LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding

Chun-Shik Shin, Shuxia Meng, Spiros D. Garbis, Annie Moradian, Robert W. Taylor, Michael J. Sweredoski, Brett Lomenick and David C. Chan ()
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Chun-Shik Shin: California Institute of Technology
Shuxia Meng: California Institute of Technology
Spiros D. Garbis: California Institute of Technology
Annie Moradian: California Institute of Technology
Robert W. Taylor: Newcastle University
Michael J. Sweredoski: California Institute of Technology
Brett Lomenick: California Institute of Technology
David C. Chan: California Institute of Technology

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract Most mitochondrial precursor polypeptides are imported from the cytosol into the mitochondrion, where they must efficiently undergo folding. Mitochondrial precursors are imported as unfolded polypeptides. For proteins of the mitochondrial matrix and inner membrane, two separate chaperone systems, HSP60 and mitochondrial HSP70 (mtHSP70), facilitate protein folding. We show that LONP1, an AAA+ protease of the mitochondrial matrix, works with the mtHSP70 chaperone system to promote mitochondrial protein folding. Inhibition of LONP1 results in aggregation of a protein subset similar to that caused by knockdown of DNAJA3, a co-chaperone of mtHSP70. LONP1 is required for DNAJA3 and mtHSP70 solubility, and its ATPase, but not its protease activity, is required for this function. In vitro, LONP1 shows an intrinsic chaperone-like activity and collaborates with mtHSP70 to stabilize a folding intermediate of OXA1L. Our results identify LONP1 as a critical factor in the mtHSP70 folding pathway and demonstrate its proposed chaperone activity.

Date: 2021
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DOI: 10.1038/s41467-020-20597-z

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