Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants

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...

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Autores principales: 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.
Formato: Artículo
Lenguaje:Inglés
Publicado: Society for Experimental Biology 2022
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Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/15419
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id I33-R139-123456789-15419
record_format dspace
institution Universidad Católica Argentina
institution_str I-33
repository_str R-139
collection Repositorio Institucional de la Universidad Católica Argentina (UCA)
language Inglés
topic PLANTAS
ACETILACIÓN DE PROTEINAS
POSTRANSCRIPCIONAL
REGULACION
ACETILACION DE PROTEINAS
MITOCONDRIAS
METABOLISMO
MALATO DESHIDROGENASA
spellingShingle PLANTAS
ACETILACIÓN DE PROTEINAS
POSTRANSCRIPCIONAL
REGULACION
ACETILACION DE PROTEINAS
MITOCONDRIAS
METABOLISMO
MALATO DESHIDROGENASA
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.
Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants
topic_facet PLANTAS
ACETILACIÓN DE PROTEINAS
POSTRANSCRIPCIONAL
REGULACION
ACETILACION DE PROTEINAS
MITOCONDRIAS
METABOLISMO
MALATO DESHIDROGENASA
description 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.
format Artículo
author 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_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_sort Balparda, Manuel
title Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants
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
publisher Society for Experimental Biology
publishDate 2022
url https://repositorio.uca.edu.ar/handle/123456789/15419
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