TY  - JOUR
A1  - Warnsmann, Verena
A1  - Meisterknecht, Jana
A1  - Wittig, Ilka
A1  - Osiewacz, Heinz D.
T1  - Aging of podospora anserina leads to alterations of OXPHOS
and the induction of non-mitochondrial salvage pathways
T2  - Cells
N2  - The accumulation of functionally impaired mitochondria is a key event in aging. Previous works with the fungal aging model Podospora anserina demonstrated pronounced age-dependent changes of mitochondrial morphology and ultrastructure, as well as alterations of transcript and protein levels, including individual proteins of the oxidative phosphorylation (OXPHOS). The identified protein changes do not reflect the level of the whole protein complexes as they function in-vivo. In the present study, we investigated in detail the age-dependent changes of assembled mitochondrial protein complexes, using complexome profiling. We observed pronounced age-depen-dent alterations of the OXPHOS complexes, including the loss of mitochondrial respiratory supercomplexes (mtRSCs) and a reduction in the abundance of complex I and complex IV. Additionally, we identified a switch from the standard complex IV-dependent respiration to an alternative respiration during the aging of the P. anserina wild type. Interestingly, we identified proteasome components, as well as endoplasmic reticulum (ER) proteins, for which the recruitment to mitochondria appeared to be increased in the mitochondria of older cultures. Overall, our data demonstrate pronounced age-dependent alterations of the protein complexes involved in energy transduction and suggest the induction of different non-mitochondrial salvage pathways, to counteract the age-dependent mitochondrial impairments which occur during aging.
KW  - Podospora anserina
KW  - aging
KW  - OXPHOS
KW  - complexome profiling
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/69293
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-692939
SN  - 2073-4409
N1  - This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) Os75/17-2 to H.D.O. and Wi3728/1-1 to I.W.
N1  - Data Availability Statement
The complexome profiling data are available in ProteomeXchange (http://www.proteomexchange.org/) via the PRIDE [138] partner repository with the identifiers PXD029352.
VL  - 10
IS  - 12, art. 3319
SP  - 1
EP  - 19
PB  - MDPI
CY  - Basel
ER  -