Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants
- Autores
- Balparda, Manuel; Elsasse, Marlene; Badía, Mariana B.; Giese, Jonas; Bovdilova, Anastasiia; Hüdig, Meike; Reinmuth, Lisa; Eirich, Jürgen; Schwarzlander, Markus; Finkemeier, Iris; Schallenberg Rüdinger, Mareike; Maurino, Verónica G.
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Balparda, Manuel. University of Bonn. Molecular Plant Physiology; Alemania
Fil: Elsasse, Marlene. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania
Fil: Elsasse, Marlene. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; Alemania
Fil: Badía, Mariana B. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania
Fil: Badía, Mariana B. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentina
Fil: Giese, Jonas. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania
Fil: Bovdilova, Anastasiia. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania
Fil: Hüdig, Meike. University of Bonn. Molecular Plant Physiology; Alemania
Fil: Hüdig, Meike. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania
Fil: Reinmuth, Lisa. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania
Fil: Eirich, Jürgen. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania
Fil: Schwarzlander, Markus. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; Alemania
Fil: Finkemeier, Iris. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania
Fil: Schallenberg Rüdinger, Mareike. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania
Fil: Maurino, Verónica G. University of Bonn. Molecular Plant Physiology; Alemania
Fil: Maurino, Verónica G. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania
Summary: Plants need to rapidly and flexibly adjust their metabolism to changes of their immediate environment. Since this necessity results from the sessile lifestyle of land plants, key mechanisms for orchestrating central metabolic acclimation are likely to have evolved early. Here, we explore the role of lysine acetylation as a post-translational modification to directly modulate metabolic function. We generated a lysine acetylome of the moss Physcomitrium patens and identified 638 lysine acetylation sites, mostly found in mitochondrial and plastidial proteins. A comparison with available angiosperm data pinpointed lysine acetylation as a conserved regulatory strategy in land plants. Focusing on mitochondrial central metabolism, we functionally analyzed acetylation of mitochondrial malate dehydrogenase (mMDH), which acts as a hub of plant metabolic flexibility. In P. patens mMDH1, we detected a single acetylated lysine located next to one of the four acetylation sites detected in Arabidopsis thaliana mMDH1. We assessed the kinetic behavior of recombinant A. thaliana and P. patens mMDH1 with site-specifically incorporated acetyl-lysines. Acetylation of A. thaliana mMDH1 at K169, K170, and K334 decreases its oxaloacetate reduction activity, while acetylation of P. patens mMDH1 at K172 increases this activity. We found modulation of the malate oxidation activity only in A. thaliana mMDH1, where acetylation of K334 strongly activated it. Comparative homology modeling of MDH proteins revealed that evolutionarily conserved lysines serve as hotspots of acetylation. Our combined analyses indicate lysine acetylation as a common strategy to fine-tune the activity of central metabolic enzymes with likely impact on plant acclimation capacity. - Fuente
- The Plant Journal Vol.109, No,1, 2022
- Materia
-
PLANTAS
ACETILACIÓN DE PROTEINAS
POSTRANSCRIPCIONAL
REGULACION
ACETILACION DE PROTEINAS
MITOCONDRIAS
METABOLISMO
MALATO DESHIDROGENASA - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Pontificia Universidad Católica Argentina
- OAI Identificador
- oai:ucacris:123456789/15419
Ver los metadatos del registro completo
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oai:ucacris:123456789/15419 |
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spelling |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plantsBalparda, ManuelElsasse, MarleneBadía, Mariana B.Giese, JonasBovdilova, AnastasiiaHüdig, MeikeReinmuth, LisaEirich, JürgenSchwarzlander, MarkusFinkemeier, IrisSchallenberg Rüdinger, MareikeMaurino, Verónica G.PLANTASACETILACIÓN DE PROTEINASPOSTRANSCRIPCIONALREGULACIONACETILACION DE PROTEINASMITOCONDRIASMETABOLISMOMALATO DESHIDROGENASAFil: Balparda, Manuel. University of Bonn. Molecular Plant Physiology; AlemaniaFil: Elsasse, Marlene. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; AlemaniaFil: Elsasse, Marlene. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; AlemaniaFil: Badía, Mariana B. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; AlemaniaFil: Badía, Mariana B. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; ArgentinaFil: Giese, Jonas. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; AlemaniaFil: Bovdilova, Anastasiia. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; AlemaniaFil: Hüdig, Meike. University of Bonn. Molecular Plant Physiology; AlemaniaFil: Hüdig, Meike. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; AlemaniaFil: Reinmuth, Lisa. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; AlemaniaFil: Eirich, Jürgen. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; AlemaniaFil: Schwarzlander, Markus. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; AlemaniaFil: Finkemeier, Iris. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; AlemaniaFil: Schallenberg Rüdinger, Mareike. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; AlemaniaFil: Maurino, Verónica G. University of Bonn. Molecular Plant Physiology; AlemaniaFil: Maurino, Verónica G. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; AlemaniaSummary: Plants need to rapidly and flexibly adjust their metabolism to changes of their immediate environment. Since this necessity results from the sessile lifestyle of land plants, key mechanisms for orchestrating central metabolic acclimation are likely to have evolved early. Here, we explore the role of lysine acetylation as a post-translational modification to directly modulate metabolic function. We generated a lysine acetylome of the moss Physcomitrium patens and identified 638 lysine acetylation sites, mostly found in mitochondrial and plastidial proteins. A comparison with available angiosperm data pinpointed lysine acetylation as a conserved regulatory strategy in land plants. Focusing on mitochondrial central metabolism, we functionally analyzed acetylation of mitochondrial malate dehydrogenase (mMDH), which acts as a hub of plant metabolic flexibility. In P. patens mMDH1, we detected a single acetylated lysine located next to one of the four acetylation sites detected in Arabidopsis thaliana mMDH1. We assessed the kinetic behavior of recombinant A. thaliana and P. patens mMDH1 with site-specifically incorporated acetyl-lysines. Acetylation of A. thaliana mMDH1 at K169, K170, and K334 decreases its oxaloacetate reduction activity, while acetylation of P. patens mMDH1 at K172 increases this activity. We found modulation of the malate oxidation activity only in A. thaliana mMDH1, where acetylation of K334 strongly activated it. Comparative homology modeling of MDH proteins revealed that evolutionarily conserved lysines serve as hotspots of acetylation. Our combined analyses indicate lysine acetylation as a common strategy to fine-tune the activity of central metabolic enzymes with likely impact on plant acclimation capacity.Society for Experimental Biology2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/154190960-74121365-313X (online)10.1111/tpj.15556Balparda, M. et al. Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants [en línea]. The Plant Journal. 2022, 109 (1). doi: 10.1111/tpj.15556. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15419The Plant Journal Vol.109, No,1, 2022reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:58:57Zoai:ucacris:123456789/15419instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:58:57.919Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse |
dc.title.none.fl_str_mv |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
title |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
spellingShingle |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants Balparda, Manuel PLANTAS ACETILACIÓN DE PROTEINAS POSTRANSCRIPCIONAL REGULACION ACETILACION DE PROTEINAS MITOCONDRIAS METABOLISMO MALATO DESHIDROGENASA |
title_short |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
title_full |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
title_fullStr |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
title_full_unstemmed |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
title_sort |
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants |
dc.creator.none.fl_str_mv |
Balparda, Manuel Elsasse, Marlene Badía, Mariana B. Giese, Jonas Bovdilova, Anastasiia Hüdig, Meike Reinmuth, Lisa Eirich, Jürgen Schwarzlander, Markus Finkemeier, Iris Schallenberg Rüdinger, Mareike Maurino, Verónica G. |
author |
Balparda, Manuel |
author_facet |
Balparda, Manuel Elsasse, Marlene Badía, Mariana B. Giese, Jonas Bovdilova, Anastasiia Hüdig, Meike Reinmuth, Lisa Eirich, Jürgen Schwarzlander, Markus Finkemeier, Iris Schallenberg Rüdinger, Mareike Maurino, Verónica G. |
author_role |
author |
author2 |
Elsasse, Marlene Badía, Mariana B. Giese, Jonas Bovdilova, Anastasiia Hüdig, Meike Reinmuth, Lisa Eirich, Jürgen Schwarzlander, Markus Finkemeier, Iris Schallenberg Rüdinger, Mareike Maurino, Verónica G. |
author2_role |
author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
PLANTAS ACETILACIÓN DE PROTEINAS POSTRANSCRIPCIONAL REGULACION ACETILACION DE PROTEINAS MITOCONDRIAS METABOLISMO MALATO DESHIDROGENASA |
topic |
PLANTAS ACETILACIÓN DE PROTEINAS POSTRANSCRIPCIONAL REGULACION ACETILACION DE PROTEINAS MITOCONDRIAS METABOLISMO MALATO DESHIDROGENASA |
dc.description.none.fl_txt_mv |
Fil: Balparda, Manuel. University of Bonn. Molecular Plant Physiology; Alemania Fil: Elsasse, Marlene. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania Fil: Elsasse, Marlene. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; Alemania Fil: Badía, Mariana B. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania Fil: Badía, Mariana B. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentina Fil: Giese, Jonas. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania Fil: Bovdilova, Anastasiia. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania Fil: Hüdig, Meike. University of Bonn. Molecular Plant Physiology; Alemania Fil: Hüdig, Meike. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania Fil: Reinmuth, Lisa. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania Fil: Eirich, Jürgen. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania Fil: Schwarzlander, Markus. University of Munster. Institute of Plant Biology and Biotechnology. Plant Energy Biology; Alemania Fil: Finkemeier, Iris. University of Munster. Institute of Plant Biology and Biotechnology. Plant Physiology; Alemania Fil: Schallenberg Rüdinger, Mareike. University of Bonn. Institute for Cellular and Molecular Botany. Molecular Evolution; Alemania Fil: Maurino, Verónica G. University of Bonn. Molecular Plant Physiology; Alemania Fil: Maurino, Verónica G. Heinrich Heine University. Institute of Developmental and Molecular Biology of Plants. Plant Molecular Physiology and Biotechnology. Cluster of Excellence on Plant Sciences; Alemania Summary: Plants need to rapidly and flexibly adjust their metabolism to changes of their immediate environment. Since this necessity results from the sessile lifestyle of land plants, key mechanisms for orchestrating central metabolic acclimation are likely to have evolved early. Here, we explore the role of lysine acetylation as a post-translational modification to directly modulate metabolic function. We generated a lysine acetylome of the moss Physcomitrium patens and identified 638 lysine acetylation sites, mostly found in mitochondrial and plastidial proteins. A comparison with available angiosperm data pinpointed lysine acetylation as a conserved regulatory strategy in land plants. Focusing on mitochondrial central metabolism, we functionally analyzed acetylation of mitochondrial malate dehydrogenase (mMDH), which acts as a hub of plant metabolic flexibility. In P. patens mMDH1, we detected a single acetylated lysine located next to one of the four acetylation sites detected in Arabidopsis thaliana mMDH1. We assessed the kinetic behavior of recombinant A. thaliana and P. patens mMDH1 with site-specifically incorporated acetyl-lysines. Acetylation of A. thaliana mMDH1 at K169, K170, and K334 decreases its oxaloacetate reduction activity, while acetylation of P. patens mMDH1 at K172 increases this activity. We found modulation of the malate oxidation activity only in A. thaliana mMDH1, where acetylation of K334 strongly activated it. Comparative homology modeling of MDH proteins revealed that evolutionarily conserved lysines serve as hotspots of acetylation. Our combined analyses indicate lysine acetylation as a common strategy to fine-tune the activity of central metabolic enzymes with likely impact on plant acclimation capacity. |
description |
Fil: Balparda, Manuel. University of Bonn. Molecular Plant Physiology; Alemania |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
https://repositorio.uca.edu.ar/handle/123456789/15419 0960-7412 1365-313X (online) 10.1111/tpj.15556 Balparda, M. et al. Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants [en línea]. The Plant Journal. 2022, 109 (1). doi: 10.1111/tpj.15556. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15419 |
url |
https://repositorio.uca.edu.ar/handle/123456789/15419 |
identifier_str_mv |
0960-7412 1365-313X (online) 10.1111/tpj.15556 Balparda, M. et al. Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants [en línea]. The Plant Journal. 2022, 109 (1). doi: 10.1111/tpj.15556. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15419 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/4.0/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/4.0/ |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Society for Experimental Biology |
publisher.none.fl_str_mv |
Society for Experimental Biology |
dc.source.none.fl_str_mv |
The Plant Journal Vol.109, No,1, 2022 reponame:Repositorio Institucional (UCA) instname:Pontificia Universidad Católica Argentina |
reponame_str |
Repositorio Institucional (UCA) |
collection |
Repositorio Institucional (UCA) |
instname_str |
Pontificia Universidad Católica Argentina |
repository.name.fl_str_mv |
Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina |
repository.mail.fl_str_mv |
claudia_fernandez@uca.edu.ar |
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1836638365941760000 |
score |
13.070432 |