein, T.C. Südhof, M.S. Brown, Rab geranylgeranyl transferase. A multisubunit enzyme that prenylates GTP-binding proteins terminating in Cys-X-Cys or Cys-Cys. Journal of Biological Chemistry. ,vol. 267, pp. 14497- 14503 ,(1992) , 10.1016/S0021-9258(19)49740-8
J.F. Moomaw, P.J. Casey, Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements. Journal of Biological Chemistry. ,vol. 267, pp. 17438- 17443 ,(1992) , 10.1016/S0021-9258(18)41945-X
R.J. Lutz, T.M. McLain, M Sinensky, Feedback inhibition of polyisoprenyl pyrophosphate synthesis from mevalonate in vitro. Implications for protein prenylation. Journal of Biological Chemistry. ,vol. 267, pp. 7983- 7986 ,(1992) , 10.1016/S0021-9258(18)42396-4
K. Yokoyama, M.H. Gelb, Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex. Journal of Biological Chemistry. ,vol. 268, pp. 4055- 4060 ,(1993) , 10.1016/S0021-9258(18)53579-1
W A Maltese, J D Robishaw, Isoprenylation of C-terminal cysteine in a G-protein gamma subunit. Journal of Biological Chemistry. ,vol. 265, pp. 18071- 18074 ,(1990) , 10.1016/S0021-9258(17)44715-6
B.T. Kinsella, W.A. Maltese, rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif. Journal of Biological Chemistry. ,vol. 266, pp. 8540- 8544 ,(1991) , 10.1016/S0021-9258(18)93008-5