title: Novel data on interactions of elongation factor Ts.
abstract: Interactions of EF-Ts with EF-Tu at all steps of the elongation cycle were studied by limited trypsinolysis, gel-filtration, analytical centrifugation and fluorescence polarization techniques. It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA.EF-Tu.GTP complex up to GTP hydrolysis stage on the ribosome. The possible role of these interactions is discussed.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
authors.forename: M G
authors.initials: MG
authors.lastname: Bubunenko
authors.forename: M L
authors.initials: ML
authors.lastname: Kireeva
authors.forename: A T
authors.initials: AT
authors.lastname: Gudkov
mesh_terms: D001665:Binding Sites; D002498:Centrifugation; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005454:Fluorescence Polarization; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
chemical_list: D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu