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Guanosine 5'-(3-O-Thio)triphosphate stimulates protein carboxyl methylation in cell membranes. 1999

R R Desrosiers, and R Béliveau
Centre de cancérologie Charles Bruneau, Université du Québec à Montréal, C. P. 8888, Succursale Centre-ville, Montréal, Québec, H3C 3P8, Canada.

Using guanosine 5'-(3-O-thio)triphosphate (GTPgammaS), we previously reported that protein carboxyl methyltransferase activities in kidney brush border membranes were increased by the GTP analog (Arch. Biochem. Biophys. 351, 149-158, 1998). Here, we investigated the distribution and characterized the effect of GTPgammaS on protein carboxyl methylation activity. The analysis of species distribution of carboxyl methylation in kidney brush border membranes showed that the GTPgammaS strongly stimulated this activity in rat (15.9-fold), mouse (14.7-fold), human (2.9-fold), and rabbit (2.7-fold). Analysis of GTPgammaS-dependent carboxyl methylation in rat tissues and cell fractions indicated that the activity was mainly localized in membranes of intestine, lung, and kidney, with the highest activity found in liver. To characterize the methyltransferase activity modulated by GTPgammaS in liver membranes, their sensitivity to the detergent 3-[(3-cholamido)dimethylammonio]-1-propanesulfonic acid (Chaps) was used. Methylation of N-acetyl-S-farnesyl cysteine, a prenylated protein methyltransferase (PPMT) substrate was strongly inhibited (86%) in the presence of Chaps, while the methylation of bovine calmodulin and ovalbumin, both of which are substrates for the protein L-isoaspartyl/d-aspartyl methyltransferase (PIMT), was slightly reduced by the detergent (0-12%). The GTPgammaS-dependent carboxyl methylation of endogenous substrates in liver membranes was decreased by 35% in the presence of Chaps, suggesting that PPMT was not the predominant methyltransferase involved in the methylation stimulated by GTPgammaS in liver membranes. Electrophoretic analysis showed that radioactive methylation of several substrates induced by GTPgammaS in liver membranes was reduced by adding calmodulin. Interestingly, addition of GTPgammaS partially inhibited the methylation of two PIMT substrates, ovalbumin (24%) and bovine calmodulin (19%), when incubated with liver membranes. Immunoprecipitation of PIMT from liver and lung membranes strongly inhibited (88-94%) the methylation stimulated by GTPgammaS. Altogether, these data support the hypothesis that GTPgammaS could regulate PIMT activity and may provide new insights into the function of the methyltransferase.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D008745 Methylation Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed) Methylations
D010047 Ovalbumin An albumin obtained from the white of eggs. It is a member of the serpin superfamily. Serpin B14
D011496 Protein Methyltransferases Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1. Protein Methylase,Protein Methylases,Protein Methyltransferase,Methylase, Protein,Methylases, Protein,Methyltransferase, Protein,Methyltransferases, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes

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