Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity.
The function of His118 in elongation factor (EF)-Tu from Escherichia coli was investigated by its substitution with glycine. The substitution had a differential effect on individual functions of the protein. The affinity for aminoacyl (aa)-tRNA and the intrinsic GTPase activity of the mutant EF-Tu were decreased whereas the response of its GTPase center to aa-tRNA was strongly increased. These results suggest that the region around His118 is involved in the binding of aa-tRNA and in the transmission of a turn-off signal generated by the interaction with aa-tRNA and directed to the GTPase center of EF-Tu.
Jonák
J
J
Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague.
Anborgh
P H
PH
Parmeggiani
A
A
D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000378:metabolism; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006639:Histidine / Q000032:analysis / Q000378:metabolism*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D010649:Phenylalanine / Q000096:biosynthesis; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D011817:Rabbits
D009838:Oligodeoxyribonucleotides; D012346:RNA, Transfer, Amino Acyl; D006153:Guanosine Diphosphate; D010649:Phenylalanine; D006639:Histidine; D006160:Guanosine Triphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D010444:Peptide Elongation Factor Tu