title: How many EF-Tu molecules participate in aminoacyl-tRNA binding?
abstract: The stoichiometry of the EF-Tu-GTP-aminoacyl-tRNA complex has been re-determined by a variety of methods, viz gel filtrations, fluorescence titrations, as well as hydrolysis and RNase protection experiments. The results of these experiments clearly demonstrate that one aminoacyl-tRNA interacts with only one EF-Tu-GTP molecule, in agreement with the established view and in contrast to the recently published results by Ehrenberg et al [6].
authors.affiliation: Abteilung Biophysikalische Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Germany.
authors.forename: K
authors.initials: K
authors.lastname: Bensch
authors.forename: U
authors.initials: U
authors.lastname: Pieper
authors.forename: G
authors.initials: G
authors.lastname: Ott
authors.forename: N
authors.initials: N
authors.lastname: Schirmer
authors.forename: M
authors.initials: M
authors.lastname: Sprinzl
authors.forename: A
authors.initials: A
authors.lastname: Pingoud
mesh_terms: D001665:Binding Sites; D002850:Chromatography, Gel; D004926:Escherichia coli / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism; D012260:Ribonucleases; D013050:Spectrometry, Fluorescence
chemical_list: D012346:RNA, Transfer, Amino Acyl; D012360:RNA, Transfer, Phe; D006160:Guanosine Triphosphate; D012260:Ribonucleases; D010444:Peptide Elongation Factor Tu