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.

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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.

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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.

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