Title : Substitution of Val20 by Gly in elongation factor Tu. Effects on the interaction with elongation factors Ts, aminoacyl-tRNA and ribosomes.

Pub. Date : 1989 Nov 6

PMID : 2684669






6 Functional Relationships(s)
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1 Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens
2 Substitution of V20 by G in the consensus element G18HVDHGK24 of EF-Tu (referred to as EF-TuG20) strongly influences the interaction with GDP as well as the GTPase activity [Jacquet, E. & Parmeggiani, A. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens
3 Substitution of V20 by G in the consensus element G18HVDHGK24 of EF-Tu (referred to as EF-TuG20) strongly influences the interaction with GDP as well as the GTPase activity [Jacquet, E. & Parmeggiani, A. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens
4 Remarkably, EF-TuG20.GDP can support the enzymatic binding of aminoacyl-tRNA to ribosome.mRNA at low MgCl2 concentration, an effect that with wild-type EF-Tu can only occur in the presence of kirromycin. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens
5 Remarkably, EF-TuG20.GDP can support the enzymatic binding of aminoacyl-tRNA to ribosome.mRNA at low MgCl2 concentration, an effect that with wild-type EF-Tu can only occur in the presence of kirromycin. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens
6 Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. Guanosine Diphosphate Tu translation elongation factor, mitochondrial Homo sapiens