Novel mutants of elongation factor G.
A novel mutant form of elongation factor G (EF-G) in Escherichia coli is described. This variant EF-G restricts reading frame errors by a factor of 2 to 3 in vivo at two different positions in a lacIZ fusion. In addition, a conventional fusidic acid resistant (fusR) mutant of EF-G was compared with the restrictive mutant. Both mutants were characterized in vitro in a steady-state poly(U) translating system. The data indicate that the restrictive EF-G variant has an altered interaction with the ribosome both in vivo and in vitro. In contrast, the conventional fusR variant is altered in its interaction with GTP, which is evident in vitro.
Richter Dahlfors
A A
AA
Department of Molecular Biology, Biomedical Center, Uppsala, Sweden.
Kurland
C G
CG
D004352:Drug Resistance, Microbial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics*; D005672:Fusidic Acid / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism*; D007700:Kinetics; D007763:Lac Operon; D009154:Mutation; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000235:genetics*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000096:biosynthesis*; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012333:RNA, Messenger; D005672:Fusidic Acid; D006160:Guanosine Triphosphate