Asset Details
Do you wish to reserve the book?
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
Do you wish to request the book?
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
2021
Overview
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.
Most mitochondrial proteins are imported from the cytosol and must fold in the mitochondria. Here, the authors show that the mitochondrial protease LONP1 plays a critical role in the mtHSP70 chaperone system independently of its protease activity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/1
/ 82/58
/ 82/83
/ ATP-Dependent Proteases - metabolism
/ Cytosol
/ Electron Transport Complex IV
/ Folding
/ HSP70 Heat-Shock Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Mitochondrial Proteins - chemistry
/ Mitochondrial Proteins - metabolism
/ Protease
/ Proteins
/ Science
