TY  - INPR
A1  - Hoernstein, Sebastian
A1  - Özdemir, Buğra
A1  - Gessel, Nico
A1  - Miniera, Alessandra A.
A1  - Rogalla von Bieberstein, Bruno
A1  - Nilges, Lars
A1  - Schweikert Farinha, Joana
A1  - Komoll, Ramona
A1  - Glauz, Stella
A1  - Weckerle, Tim
A1  - Scherzinger, Friedrich
A1  - Rodríguez-Franco, Marta
A1  - Müller-Schüssele, Stefanie J.
A1  - Reski, Ralf
T1  - A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in 2 Physcomitrella and Arabidopsis
T2  - bioRxiv
N2  - Reactive oxygen species (ROS) are constant by-products of aerobic life. In excess, ROS lead to cytotoxic protein aggregates, which are a hallmark of ageing in animals and linked to age-related pathologies in humans. Acylamino acid-releasing enzymes (AARE) are bifunctional serine proteases, acting on oxidized proteins. AARE are found in all domains of life, albeit under different names, such as acylpeptide hydrolase (APEH/ACPH), acylaminoacyl peptidase (AAP), or oxidized protein hydrolase (OPH). In humans, AARE malfunction is associated with age-related pathologies, while their function in plants is less clear. Here, we provide a detailed analysis of AARE genes in the plant lineage and an in-depth analysis of AARE localization and function in the moss Physcomitrella and the angiosperm Arabidopsis. AARE loss-of-function mutants have not been described for any organism so far. We generated and analysed such mutants and describe a connection between AARE function, aggregation of oxidized proteins and plant ageing, including accelerated developmental progression and reduced life span. Our findings complement similar findings in animals and humans, and suggest a unified concept of ageing may exist in different life forms.
Y1  - 2022
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/85844
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-858441
UR  - https://www.biorxiv.org/content/10.1101/2022.05.18.492440v3
IS  - 2022.05.18.492440 Version 3
PB  - bioRxiv
ER  -