The isolation and characterization of elongation factor eEF-Ts from Krebs-II mouse-ascites-tumor cells and its role in the elongation process.
A factor having activity similar to that described in other systems for the eukaryotic elongation factor eEF-Ts was isolated from the heavy, aggregate form of eEF-TH (formally named EF-1H). This protein has a molecular weight of 52000 under native conditions and of 25500 under denaturing conditions. It has been shown to stimulate eEF-Tu-dependent aminoacyl-tRNA binding to ribosomes and therefore eEF-Tu/eEF-G-dependent polyphenylalanine synthesis by ribosomes and was found to stimulate GDP-GTP exchange in eEF-Tu . GDP complexes. In the course of this work, it was also demonstrated that the removal of deacylated tRNA from the ribosome is a GTP-dependent process. This report, therefore, adds further support to the concept that a third elongation factor, eEF-Ts, may be common to all systems in the eukaryotic domain.
D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000378:metabolism*; D002478:Cells, Cultured; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D051379:Mice; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D010445:Peptide Elongation Factors / Q000302:isolation & purification / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism; D011072:Poly U / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D010445:Peptide Elongation Factors; D006153:Guanosine Diphosphate; D011072:Poly U; D006165:Guanylyl Imidodiphosphate; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D012343:RNA, Transfer