Document Detail


Quantitation of (a)symmetric inheritance of functional and of oxidatively damaged mitochondrial aconitase in the cell division of old yeast mother cells.
MedLine Citation:
PMID:  20382214     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Asymmetric segregation of oxidatively damaged proteins is discussed in the literature as a mechanism in cell division cycles which at the same time causes rejuvenation of the daughter cell and aging of the mother cell. This process must be viewed as cooperating with the cellular degradation processes like autophagy, proteasomal degradation and others. Together, these two mechanisms guarantee survival of the species and prevent clonal senescence of unicellular organisms, like yeast. It is widely believed that oxidative damage to proteins is primarily caused by oxygen radicals and their follow-up products produced in the mitochondria. As we have shown previously, old yeast mother cells in contrast to young cells contain reactive oxygen species and undergo programmed cell death. Here we show that aconitase of the mitochondrial matrix is readily inactivated by oxidative stress, but even in its inactive form is relatively long-lived and retains fluorescence in the Aco1p-eGFP form. The fluorescent protein is distributed between old mothers and their daughters approximately corresponding to the different sizes of mother and daughter cells. However, the remaining active enzyme is primarily inherited by the daughter cells. This indicates that asymmetric distribution of the still active enzyme takes place and a mechanism for discrimination between active and inactive enzyme must exist. As the aconitase remains mitochondrial during aging and cell division, our findings could indicate discrimination between active and no longer active mitochondria during the process.
Authors:
Harald Klinger; Mark Rinnerthaler; Yuen T Lam; Peter Laun; Gino Heeren; Andrea Klocker; Birgit Simon-Nobbe; J Richard Dickinson; Ian W Dawes; Michael Breitenbach
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-08
Journal Detail:
Title:  Experimental gerontology     Volume:  45     ISSN:  1873-6815     ISO Abbreviation:  Exp. Gerontol.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-06-01     Completed Date:  2010-09-14     Revised Date:  2011-04-06    
Medline Journal Info:
Nlm Unique ID:  0047061     Medline TA:  Exp Gerontol     Country:  England    
Other Details:
Languages:  eng     Pagination:  533-42     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Cell Biology, Division of Genetics, University of Salzburg, Hellbrunnerstrasse 34, Salzburg, Austria.
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MeSH Terms
Descriptor/Qualifier:
Aconitate Hydratase / genetics,  metabolism*
Apoptosis
Base Sequence
Cell Division / genetics,  physiology*
DNA Primers / genetics
Genes, Fungal
Green Fluorescent Proteins / genetics,  metabolism
Microscopy, Fluorescence
Mitochondria / metabolism*
Mitosis
Oxidative Stress
Reactive Oxygen Species / metabolism
Recombinant Fusion Proteins / genetics,  metabolism
Saccharomyces cerevisiae / cytology*,  genetics,  metabolism*
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
S 9302-B18//Austrian Science Fund FWF
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Reactive Oxygen Species; 0/Recombinant Fusion Proteins; 0/Saccharomyces cerevisiae Proteins; 0/enhanced green fluorescent protein; 147336-22-9/Green Fluorescent Proteins; EC 4.2.1.3/Aconitate Hydratase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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