Selective protein degradation: a journey's end within the proteasome

Article Abstract:

The ubiquitin/proteasome proteolytic system is capable of degrading all proteins in a controlled manner. Proteins probably contain degradation signal analogues which help the proteasome system identify the proteins which need to be degraded. Proteins containing multiubiquitin chains are degraded into small peptides. The location of the beta-subunits in the proteasome cavity prevents the controlled lysis of proteins. The rate of protein lysis and the size of the peptides formed can be changed by changing these beta subunits. The proteasome system also processes precursors into mature antigens.

Observations, Proteases

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Yeast Hct1 is a regulator of Clb2 cyclin proteolysis

Article Abstract:

A study shows that the conserved eukaryote protein, yeast Hct1, is vital component to the proteolysis pathway. Proteolytic substrates such as G1 cyclins were found to be short-lived and Clb2 was found to cause DNA replication in hct1 mutants. Results indicate that cyclin-dependent kinase inhibition may reduce the adverse effects of cyclin proteolysis defects. Hct1 and related Cdc20 may also act as substrate-specific proteolysis regulators during mitosis.

Genetic regulation, Mitosis, Proteolytic enzyme genes

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein

Article Abstract:

A study was conducted to investigate the two activities of the heat shock protein DegP and their temperature-dependent switch. Results indicate the DegP performs general molecular chaperone activity at low temperatures, which induces protein refolding of chemically denatured substrates. It was also observed that in elevated temperatures, refolding is suppressed and DegP has shifted to performing proteolytic activity.

Physiological aspects, Heat shock proteins, Protein folding, Temperature

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