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Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins

Journal article
Authors Sarah Hanzén
Katarina Vielfort
Junsheng Yang
Friederike Roger
Veronica Andersson
Sara Zamarbide-Fores
Rebecca Andersson
Lisa Malm
G. Palais
B. Biteau
Beidong Liu
M. B. Toledano
Mikael Molin
Thomas Nyström
Published in Cell
Volume 166
Issue 1
Pages 140-151
ISSN 0092-8674
Publication year 2016
Published at Institute of Biomedicine
Department of Chemistry and Molecular Biology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 140-151
Language en
Keywords human lung-cancer, saccharomyces-cerevisiae, quality-control, budding, yeast, asymmetric inheritance, genome instability, peroxiredoxin tsa1, hydrogen-peroxide, damaged proteins, oxidative stress, Biochemistry & Molecular Biology, Cell Biology
Subject categories Biological Sciences


Caloric restriction (CR) extends the lifespan of flies, worms, and yeast by counteracting age-related oxidation of H2O2-scavenging peroxiredoxins (Prxs). Here, we show that increased dosage of the major cytosolic Prx in yeast, Tsa1, extends lifespan in an Hsp70 chaperone-dependent and CR-independent manner without increasing H2O2 scavenging or genome stability. We found that Tsa1 and Hsp70 physically interact and that hyperoxidation of Tsa1 by H2O2 is required for the recruitment of the Hsp70 chaperones and the Hsp104 disaggregase to misfolded and aggregated proteins during aging, but not heat stress. Tsa1 counteracted the accumulation of ubiquitinated aggregates during aging and the reduction of hyperoxidized Tsa1 by sulfiredoxin facilitated clearance of H2O2-generated aggregates. The data reveal a conceptually new role for H2O2 signaling in proteostasis and lifespan control and shed new light on the selective benefits endowed to eukaryotic peroxiredoxins by their reversible hyperoxidation.

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