The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

Article Abstract:

Research has been conducted on bacterial and eukaryotic proteins which are capable of rescuing stress-damaged proteins from an aggregated states. The structure of bacterial protein ClpB has been investigated via the use of X-ray crystallography and cryo-electron microscopy, and the results have revealed the mechanism by which ClpBi mediates the disaggregation of high molecular weight aggregates.

Japan, Usage, Eukaryotes, Protein folding, X-ray crystallography, Bacterial proteins, Molecules, Structure

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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB

Article Abstract:

A ClpB variant, BAP, which associates with the ClpP peptidase and thereby is converted into a degrading disaggregase is engineered in a study. This activity switch of BAP to a degrading disaggregase does not support thermotolerance development, demonstrating that cell survival during severe thermal stress requires reactivation of aggregated proteins.

Science & research, Research, Protein binding, Translocation (Genetics), Thermal stresses, Translocations (Genetics)

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Functional siRNAs and miRNAs exhibit strands bias

Article Abstract:

Research has been conducted on microRNAs. The authors suggest that the thermodynamic properties of these RNAs are critically important for determining the molecules' functions and longevity.

Physiological aspects, Chemical thermodynamics, Gene silencing, RNA interference

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