Reconstruction of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16.

R M Baxter, M C Ganoza, N Zahid, D G Chung

European journal of biochemistry / FEBS 1987 Mar 16

filter terms:

Ribosomal protein L16 was digested with Staphylococcus aureus protease V8 and the resulting peptides were separated by reversed-phase high-performance liquid chromatography. One of the fragments, identified by sequence analysis as the N-terminal peptide of L16, was shown to exhibit partial peptide-bond-formation and transesterification activities of peptidyltransferase upon reconstitution with L16-depleted 50S core particles. However, several proteins enhanced these activities. L15 increased both reactions when added to the reconstitution mixture, suggesting a limited capacity of the L16 peptide to incorporate into 50S core particles. In contrast, the interaction of L11 with the N-terminal peptide stimulated the transesterification reaction but not the peptide-bond-forming activity of ribosomes, indicating a different topological domain for these reactions. Also, EF-P, a soluble protein which reconstructs the peptide-bond formation and transesterification reactions on 70S ribosomes, stimulated both peptidyltransferase activities exhibited by the L16 N-terminal peptide.

Citation

R M Baxter, M C Ganoza, N Zahid, D G Chung. Reconstruction of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16. European journal of biochemistry / FEBS. 1987 Mar 16;163(3):473-9