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  1. Buch ; Online ; Dissertation / Habilitation: Molecular adaptations and post-translational regulation of C4-NADP-malic enzyme

    Bovdilova, Anastasiia [Verfasser]

    2020  

    Verfasserangabe Anastasiia Bovdilova
    Schlagwörter Biowissenschaften, Biologie ; Life Science, Biology
    Thema/Rubrik (Code) sg570
    Sprache Englisch
    Verlag Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf
    Erscheinungsort Düsseldorf
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
    Datenquelle Digitale Dissertationen im Internet

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  2. Artikel: Acetylation of conserved lysines fine‐tunes mitochondrial malate dehydrogenase activity in land plants

    Balparda, Manuel / Elsässer, Marlene / Badia, Mariana B. / Giese, Jonas / Bovdilova, Anastasiia / Hüdig, Meike / Reinmuth, Lisa / Eirich, Jürgen / Schwarzländer, Markus / Finkemeier, Iris / Schallenberg‐Rüdinger, Mareike / Maurino, Veronica G.

    plant journal. 2022 Jan., v. 109, no. 1

    2022  

    Abstract: 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 ... ...

    Abstract 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.
    Schlagwörter Arabidopsis thaliana ; Physcomitrium ; acclimation ; acetylation ; biochemical pathways ; lifestyle ; lysine ; malate dehydrogenase ; malates ; mitochondria ; mosses and liverworts ; oxaloacetic acid ; oxidation ; post-translational modification
    Sprache Englisch
    Erscheinungsverlauf 2022-01
    Umfang p. 92-111.
    Erscheinungsort John Wiley & Sons, Ltd
    Dokumenttyp Artikel
    Anmerkung JOURNAL ARTICLE
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/tpj.15556
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  3. Artikel ; Online: PsbS contributes to photoprotection in Chlamydomonas reinhardtii independently of energy dissipation.

    Redekop, Petra / Rothhausen, Natalie / Rothhausen, Natascha / Melzer, Michael / Mosebach, Laura / Dülger, Emin / Bovdilova, Anastasiia / Caffarri, Stefano / Hippler, Michael / Jahns, Peter

    Biochimica et biophysica acta. Bioenergetics

    2020  Band 1861, Heft 5-6, Seite(n) 148183

    Abstract: Photosynthetic organisms are frequently exposed to excess light conditions and hence to photo-oxidative stress. To counteract photo-oxidative damage, land plants and most algae make use of non- photochemical quenching (NPQ) of excess light energy, in ... ...

    Abstract Photosynthetic organisms are frequently exposed to excess light conditions and hence to photo-oxidative stress. To counteract photo-oxidative damage, land plants and most algae make use of non- photochemical quenching (NPQ) of excess light energy, in particular the rapidly inducible and relaxing qE-mechanism. In vascular plants, the constitutively active PsbS protein is the key regulator of qE. In the green algae C. reinhardtii, however, qE activation is only possible after initial high-light (HL) acclimation for several hours and requires the synthesis of LHCSR proteins which act as qE regulators. The precise function of PsbS, which is transiently expressed during HL acclimation in C. reinhardtii, is still unclear. Here, we investigated the impact of different PsbS amounts on HL acclimation characteristics of C. reinhardtii cells. We demonstrate that lower PsbS amounts negatively affect HL acclimation at different levels, including NPQ capacity, electron transport characteristics, antenna organization and morphological changes, resulting in an overall increased HL sensitivity and lower vitality of cells. Contrarily, higher PsbS amounts do not result in a higher NPQ capacity, but nevertheless provide higher fitness and tolerance towards HL stress. Strikingly, constitutively expressed PsbS protein was found to be degraded during HL acclimation. We propose that PsbS is transiently required during HL acclimation for the reorganization of thylakoid membranes and/or antenna proteins along with the activation of NPQ and adjustment of electron transfer characteristics, and that degradation of PsbS is essential in the fully HL acclimated state.
    Mesh-Begriff(e) Algal Proteins/metabolism ; Algal Proteins/ultrastructure ; Chlamydomonas reinhardtii/metabolism ; Chlamydomonas reinhardtii/radiation effects ; Chlamydomonas reinhardtii/ultrastructure ; Energy Transfer ; Light ; Photochemical Processes ; Photosystem I Protein Complex/metabolism ; Photosystem II Protein Complex/metabolism ; Protective Agents/metabolism ; Reactive Oxygen Species/metabolism ; Thylakoids/metabolism
    Chemische Substanzen Algal Proteins ; Photosystem I Protein Complex ; Photosystem II Protein Complex ; Protective Agents ; Reactive Oxygen Species
    Sprache Englisch
    Erscheinungsdatum 2020-03-12
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2020.148183
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: PsbS contributes to photoprotection in Chlamydomonas reinhardtii independently of energy dissipation

    Redekop, Petra / Rothhausen, Natalie / Rothhausen, Natascha / Melzer, Michael / Mosebach, Laura / Dülger, Emin / Bovdilova, Anastasiia / Caffarri, Stefano / Hippler, Michael / Jahns, Peter

    Biochimica et biophysica acta. 2020 June 01, v. 1861, no. 5-6

    2020  

    Abstract: Photosynthetic organisms are frequently exposed to excess light conditions and hence to photo-oxidative stress. To counteract photo-oxidative damage, land plants and most algae make use of non- photochemical quenching (NPQ) of excess light energy, in ... ...

    Abstract Photosynthetic organisms are frequently exposed to excess light conditions and hence to photo-oxidative stress. To counteract photo-oxidative damage, land plants and most algae make use of non- photochemical quenching (NPQ) of excess light energy, in particular the rapidly inducible and relaxing qE-mechanism. In vascular plants, the constitutively active PsbS protein is the key regulator of qE. In the green algae C. reinhardtii, however, qE activation is only possible after initial high-light (HL) acclimation for several hours and requires the synthesis of LHCSR proteins which act as qE regulators. The precise function of PsbS, which is transiently expressed during HL acclimation in C. reinhardtii, is still unclear. Here, we investigated the impact of different PsbS amounts on HL acclimation characteristics of C. reinhardtii cells. We demonstrate that lower PsbS amounts negatively affect HL acclimation at different levels, including NPQ capacity, electron transport characteristics, antenna organization and morphological changes, resulting in an overall increased HL sensitivity and lower vitality of cells. Contrarily, higher PsbS amounts do not result in a higher NPQ capacity, but nevertheless provide higher fitness and tolerance towards HL stress. Strikingly, constitutively expressed PsbS protein was found to be degraded during HL acclimation. We propose that PsbS is transiently required during HL acclimation for the reorganization of thylakoid membranes and/or antenna proteins along with the activation of NPQ and adjustment of electron transfer characteristics, and that degradation of PsbS is essential in the fully HL acclimated state.
    Schlagwörter Chlamydomonas reinhardtii ; acclimation ; algae ; autotrophs ; electron transfer ; embryophytes ; energy ; gene expression ; light harvesting complex ; photochemistry ; radiation resistance ; thylakoids ; vascular plants
    Sprache Englisch
    Erscheinungsverlauf 2020-0601
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2020.148183
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  5. Artikel ; Online: Acetylation of conserved lysines fine-tunes mitochondrial malate dehydrogenase activity in land plants.

    Balparda, Manuel / Elsässer, Marlene / Badia, Mariana B / Giese, Jonas / Bovdilova, Anastasiia / Hüdig, Meike / Reinmuth, Lisa / Eirich, Jürgen / Schwarzländer, Markus / Finkemeier, Iris / Schallenberg-Rüdinger, Mareike / Maurino, Veronica G

    The Plant journal : for cell and molecular biology

    2021  Band 109, Heft 1, Seite(n) 92–111

    Abstract: 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 ... ...

    Abstract 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.
    Mesh-Begriff(e) Acetylation ; Embryophyta/enzymology ; Embryophyta/genetics ; Lysine/metabolism ; Malate Dehydrogenase/genetics ; Malate Dehydrogenase/metabolism ; Mitochondria/enzymology ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Protein Processing, Post-Translational
    Chemische Substanzen Mitochondrial Proteins ; Plant Proteins ; Malate Dehydrogenase (EC 1.1.1.37) ; Lysine (K3Z4F929H6)
    Sprache Englisch
    Erscheinungsdatum 2021-11-10
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1088037-9
    ISSN 1365-313X ; 0960-7412
    ISSN (online) 1365-313X
    ISSN 0960-7412
    DOI 10.1111/tpj.15556
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Corrigendum to: Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day.

    Bovdilova, Anastasiia / Alexandre, Bruno M / Höppner, Astrid / Luís, Inês Matias / Alvarez, Clarisa E / Bickel, David / Gohlke, Holger / Decker, Christina / Nagel-Steger, Luitgard / Alseekh, Saleh / Fernie, Alisdair R / Drincovich, Maria F / Abreu, Isabel A / Maurino, Veronica G

    The Plant cell

    2021  Band 34, Heft 1, Seite(n) 698–699

    Sprache Englisch
    Erscheinungsdatum 2021-10-29
    Erscheinungsland England
    Dokumenttyp Journal Article ; Published Erratum
    ZDB-ID 623171-8
    ISSN 1532-298X ; 1040-4651
    ISSN (online) 1532-298X
    ISSN 1040-4651
    DOI 10.1093/plcell/koab262
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  7. Artikel ; Online: Molecular adaptations of NADP-malic enzyme for its function in C

    Alvarez, Clarisa E / Bovdilova, Anastasiia / Höppner, Astrid / Wolff, Christian-Claus / Saigo, Mariana / Trajtenberg, Felipe / Zhang, Tao / Buschiazzo, Alejandro / Nagel-Steger, Luitgard / Drincovich, Maria F / Lercher, Martin J / Maurino, Veronica G

    Nature plants

    2019  Band 5, Heft 7, Seite(n) 755–765

    Abstract: ... In ... ...

    Abstract In C
    Mesh-Begriff(e) Amino Acid Motifs ; Biocatalysis ; Catalytic Domain ; Hydrogen-Ion Concentration ; Malate Dehydrogenase/chemistry ; Malate Dehydrogenase/genetics ; Malate Dehydrogenase/metabolism ; Malates/metabolism ; Photosynthesis ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Sorghum/chemistry ; Sorghum/enzymology ; Sorghum/genetics ; Zea mays/chemistry ; Zea mays/enzymology ; Zea mays/genetics
    Chemische Substanzen Malates ; Plant Proteins ; malic acid (817L1N4CKP) ; Malate Dehydrogenase (EC 1.1.1.37) ; malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40)
    Sprache Englisch
    Erscheinungsdatum 2019-06-24
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2055-0278
    ISSN (online) 2055-0278
    DOI 10.1038/s41477-019-0451-7
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Posttranslational Modification of the NADP-Malic Enzyme Involved in C

    Bovdilova, Anastasiia / Alexandre, Bruno M / Höppner, Astrid / Luís, Inês Matias / Alvarez, Clarisa E / Bickel, David / Gohlke, Holger / Decker, Christina / Nagel-Steger, Luitgard / Alseekh, Saleh / Fernie, Alisdair R / Drincovich, Maria F / Abreu, Isabel A / Maurino, Veronica G

    The Plant cell

    2019  Band 31, Heft 10, Seite(n) 2525–2539

    Abstract: Evolution of the ... ...

    Abstract Evolution of the C
    Mesh-Begriff(e) Biomimetics ; Gene Expression ; Kinetics ; Light ; Malate Dehydrogenase/chemistry ; Malate Dehydrogenase/genetics ; Malate Dehydrogenase/metabolism ; Mass Spectrometry ; Molecular Dynamics Simulation ; Mutation ; NADP/chemistry ; NADP/metabolism ; Phosphorylation/radiation effects ; Photosynthesis/genetics ; Photosynthesis/physiology ; Photosynthesis/radiation effects ; Plant Leaves/chemistry ; Plant Leaves/metabolism ; Plant Proteins/metabolism ; Protein Processing, Post-Translational/radiation effects ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Zea mays/enzymology ; Zea mays/radiation effects
    Chemische Substanzen Plant Proteins ; Recombinant Proteins ; NADP (53-59-8) ; Malate Dehydrogenase (EC 1.1.1.37) ; malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40)
    Sprache Englisch
    Erscheinungsdatum 2019-07-30
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 623171-8
    ISSN 1532-298X ; 1040-4651
    ISSN (online) 1532-298X
    ISSN 1040-4651
    DOI 10.1105/tpc.19.00406
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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