Document Detail


Mitochondrial quality control during inheritance is associated with lifespan and mother-daughter age asymmetry in budding yeast.
MedLine Citation:
PMID:  21726403     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fluorescence loss in photobleaching experiments and analysis of mitochondrial function using superoxide and redox potential biosensors revealed that mitochondria within individual yeast cells are physically and functionally distinct. Mitochondria that are retained in mother cells during yeast cell division have a significantly more oxidizing redox potential and higher superoxide levels compared to mitochondria in buds. Retention of mitochondria with more oxidizing redox potential in mother cells occurs to the same extent in young and older cells and can account for the age-associated decline in total cellular mitochondrial redox potential in yeast as they age from 0 to 5 generations. Deletion of Mmr1p, a member of the DSL1 family of tethering proteins that localizes to mitochondria at the bud tip and is required for normal mitochondrial inheritance, produces defects in mitochondrial quality control and heterogeneity in replicative lifespan (RLS). Long-lived mmr1Δ cells exhibit prolonged RLS, reduced mean generation times, more reducing mitochondrial redox potential and lower mitochondrial superoxide levels compared to wild-type cells. Short-lived mmr1Δ cells exhibit the opposite phenotypes. Moreover, short-lived cells give rise exclusively to short-lived cells, while the majority of daughters of long-lived cells are long lived. These findings support the model that the mitochondrial inheritance machinery promotes retention of lower-functioning mitochondria in mother cells and that this process contributes to both mother-daughter age asymmetry and age-associated declines in cellular fitness.
Authors:
José Ricardo McFaline-Figueroa; Jason Vevea; Theresa C Swayne; Chun Zhou; Christopher Liu; Galen Leung; Istvan R Boldogh; Liza A Pon
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Publication Detail:
Type:  Journal Article; Research Support, American Recovery and Reinvestment Act; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-08-07
Journal Detail:
Title:  Aging cell     Volume:  10     ISSN:  1474-9726     ISO Abbreviation:  Aging Cell     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-09-14     Completed Date:  2012-01-09     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  101130839     Medline TA:  Aging Cell     Country:  England    
Other Details:
Languages:  eng     Pagination:  885-95     Citation Subset:  IM    
Copyright Information:
© 2011 The Authors. Aging Cell © 2011 Blackwell Publishing Ltd/Anatomical Society of Great Britain and Ireland.
Affiliation:
Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
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MeSH Terms
Descriptor/Qualifier:
Cell Division
Fluorescence
Genes, Mitochondrial
Mitochondria / genetics,  metabolism,  physiology*
Mitochondrial Proteins / genetics,  metabolism
Mutation
Oxidation-Reduction
Photobleaching
Recombinant Fusion Proteins / metabolism
Saccharomyces cerevisiae / genetics,  metabolism,  physiology*
Saccharomyces cerevisiae Proteins / metabolism*
Silent Information Regulator Proteins, Saccharomyces cerevisiae / metabolism
Sirtuin 2 / metabolism
Superoxides / metabolism
Time Factors
Grant Support
ID/Acronym/Agency:
1 F31 AG034835/AG/NIA NIH HHS; 1S10RR025686/RR/NCRR NIH HHS; 5 P30 CA13696/CA/NCI NIH HHS; GM45735/GM/NIGMS NIH HHS; GM45735S1/GM/NIGMS NIH HHS; R01 GM045735/GM/NIGMS NIH HHS; R01 GM045735-13/GM/NIGMS NIH HHS; R01 GM045735-14/GM/NIGMS NIH HHS; R01 GM045735-15/GM/NIGMS NIH HHS; R01 GM045735-15S1/GM/NIGMS NIH HHS; R01 GM096445/GM/NIGMS NIH HHS; R01 GM096445-01/GM/NIGMS NIH HHS; R01 GM096445-02/GM/NIGMS NIH HHS; S10 RR025686/RR/NCRR NIH HHS; S10 RR025686-01A1/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/DSL1 protein, S cerevisiae; 0/Mitochondrial Proteins; 0/Recombinant Fusion Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Silent Information Regulator Proteins, Saccharomyces cerevisiae; 11062-77-4/Superoxides; EC 3.5.1.-/SIR2 protein, S cerevisiae; EC 3.5.1.-/Sirtuin 2
Comments/Corrections

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