Open AccessPeptide Bond Formation Stimulated by Protein Synthesis Factor EF‐P Depends on the Aminoacyl Moiety of the Acceptor
Author(s) -
GLICK Bernard R.,
CHLÁDEK Stanislav,
GANOZA M. Clelia
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb13081.x
Subject(s) - puromycin , peptide bond , peptidyl transferase , ribosome , moiety , protein biosynthesis , elongation factor , chemistry , stereochemistry , peptide , aminoacyl trna , transferase , biochemistry , enzyme , rna , gene
Elongation factor EF‐P is a soluble protein that stimulates peptide bond synthesis catalyzed by the 50‐S ribosomal subunit. This factor was previously identified and characterized based on its ability to promote the synthesis of formylmethionine‐puromycin. In the present work, we tested the ability of EF‐P to promote peptide bond synthesis between ribosome‐bound fMet‐tRNA and several analogues of the 3′ terminus of aminoacyl‐tRNA, i.e. the cytidylyl(3′‐5′)‐[2′(3′)‐ O ‐ l ‐aminoacyladenosines]. EF‐P promoted synthesis to the greatest extent with certain acceptors which were otherwise inefficient in the peptidyl transferase reaction. This activity of EF‐P could not be replaced by the other soluble proteins known to be involved in polypeptide synthesis, such as EF‐Tu, EF‐Ts and EF‐G. One role of EF‐P in protein synthesis may be to allow peptide bond synthesis to occur more efficiently with some aminoacyl‐tRNAs that are poor acceptors for the ribosomal peptidyl transferase.