Unusual resistance of peptidyl transferase to protein extraction procedures - PubMed (original) (raw)

. 1992 Jun 5;256(5062):1416-9.

doi: 10.1126/science.1604315.

Affiliations

• PMID: 1604315
• DOI: 10.1126/science.1604315

Unusual resistance of peptidyl transferase to protein extraction procedures

H F Noller et al. Science. 1992.

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 50S 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 23S ribosomal RNA participates in the peptidyl transferase function.

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Comment in

• Finding RNA makes proteins gives 'RNA world' a big boost.
  Waldrop MM. Waldrop MM. Science. 1992 Jun 5;256(5062):1396-7. doi: 10.1126/science.1376495. Science. 1992. PMID: 1376495 No abstract available.
• New horizons for RNA catalysis.
  Pace NR. Pace NR. Science. 1992 Jun 5;256(5062):1402-3. doi: 10.1126/science.1376496. Science. 1992. PMID: 1376496 No abstract available.

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