Related Experiment Video
Updated: Jun 18, 2026

In Vitro Reassociation Assay to Measure the Formation of 80S Ribosomal Particles Using Salt-washed Ribosomal Subunits
Published on: December 16, 2025
Ribosome reactivation by replacement of damaged proteins
Arto Pulk1, Aivar Liiv, Lauri Peil
1Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Abstract:
Ribosomal functions are vital for all organisms. Bacterial ribosomes are stable 2.4 MDa particles composed of three RNAs and over 50 different proteins. Accumulating damage to ribosomal RNA or proteins can disturb ribosome functioning. Organisms could benefit from degrading or possibly repairing inactive or partially active ribosomes. Reactivation of chemically damaged ribosomes by a process of protein replacement was studied in vitro. Ribosomes were inactivated by chemical modification of Cys residues. Incubation of modified ribosomes with total ribosomal proteins led to reactivation of translational activity. Intriguingly, ribosomal proteins extracted by LiCl are equally active in the restoration of ribosome function. Incubation of 70S ribosomes with isotopically labelled r-proteins followed by separation of ribosomes was used to identify exchangeable proteins. A similar set of proteins was found to be exchanged in vivo under stress conditions in the stationary phase. We propose that repair of damaged ribosomes might be an important mechanism for maintaining protein synthesis activity following chemical damage.
Related Concept Videos
Coordination of Gene Expression Processes in Bacteria
The Unfolded Protein Response
Improving Translational Accuracy
Regulation of the Unfolded Protein Response
Bacterial Protein Maturation
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA molecules by RNA...

