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2. Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria

Author

Koivulehto Marianne, Battchikova Natalia, Korpela Saara, Khalikova Elvira, Zavialov Anton, and Korpela Timo

Subjects
pyridoxal 5´-phosphate dependent enzymes, phosphoserine aminotransferase, protons at the active site of transaminases, Chemistry, QD1-999
Abstract

Intracellular pyridoxal 5´-phosphate (PLP) -dependent recombinant phosphoserine aminotransferases (PSATs; EC 2.6.1.52) from two alkaliphilic Bacillus strains were overproduced in Escherichia coli, purified to homogeneity and their enzymological characteristics were compared to PSAT from neutralophilic E. coli. Some of the enzymatic characteristics of the PSATs from the alkaliphiles were unique, showing high and sharp pH optimal of the activity related to putative internal pH inside the microbes. The specific activities of all of the studied enzymes were similar (42-44 U/mg) as measured at the pH optima of the enzymes. The spectrophotometric acid-base titration of the PLP chromophore of the enzymes from the alkaliphiles showed that the pH optimum of the activity appeared at the pH wherein the active sites were half-protonated. Detachment of PLP from holoenzymes did not take place even at pH up to 11. The kinetics of the activity loss at acid and alkaline pHs were similar in all three enzymes and followed similar kinetics. The available 3-D structural data is discussed as well as the role of protons at the active site of aminotransferases.

Published
2020
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21. Author response: Pyruvate:ferredoxin oxidoreductase and low abundant ferredoxins support aerobic photomixotrophic growth in cyanobacteria

Author

Wang, Yingying, primary, Chen, Xi, additional, Spengler, Katharina, additional, Terberger, Karoline, additional, Boehm, Marko, additional, Appel, Jens, additional, Barske, Thomas, additional, Timm, Stefan, additional, Battchikova, Natalia, additional, Hagemann, Martin, additional, and Gutekunst, Kirstin, additional

Published
2022
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29. Arabidopsis poly(ADP-ribose)-binding protein RCD1 interacts with Photoregulatory Protein Kinases in nuclear bodies

Author

Vainonen, Julia P., primary, Shapiguzov, Alexey, additional, Krasensky-Wrzaczek, Julia, additional, Gossens, Richard, additional, Masi, Raffaella De, additional, Danciu, Iulia, additional, Puukko, Tuomas, additional, Battchikova, Natalia, additional, Jonak, Claudia, additional, Wirthmueller, Lennart, additional, Wrzaczek, Michael, additional, and Kangasjärvi, Jaakko, additional

Published
2020
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31. CORRECTION: The Cytochrome b6f Complex is not Involved in Cyanobacterial State Transitions

Author

Calzadilla, Pablo I., Zhan, Jiao, Sétif, Pierre, Lemaire, Claire, Solymosi, Daniel, Battchikova, Natalia, Wang, Qiang, Kirilovsky, Diana, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Mécanismes régulateurs chez les organismes photosynthétiques (MROP), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Laboratoire des Protéines et Systèmes Membranaires (LPSM)

Subjects
[SDV]Life Sciences [q-bio]
Published
2019

38. Light has a specific role in modulating Arabidopsis gene expression at low temperature

Author

Battchikova Natalia, Allahverdiyeva Yagut, Piippo Mirva, Soitamo Arto J, and Aro Eva-Mari

Subjects
Botany, QK1-989
Abstract

Abstract Background Light and temperature are the key abiotic modulators of plant gene expression. In the present work the effect of light under low temperature treatment was analyzed by using microarrays. Specific attention was paid to the up and down regulated genes by using promoter analysis. This approach revealed putative regulatory networks of transcription factors behind the induction or repression of the genes. Results Induction of a few oxidative stress related genes occurred only under the Cold/Light treatment including genes encoding iron superoxide dismutase (FeSOD) and glutathione-dependent hydrogen peroxide peroxidases (GPX). The ascorbate dependent water-water cycle genes showed no response to Cold/Light or Cold/Dark treatments. Cold/Light specifically induced genes encoding protective molecules like phenylpropanoids and photosynthesis-related carotenoids also involved in the biosynthesis of hormone abscisic acid (ABA) crucial for cold acclimation. The enhanced/repressed transcript levels were not always reflected on the respective protein levels as demonstrated by dehydrin proteins. Conclusion Cold/Light up regulated twice as many genes as the Cold/Dark treatment and only the combination of light and low temperature enhanced the expression of several genes earlier described as cold-responsive genes. Cold/Light-induced genes included both cold-responsive transcription factors and several novel ones containing zinc-finger, MYB, NAC and AP2 domains. These are likely to function in concert in enhancing gene expression. Similar response elements were found in the promoter regions of both the transcription factors and their target genes implying a possible parallel regulation or amplification of the environmental signals according to the metabolic/redox state in the cells.

Published
2008
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39. Septal protein SepJ from the heterocyst‐forming cyanobacterium Anabaena forms multimers and interacts with peptidoglycan

Author

Ramos León, Félix, Mariscal Romero, Vicente, Flores García, Enrique, Battchikova, Natalia, Ramos León, Félix, Mariscal Romero, Vicente, Flores García, Enrique, and Battchikova, Natalia

Abstract

Heterocyst‐forming cyanobacteria grow as filaments that can be hundreds of cells long. Proteinaceous septal junctions provide cell–cell binding and communication functions in the filament. In Anabaena sp. strain PCC 7120, the SepJ protein is important for the formation of septal junctions. SepJ consists of integral membrane and extramembrane sections – the latter including linker and coiled‐coil domains. SepJ (predicted MW, 81.3 kDa) solubilized from Anabaena membranes was found in complexes of about 296–334 kDa, suggesting that SepJ forms multimeric complexes. We constructed an Anabaena strain producing a double‐tagged SepJ protein (SepJ‐GFP‐His10) and isolated the tagged protein by a two‐step affinity chromatography procedure. Analysis of the purified protein preparation provided no indication of the presence of specific SepJ partners, but suggested that SepJ is processed to remove an N‐terminal fragment. Additionally, pull‐down experiments showed that His6‐tagged versions of SepJ and of the SepJ coiled‐coil domain interact with Anabaena peptidoglycan (PG). Our results indicate that SepJ forms multimers, that it interacts with PG, and that the coiled‐coil domain is involved in this interaction. These observations support the idea that SepJ is a component of the septal junctions that join the cells in the Anabaena filament.

Published
2017

40. Septal protein SepJ from the heterocyst-forming cyanobacterium Anabaena forms multimers and interacts with peptidoglycan

Author

Academy of Finland, European Commission, Ministerio de Economía y Competitividad (España), Ramos-León, Félix, Mariscal, Vicente, Battchikova, Natalia, Aro, Eva-Mari, Flores, Enrique, Academy of Finland, European Commission, Ministerio de Economía y Competitividad (España), Ramos-León, Félix, Mariscal, Vicente, Battchikova, Natalia, Aro, Eva-Mari, and Flores, Enrique

Abstract

Heterocyst-forming cyanobacteria grow as filaments that can be hundreds of cells long. Proteinaceous septal junctions provide cell–cell binding and communication functions in the filament. In Anabaena sp. strain PCC 7120, the SepJ protein is important for the formation of septal junctions. SepJ consists of integral membrane and extramembrane sections – the latter including linker and coiled-coil domains. SepJ (predicted MW, 81.3 kDa) solubilized from Anabaena membranes was found in complexes of about 296–334 kDa, suggesting that SepJ forms multimeric complexes. We constructed an Anabaena strain producing a double-tagged SepJ protein (SepJ-GFP-His) and isolated the tagged protein by a two-step affinity chromatography procedure. Analysis of the purified protein preparation provided no indication of the presence of specific SepJ partners, but suggested that SepJ is processed to remove an N-terminal fragment. Additionally, pull-down experiments showed that His-tagged versions of SepJ and of the SepJ coiled-coil domain interact with Anabaena peptidoglycan (PG). Our results indicate that SepJ forms multimers, that it interacts with PG, and that the coiled-coil domain is involved in this interaction. These observations support the idea that SepJ is a component of the septal junctions that join the cells in the Anabaena filament.

Published
2017

43. Dynamic Changes in the Proteome of Synechocystis6803 in Response to CO2Limitation Revealed by Quantitative Proteomics

Author

Battchikova, Natalia, Vainonen, Julia P., Vorontsova, Natalia, Keränen, Mika, Carmel, Dalton, and Aro, Eva-Mari

Abstract

Cyanobacteria developed efficient carbon concentrating mechanisms which significantly improve the photosynthetic performance and survival of cells under limiting CO2conditions. Dynamic changes of the Synechocystisproteome to CO2limitation were investigated using shotgun LC−MS/MS approach with isobaric tag for relative and absolute quantification (iTRAQ) technique. Synechocystiscells grown at high (3%) CO2were shifted to air-level CO2followed by protein extraction after 6, 24, and 72 h. About 19% of the cyanobacterial proteome was identified and the expression changes were quantified for 17% of theoretical ORFs. For 76 proteins, up- or down-regulation was found to be significant (more than 1.5 or less than 0.7). Major changes were observed in proteins participating in inorganic carbon uptake, CO2fixation, nitrogen transport and assimilation, as well as in the protection of the photosynthetic machinery from excess of light. Further, a number of hypothetical proteins with unknown functions were discovered. In general, the cells appear to acclimate to low CO2without a significant stress since the stress-related molecular chaperones were down-regulated and only a minor decline was detected for proteins of phycobilisomes, photosynthetic complexes, and translation machinery. The results of iTRAQ experiment were validated by the Western blot analysis for selected proteins.

Published
2024
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44. Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

Author

Raleiras, Patrícia, Khanna, Namita, Miranda, Hélder, Mészáros, Lívia S., Krassen, Henning, Felix, Ho, Battchikova, Natalia, Aro, Eva-Mari, Magnuson, Ann, Lindblad, Peter, Stenbjörn, Styring, Raleiras, Patrícia, Khanna, Namita, Miranda, Hélder, Mészáros, Lívia S., Krassen, Henning, Felix, Ho, Battchikova, Natalia, Aro, Eva-Mari, Magnuson, Ann, Lindblad, Peter, and Stenbjörn, Styring

Published
2016
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45. Flavodiiron Protein Flv2/Flv4-Related Photoprotective Mechanism Dissipates Excitation Pressure of PSII in Cooperation with Phycobilisomes in Cyanobacteria1[C][W][OPEN]

Author

Bersanini, Luca, Battchikova, Natalia, Jokel, Martina, Rehman, Ateeq, Vass, Imre, Allahverdiyeva, Yagut, and Aro, Eva-Mari

Subjects
Chlorophyll, Singlet Oxygen, Plastoquinone, Chlorophyll A, Immunoblotting, Synechocystis, food and beverages, Photosystem II Protein Complex, macromolecular substances, Photochemical Processes, Carotenoids, Article, Oxygen, Kinetics, Phenotype, Spectrometry, Fluorescence, Bacterial Proteins, Mutation, Operon, Phycobilisomes, bacteria, Oxidation-Reduction
Abstract

Oxygenic photosynthesis evolved with cyanobacteria, the ancestors of plant chloroplasts. The highly oxidizing chemistry of water splitting required concomitant evolution of efficient photoprotection mechanisms to safeguard the photosynthetic machinery. The role of flavodiiron proteins (FDPs), originally called A-type flavoproteins or Flvs, in this context has only recently been appreciated. Cyanobacterial FDPs constitute a specific protein group that evolved to protect oxygenic photosynthesis. There are four FDPs in Synechocystis sp. PCC 6803 (Flv1 to Flv4). Two of them, Flv2 and Flv4, are encoded by an operon together with a Sll0218 protein. Their expression, tightly regulated by CO2 levels, is also influenced by changes in light intensity. Here we describe the overexpression of the flv4-2 operon in Synechocystis sp. PCC 6803 and demonstrate that it results in improved photochemistry of PSII. The flv4-2/OE mutant is more resistant to photoinhibition of PSII and exhibits a more oxidized state of the plastoquinone pool and reduced production of singlet oxygen compared with control strains. Results of biophysical measurements indicate that the flv4-2 operon functions in an alternative electron transfer pathway from PSII, and thus alleviates PSII excitation pressure by channeling up to 30% of PSII-originated electrons. Furthermore, intact phycobilisomes are required for stable expression of the flv4-2 operon genes and for the Flv2/Flv4 heterodimer-mediated electron transfer mechanism. The latter operates in photoprotection in a complementary way with the orange carotenoid protein-related nonphotochemical quenching. Expression of the flv4-2 operon and exchange of the D1 forms in PSII centers upon light stress, on the contrary, are mutually exclusive photoprotection strategies among cyanobacteria.

Published
2013

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