Cargando…
A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis
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...
Autores principales: | , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9845386/ https://www.ncbi.nlm.nih.gov/pubmed/36650210 http://dx.doi.org/10.1038/s42003-023-04428-7 |
_version_ | 1784870896099393536 |
---|---|
author | Hoernstein, Sebastian N. W. Özdemir, Buğra van Gessel, Nico Miniera, Alessandra A. Rogalla von Bieberstein, Bruno Nilges, Lars Schweikert Farinha, Joana Komoll, Ramona Glauz, Stella Weckerle, Tim Scherzinger, Friedrich Rodriguez‐Franco, Marta Müller-Schüssele, Stefanie J. Reski, Ralf |
author_facet | Hoernstein, Sebastian N. W. Özdemir, Buğra van Gessel, Nico Miniera, Alessandra A. Rogalla von Bieberstein, Bruno Nilges, Lars Schweikert Farinha, Joana Komoll, Ramona Glauz, Stella Weckerle, Tim Scherzinger, Friedrich Rodriguez‐Franco, Marta Müller-Schüssele, Stefanie J. Reski, Ralf |
author_sort | Hoernstein, Sebastian N. W. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9845386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98453862023-01-19 A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis Hoernstein, Sebastian N. W. Özdemir, Buğra van Gessel, Nico Miniera, Alessandra A. Rogalla von Bieberstein, Bruno Nilges, Lars Schweikert Farinha, Joana Komoll, Ramona Glauz, Stella Weckerle, Tim Scherzinger, Friedrich Rodriguez‐Franco, Marta Müller-Schüssele, Stefanie J. Reski, Ralf Commun Biol Article 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. Nature Publishing Group UK 2023-01-17 /pmc/articles/PMC9845386/ /pubmed/36650210 http://dx.doi.org/10.1038/s42003-023-04428-7 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Hoernstein, Sebastian N. W. Özdemir, Buğra van Gessel, Nico Miniera, Alessandra A. Rogalla von Bieberstein, Bruno Nilges, Lars Schweikert Farinha, Joana Komoll, Ramona Glauz, Stella Weckerle, Tim Scherzinger, Friedrich Rodriguez‐Franco, Marta Müller-Schüssele, Stefanie J. Reski, Ralf A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title | A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title_full | A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title_fullStr | A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title_full_unstemmed | A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title_short | A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis |
title_sort | deeply conserved protease, acylamino acid-releasing enzyme (aare), acts in ageing in physcomitrella and arabidopsis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9845386/ https://www.ncbi.nlm.nih.gov/pubmed/36650210 http://dx.doi.org/10.1038/s42003-023-04428-7 |
work_keys_str_mv | AT hoernsteinsebastiannw adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT ozdemirbugra adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT vangesselnico adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT minieraalessandraa adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT rogallavonbiebersteinbruno adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT nilgeslars adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT schweikertfarinhajoana adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT komollramona adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT glauzstella adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT weckerletim adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT scherzingerfriedrich adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT rodriguezfrancomarta adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT mullerschusselestefaniej adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT reskiralf adeeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT hoernsteinsebastiannw deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT ozdemirbugra deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT vangesselnico deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT minieraalessandraa deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT rogallavonbiebersteinbruno deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT nilgeslars deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT schweikertfarinhajoana deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT komollramona deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT glauzstella deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT weckerletim deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT scherzingerfriedrich deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT rodriguezfrancomarta deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT mullerschusselestefaniej deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis AT reskiralf deeplyconservedproteaseacylaminoacidreleasingenzymeaareactsinageinginphyscomitrellaandarabidopsis |