Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
Abstract
Peptidyl transferase, the ribosomal activity responsible for catalysis of peptide bond formation, is resistant to vigorous procedures that are conventionally employed to remove proteins from protein-nucleic acid complexes. When the "fragment reaction" was used as a model assay for peptide bond formation, Escherichia coli ribosomes or 50 S subunits retained 20 to 40 percent activity after extensive treatment with proteinase K and SDS, but lost activity after extraction with phenol or exposure to EDTA. Ribosomes from the thermophilic eubacterium Thermus aquaticus remained more than 80 percent active after treatment with proteinase K and SDS, which was followed by vigorous extraction with phenol. This activity is attributable to peptidyl transferase, as judged by specific inhibition by the peptidyl transferase-specific antibiotics chloramphenicol and carbomycin. In contrast, activity is abolished by treatment with ribonuclease T1. These findings support the possibility that 23 S ribosomal RNA participates in the peptidyl transferase function.
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The fact that the peptidyl transferase at the center of modern ribosomes is still a ribozyme provides support for an early role of RNA catalysis.
“The fact that the peptidyl transferase at the center of modern ribosomes is still a ribozyme provides support for an early role of RNA catalysis [119,120,121].”
From Opinion: The Key Steps in the Origin of Life to the Formation of the Eukaryotic Cell (2024) · cites this paper as [119]
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“The fact that the peptidyl transferase at the center of modern ribosomes is still a ribozyme provides support for an early role of RNA catalysis [119–121].”
Background
- Authors
- Noller, H. F., Hoffarth, V., & Zimniak, L.
- Affiliations
- University of California, Santa Cruz (US)
- ORCID
- Noller, Harry F.
- Venue
- Science
- Published
- 1992-06-05
- Volume
- 256
- Issue
- 5062
- Pages
- 1416-1419
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1989794771
- Cited by
- 728
- References
- 2
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 10 · 2023: 5 · 2022: 10 · 2021: 17 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 14 · 2016: 13 · 2015: 13 · 2014: 20 · 2013: 12 · 2012: 21
- FWCI
- 22.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-17129)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Keywords
- peptidyl transferase, ribosome, protein extraction, protein-nucleic acid complexes, peptide bond formation, 50S ribosomal subunit, Thermus aquaticus, ribosomal RNA, 23S rRNA, chloramphenicol, carbomycin, ribonuclease T1, proteinase K, SDS, phenol extraction, EDTA
- MeSH terms
- Electrophoresis, Polyacrylamide Gel, Escherichia coli, Molecular Weight, Peptidyl Transferases, Puromycin, Ribosomes, RNA, Ribosomal, 23S, Sulfur Radioisotopes, Thermus, Macromolecular Substances
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