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
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/15419

id RIUCA_739c9264ba4ca4037be7ebb8d4d88003
oai_identifier_str oai:ucacris:123456789/15419
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
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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score 13.070432