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. 1971 Jul;68(7):1474–1478. doi: 10.1073/pnas.68.7.1474

A Translocation-Associated Ribosomal Conformation Change Detected by Hydrogen Exchange and Sedimentation Velocity

De-Maw Chuang 1, Melvin V Simpson 1
PMCID: PMC389221  PMID: 4934519

Abstract

Translocation in ribosomes consists of transposition of peptidyl-tRNA from the aminoacyl to the peptidyl site and, probably concomitantly, the movement of ribosomes on mRNA. Does a conformational change in the ribosome provide the motive force for this process? Hydrogen exchange and sedimentation velocity experiments indicate that the Escherichia coli ribosome does undergo a conformational change associated with translocation. When pretranslocational ribosomes carrying acetyldiphenylalanyl-tRNA in the aminoacyl site were incubated with G factor and GTP, translocation occurred, with a concomitant increase in hydrogen exchange rate and a decrease in sedimentation constant. These changes did not occur when GTP was replaced by a nonhydrolyzable analogue, GDP-CH2-P, and they were blocked by the antibiotics fusidic acid and thiostrepton. When posttranslocational ribosomes were cycled back to the pretranslocational state by T factor, GTP, and phenylalanyl-tRNA, the sedimentation constant reverted to the original value. Whether or not this conformation change drives translocation requires further study.

Keywords: fusidic acid, thiostrepton, 5′-guanylylmethylenediphosphonate

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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