Measurement of Internal Movements within the 30 S Ribosomal Subunit Using Förster Resonance Energy Transfer
| Autor: | Harry F. Noller, Robyn P. Hickerson, Albion E. Baucom, Robert M. Clegg, Zigurts K. Majumdar |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Ribosomal Proteins Binding Sites Protein Conformation Cryo-electron microscopy Protein subunit Energy transfer Cryoelectron Microscopy Ribosomal RNA Biology Crystallography X-Ray Ribosome Crystallography Förster resonance energy transfer Structural Biology Ribosomal protein Escherichia coli Fluorescence Resonance Energy Transfer Ribosomes Molecular Biology |
| Zdroj: | Journal of Molecular Biology. 354:459-472 |
| ISSN: | 0022-2836 |
| Popis: | We have used Förster resonance energy transfer (FRET) to study specific conformational changes in the Escherichia coli 30 S ribosomal subunit that occur upon association with the 50 S subunit. By measuring energy transfer between 13 different pairs of fluorescent probes attached to specific positions on 30 S subunit proteins, we have monitored changes in distance between different locations within the 30 S subunit in its free and 50 S-bound states. The measured distance changes provide restraints for modeling the movement that occurs within the 30 S subunit upon formation of the 70 S ribosome in solution. Treating the head, body, and platform domains of the 30 S subunit as simple rigid bodies, the lowest-energy solution converges on a model that satisfies each of the individual FRET restraints. In this model, the 30 S subunit head tilts towards the 50 S subunit, similar to the movement found in comparing 30 S subunits and 70 S ribosomes from X-ray and cryo-electron microscope structures, and the platform is predicted to undergo a clock-wise rotation upon association. |
| Databáze: | OpenAIRE |
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