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Protein metabolism

How the proteasome adapts to stress

Nature Reviews Molecular Cell Biology volume 15, pages 562–563 (2014)Cite this article

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It is known that the expression of proteasome subunits increases in response to stress and that this is dependent on the accumulation of the transcription factor Rnp4. However, it is unclear how the subunits assemble into a functional proteasome under stress conditions. In a screen to identify factors that rescue the growth defects of a yeast thermosensitive mutant (cim3-1) that carries a mutation in the Rpt6 proteasome regulatory subunit, the authors isolated the previously uncharacterized ADC17 gene.

Each active 26S proteasome comprises a core particle (CP) bound to one or two regulatory particles (RPs). At restrictive temperatures, cim3-1-mutant strains showed low levels of Rpt6 and proteasome abnormalities with almost complete loss of CP–RP complexes. Overexpression of ADC17 rescued these defects, whereas deletion of ADC17 aggravated them, which suggests that Adc17 is important for proteasome integrity.

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References

  1. Hanssum, A. et al. An inducible chaperone adapts proteasome assembly to stress. Mol. Cell http://dx.doi.org/10.1016/j.molcel.2014.06.017 (2014)

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  1. Kim Baumann
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Bhattacharyya, S. et al. Regulated protein turnover: snapshots of the proteasome in action. Nature Rev. Mol. Cell Biol. 15, 122–133 (2014)

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Baumann, K. How the proteasome adapts to stress. Nat Rev Mol Cell Biol 15, 562–563 (2014). https://doi.org/10.1038/nrm3855

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