melitten and isopentenyl-pyrophosphate

melitten has been researched along with isopentenyl-pyrophosphate* in 1 studies

Other Studies

1 other study(ies) available for melitten and isopentenyl-pyrophosphate

Article	Year
Posttranslational isoprenylation of rho protein is a prerequisite for its interaction with mastoparan and other amphiphilic agents. Biochemical and biophysical research communications, 1992, Jul-15, Volume: 186, Issue:1 The amphiphilic agents melittin, compound 48/80 and mastoparan inhibit ADP-ribosylation of porcine brain rho protein by Clostridium botulinum exoenzyme C3. However, ADP-ribosylation of recombinant rhoA expressed in E.coli was not inhibited by these agents. Accordingly, steady state GTP hydrolysis by recombinant rhoA was not stimulated by mastoparan, whereas GTP hydrolysis by porcine brain rho was stimulated 2.5-fold in the presence of this wasp venom. After microinjection of recombinant rhoA into Xenopus laevis oocytes the inhibitory effect of mastoparan on C3 ADP-ribosylation was restored. The data suggest that the amphiphilic agents tested are only active at the posttranslationally processed form of rho and that they exert their effects via the C-terminal end. Topics: Adenosine Diphosphate Ribose; Animals; Autoradiography; Brain; Carbon Radioisotopes; Cloning, Molecular; Cytosol; Escherichia coli; GTP-Binding Proteins; Guanosine Triphosphate; Hemiterpenes; Intercellular Signaling Peptides and Proteins; Melitten; NAD; Oocytes; Organophosphorus Compounds; p-Methoxy-N-methylphenethylamine; Peptides; Protein Processing, Post-Translational; Recombinant Proteins; rhoA GTP-Binding Protein; Swine; Wasp Venoms; Xenopus laevis	1992

Article

Year

Posttranslational isoprenylation of rho protein is a prerequisite for its interaction with mastoparan and other amphiphilic agents.

Biochemical and biophysical research communications, 1992, Jul-15, Volume: 186, Issue:1

The amphiphilic agents melittin, compound 48/80 and mastoparan inhibit ADP-ribosylation of porcine brain rho protein by Clostridium botulinum exoenzyme C3. However, ADP-ribosylation of recombinant rhoA expressed in E.coli was not inhibited by these agents. Accordingly, steady state GTP hydrolysis by recombinant rhoA was not stimulated by mastoparan, whereas GTP hydrolysis by porcine brain rho was stimulated 2.5-fold in the presence of this wasp venom. After microinjection of recombinant rhoA into Xenopus laevis oocytes the inhibitory effect of mastoparan on C3 ADP-ribosylation was restored. The data suggest that the amphiphilic agents tested are only active at the posttranslationally processed form of rho and that they exert their effects via the C-terminal end.

Topics: Adenosine Diphosphate Ribose; Animals; Autoradiography; Brain; Carbon Radioisotopes; Cloning, Molecular; Cytosol; Escherichia coli; GTP-Binding Proteins; Guanosine Triphosphate; Hemiterpenes; Intercellular Signaling Peptides and Proteins; Melitten; NAD; Oocytes; Organophosphorus Compounds; p-Methoxy-N-methylphenethylamine; Peptides; Protein Processing, Post-Translational; Recombinant Proteins; rhoA GTP-Binding Protein; Swine; Wasp Venoms; Xenopus laevis

1992