Protein synthesis by single ribosomes
- FRANCESCO VANZI1,4,
- SERGUEI VLADIMIROV2,
- CHARLOTTE R. KNUDSEN3,
- YALE E. GOLDMAN1, and
- BARRY S. COOPERMAN2
- 1Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6083, USA
- 2Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA
- 3Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
Abstract
The ribosome is universally responsible for synthesizing proteins by translating the genetic code transcribed in mRNA into an amino acid sequence. Ribosomes use cellular accessory proteins, soluble transfer RNAs, and metabolic energy to accomplish the initiation, elongation, and termination of peptide synthesis. In translocating processively along the mRNA template during the elongation cycle, ribosomes act as supramolecular motors. Here we demonstrate that ribosomes adsorbed on a surface, as for mechanical or spectroscopic studies, are capable of polypeptide synthesis and that tethered particle analysis of fluorescent beads connected to ribosomes via polyuridylic acid can be used to estimate the rate of polyphenylalanine synthesis by individual ribosomes. This work opens the way for application of biophysical techniques, originally developed for the classical motor proteins, to the understanding of protein biosynthesis.
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Footnotes
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↵4 Present address: LENS–INFM, University of Florence, Florence, Italy.
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Article and publication are at http://www.rnajournal.org/cgi/doi/10.1261/rna.5800303.
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- Accepted July 9, 2003.
- Received April 30, 2003.
- Copyright 2003 by RNA Society
