Reflections on the 20th anniversary of RNA
- Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
- Corresponding author: zimmermann{at}biochem.umass.edu
This extract was created in the absence of an abstract.
What makes the ribosome tick? Proteins, proteins, proteins, it always seemed to be proteins, ribosomal proteins and a series of nonribosomal protein factors in particular. When I was cutting my molecular biology teeth, excitement centered on the identification, enumeration and characterization of the several dozen bacterial ribosomal proteins by column chromatography, gel electrophoresis, sequencing and biochemical analysis. How many were there? Were there sequences in common? Did they have enzymatic activity? Was one of them, perhaps, peptidyl transferase—the activity responsible for synthesis of the peptide bond? At the time, the role of ribosomal RNA was something of a mystery despite the fact that it comprised two-thirds of the bacterial ribosome mass. The analytical tools required to answer this question were few and far between.
It was established early on that rRNAs were not informational: they were uniform in structure and encoded no proteins. Could they then just serve as a …
