title: Sites of action of fusidic acid in eukaryotes. Inhibition by fusidic acid of a ribosome-independent GTPase from Artemia salina embryos.
abstract: 1. A ribosome-independent GTPase activity has been isolated from the high-speed supernatant fraction of Artemia salina embryos, and some of its properties have been studied. This activity is inhibited by fusidic acid, an antibiotic generally thought to inhibit only EF-2 in eukaryotes. However, several lines of evidence indicate that the GTPase activity, described here, is distinct from EF-2. The results suggest, therefore, that the inhibitory effect of fusidic acid in eukaryotic systems is not restricted to EF-2 (and ribosome)-dependent functions only. 2. The results of other experiments have revealed that, despite its ability to inhibit the GTPase activity mentioned above, fusidic acid is not a non-specific inhibitor of all ribosome-independent GTPase and ATPase activities present in eukaryotic cells.
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D003445:Crustacea / Q000201:enzymology*; D004305:Dose-Response Relationship, Drug; D005672:Fusidic Acid / Q000494:pharmacology*; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000037:antagonists & inhibitors*; D010445:Peptide Elongation Factors; D010649:Phenylalanine; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors*; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes
chemical_list: D010445:Peptide Elongation Factors; D010649:Phenylalanine; D005672:Fusidic Acid; D012343:RNA, Transfer; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D020963:GTP Phosphohydrolase-Linked Elongation Factors