The heat shock protein LarA activates the Lon protease in response to proteotoxic stress

Deike J. Omnus, Matthias J. Fink, Aswathy Kallazhi, Maria Xandri Zaragoza, Axel Leppert, Michael Landreh and Kristina Jonas ()
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Deike J. Omnus: Stockholm University
Matthias J. Fink: Stockholm University
Aswathy Kallazhi: Stockholm University
Maria Xandri Zaragoza: Stockholm University
Axel Leppert: Karolinska Institutet
Michael Landreh: Karolinska Institutet
Kristina Jonas: Stockholm University

Nature Communications, 2023, vol. 14, issue 1, 1-19

Abstract: Abstract The Lon protease is a highly conserved protein degradation machine that has critical regulatory and protein quality control functions in cells from the three domains of life. Here, we report the discovery of a α-proteobacterial heat shock protein, LarA, that functions as a dedicated Lon regulator. We show that LarA accumulates at the onset of proteotoxic stress and allosterically activates Lon-catalysed degradation of a large group of substrates through a five amino acid sequence at its C-terminus. Further, we find that high levels of LarA cause growth inhibition in a Lon-dependent manner and that Lon-mediated degradation of LarA itself ensures low LarA levels in the absence of stress. We suggest that the temporal LarA-dependent activation of Lon helps to meet an increased proteolysis demand in response to protein unfolding stress. Our study defines a regulatory interaction of a conserved protease with a heat shock protein, serving as a paradigm of how protease activity can be tuned under changing environmental conditions.

Date: 2023
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DOI: 10.1038/s41467-023-43385-x

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