WFRF:(Fink Matthias J. 1988 )
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The heat shock protein LarA activates the Lon protease in response to proteotoxic stress
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- Omnus, Deike J., 1981- (author)
- Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut,Science for Life Laboratory (SciLifeLab),Uppsala University, Sweden,Stockholm Univ, Wenner Gren Inst, Sci Life Lab, Svante Arrhenius Vag 20C, S-10691 Stockholm, Sweden.;Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, Svante Arrhenius vag 20C, S-10691 Stockholm, Sweden.
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- Fink, Matthias J., 1988- (author)
- Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut,Science for Life Laboratory (SciLifeLab),Uppsala University, Sweden,Stockholm Univ, Wenner Gren Inst, Sci Life Lab, Svante Arrhenius Vag 20C, S-10691 Stockholm, Sweden.;Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, Svante Arrhenius vag 20C, S-10691 Stockholm, Sweden.
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- Kallazhi, Aswathy, 1992- (author)
- Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut,Science for Life Laboratory (SciLifeLab),Stockholm Univ, Wenner Gren Inst, Sci Life Lab, Svante Arrhenius Vag 20C, S-10691 Stockholm, Sweden.;Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, Svante Arrhenius vag 20C, S-10691 Stockholm, Sweden.
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- Springer Nature, 2023
- 2023
- English.
- In: Nature Communications. - : Springer Nature. - 2041-1723. ; 14
- Journal article (peer-reviewed)
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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