Identification of a soluble protein that stimulates peptide bond synthesis.
- 1 November 1975
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (11), 4257-4260
- https://doi.org/10.1073/pnas.72.11.4257
Abstract
A soluble protein factor was isolated, free of elongation factor (EF)-T and EF-G, based on its ability to stimulate the synthesis of peptide bonds using ribosomal bound 70S-AUG-N-formyl-[35S]methionyl-tRNA complex and added puromycin as substrates. Over 90% of this activity was found in the ribosome-free cytoplasm of Escherichia coli extracts. Otherfeatures such as molecular weight, purification properties, and catalytic activities distinguish this factor from ribosomal proteins and known activators of translation. The factor requires all components needed for peptide bond synthesis and is inhibited by antibiotics known to specifically block the peptidyl transferase activity of ribosomes. The factor increases the binding affinity of the ribosome for the aminoacyl-tRNA analog puromycin about 10-fold. We suggest that this extraribosomal factor modulates the intrinsic activity of ribosomes to catalyze peptide-bond synthesis, and regard it as a new factor required for peptide chain elongation, which we call EF-P.Keywords
This publication has 17 references indexed in Scilit:
- Occurrence of initiation factor 2 in the postribosomal fraction and identification of an initiation inhibitor as elongation factor GArchives of Biochemistry and Biophysics, 1974
- Inhibition of Polypeptide Chain Initiation in Escherichia coli by Elongation Factor GProceedings of the National Academy of Sciences, 1974
- Enhancement of peptidyl transferase activity by antibiotics acting on the 50 S ribosomal subunitJournal of Molecular Biology, 1974
- Isolation of a Soluble Factor Needed for Protein Synthesis with Various Messenger Ribonucleic Acids Other Than Poly(U)Journal of Biological Chemistry, 1974
- Elongation Factor T Altered in a Temperature-sensitive Escherichia coli MutantNature New Biology, 1973
- Mechanism of polypeptide chain termination. Translation of tandem amber termination codons by an amber suppressor transfer ribonucleic acid.1972
- Peptidyl-Puromycin Synthesis on Polyribosomes from Escherichia coliProceedings of the National Academy of Sciences, 1972
- The reactions of the sulfhydryl groups on the elongation factors Tu and TsArchives of Biochemistry and Biophysics, 1971
- Mutants of Escherichia coli blocked in Protein Synthesis: Mutants with an Altered G FactorPublished by Cold Spring Harbor Laboratory ,1969
- The Peptidyl Transferase Activity of RibosomesCold Spring Harbor Symposia on Quantitative Biology, 1969