The isolation and characterization of elongation factor eEF-Ts from Krebs-II mouse-ascites-tumor cells and its role in the elongation process.

Abstract

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.

• Authors: H Grasmuk, R D Nolan, J Drews
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 92 Issue 2 Pg. 479-90 (Dec 1978) ISSN: 0014-2956 [Print] England
• PMID: 738276 (Publication Type: Journal Article)

Chemical References

• Peptide Elongation Factors
• Guanosine Diphosphate
• Poly U
• Guanylyl Imidodiphosphate
• Phenylalanine
• Guanosine Triphosphate
• RNA, Transfer

Topics

• Animals
• Carcinoma, Krebs 2 (metabolism)
• Cells, Cultured
• Guanosine Diphosphate (metabolism)
• Guanosine Triphosphate (metabolism)
• Guanylyl Imidodiphosphate (pharmacology)
• Mice
• Molecular Weight
• Peptide Biosynthesis
• Peptide Elongation Factors (isolation & purification, metabolism)
• Phenylalanine (metabolism)
• Poly U (metabolism)
• RNA, Transfer (metabolism)
• Ribosomes (metabolism)