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Relevant bibliographies by topics / STN8 kinase

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Academic literature on the topic 'STN8 kinase'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "STN8 kinase"

1

Rochaix, Jean-David, Sylvain Lemeille, Alexey Shapiguzov, Iga Samol, Geoffrey Fucile, Adrian Willig, and Michel Goldschmidt-Clermont. "Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1608 (December 19, 2012): 3466–74. http://dx.doi.org/10.1098/rstb.2012.0064.

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Photosynthetic organisms are subjected to frequent changes in light quality and quantity and need to respond accordingly. These acclimatory processes are mediated to a large extent through thylakoid protein phosphorylation. Recently, two major thylakoid protein kinases have been identified and characterized. The Stt7/STN7 kinase is mainly involved in the phosphorylation of the LHCII antenna proteins and is required for state transitions. It is firmly associated with the cytochrome b 6 f complex, and its activity is regulated by the redox state of the plastoquinone pool. The other kinase, Stl1/STN8, is responsible for the phosphorylation of the PSII core proteins. Using a reverse genetics approach, we have recently identified the chloroplast PPH1/TAP38 and PBPC protein phosphatases, which counteract the activity of STN7 and STN8 kinases, respectively. They belong to the PP2C-type phosphatase family and are conserved in land plants and algae. The picture that emerges from these studies is that of a complex regulatory network of chloroplast protein kinases and phosphatases that is involved in light acclimation, in maintenance of the plastoquinone redox poise under fluctuating light and in the adjustment to metabolic needs.

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2

Flood, Pádraic J., Lan Yin, Andrei Herdean, Jeremy Harbinson, Mark G. M. Aarts, and Cornelia Spetea. "Natural variation in phosphorylation of photosystem II proteins in Arabidopsis thaliana : is it caused by genetic variation in the STN kinases?" Philosophical Transactions of the Royal Society B: Biological Sciences 369, no. 1640 (April 19, 2014): 20130499. http://dx.doi.org/10.1098/rstb.2013.0499.

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Reversible phosphorylation of photosystem II (PSII) proteins is an important regulatory mechanism that can protect plants from changes in ambient light intensity and quality. We hypothesized that there is natural variation in this process in Arabidopsis ( Arabidopsis thaliana ), and that this results from genetic variation in the STN7 and STN8 kinase genes. To test this, Arabidopsis accessions of diverse geographical origins were exposed to two light regimes, and the levels of phospho-D1 and phospho-light harvesting complex II (LHCII) proteins were quantified by western blotting with anti-phosphothreonine antibodies. Accessions were classified as having high, moderate or low phosphorylation relative to Col-0. This variation could not be explained by the abundance of the substrates in thylakoid membranes. In genotypes with atrazine-resistant forms of the D1 protein, low D1 and LHCII protein phosphorylation was observed, which may be due to low PSII efficiency, resulting in reduced activation of the STN kinases. In the remaining genotypes, phospho-D1 levels correlated with STN8 protein abundance in high-light conditions. In growth light, D1 and LHCII phosphorylation correlated with longitude and in the case of LHCII phosphorylation also with temperature variability. This suggests a possible role of natural variation in PSII protein phosphorylation in the adaptation of Arabidopsis to diverse environments.

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Schönberg, Anna, Anja Rödiger, Wiebke Mehwald, Johann Galonska, Gideon Christ, Stefan Helm, Domenika Thieme, Petra Majovsky, Wolfgang Hoehenwarter, and Sacha Baginsky. "Identification of STN7/STN8 kinase targets reveals connections between electron transport, metabolism and gene expression." Plant Journal 90, no. 6 (April 21, 2017): 1176–86. http://dx.doi.org/10.1111/tpj.13536.

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4

Vainonen, Julia P., Maria Hansson, and Alexander V. Vener. "STN8 Protein Kinase inArabidopsis thalianaIs Specific in Phosphorylation of Photosystem II Core Proteins." Journal of Biological Chemistry 280, no. 39 (July 22, 2005): 33679–86. http://dx.doi.org/10.1074/jbc.m505729200.

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5

Gerotto, Caterina, Andrea Trotta, Azfar Ali Bajwa, Ilaria Mancini, Tomas Morosinotto, and Eva-Mari Aro. "Thylakoid Protein Phosphorylation Dynamics in a Moss Mutant Lacking SERINE/THREONINE PROTEIN KINASE STN8." Plant Physiology 180, no. 3 (May 6, 2019): 1582–97. http://dx.doi.org/10.1104/pp.19.00117.

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6

Reiland, S., G. Finazzi, A. Endler, A. Willig, K. Baerenfaller, J. Grossmann, B. Gerrits, et al. "Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF)." Proceedings of the National Academy of Sciences 108, no. 31 (July 18, 2011): 12955–60. http://dx.doi.org/10.1073/pnas.1104734108.

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7

Poudyal, Roshan Sharma, Krishna Nath, Ismayil S. Zulfugarov, and Choon-Hwan Lee. "Production of superoxide from photosystem II-light harvesting complex II supercomplex in STN8 kinase knock-out rice mutants under photoinhibitory illumination." Journal of Photochemistry and Photobiology B: Biology 162 (September 2016): 240–47. http://dx.doi.org/10.1016/j.jphotobiol.2016.06.050.

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8

Betterle, Nico, Roshan Sharma Poudyal, Anthony Rosa, Guangxi Wu, Roberto Bassi, and Choon-Hwan Lee. "The STN8 kinase-PBCP phosphatase system is responsible for high-light-induced reversible phosphorylation of the PSII inner antenna subunit CP29 in rice." Plant Journal 89, no. 4 (February 2017): 681–91. http://dx.doi.org/10.1111/tpj.13412.

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9

Wu, Jianghao, Liwei Rong, Weijun Lin, Lingxi Kong, Dengjie Wei, Lixin Zhang, Jean-David Rochaix, and Xiumei Xu. "Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7." Plant Physiology 186, no. 2 (February 23, 2021): 964–76. http://dx.doi.org/10.1093/plphys/kiab091.

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Abstract In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1.

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Eisa, Ahmed, Bettina Bölter, and Serena Schwenkert. "The ACT domain in chloroplast precursor–phosphorylating STY kinases binds metabolites and allosterically regulates kinase activity." Journal of Biological Chemistry 294, no. 46 (October 8, 2019): 17278–88. http://dx.doi.org/10.1074/jbc.ra119.010298.

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Protein import of nucleus-encoded proteins into plant chloroplasts is a highly regulated process, requiring fine-tuning mechanisms especially during chloroplast differentiation. One way of altering import efficiency is phosphorylation of chloroplast transit peptides in the cytosol. We recently investigated the role of three serine/threonine/tyrosine (STY) kinases, STY8, STY17, and STY46, in precursor phosphorylation. These three kinases have a high degree of similarity and harbor a conserved aspartate kinase–chorismate mutase–tyrA (prephenate dehydrogenase) (ACT) domain upstream of the kinase domain. The ACT domain is a widely distributed structural motif known to be important for allosteric regulation of many enzymes. In this work, using biochemical and biophysical techniques in vitro and in planta, including kinase assays, microscale thermophoresis, size exclusion chromatography, as well as site-directed mutagenesis approaches, we show that the ACT domain regulates autophosphorylation and substrate phosphorylation of the STY kinases. We found that isoleucine and S-adenosylmethionine bind to the ACT domain, negatively influencing its autophosphorylation ability. Moreover, we investigated the role of the ACT domain in planta and confirmed its involvement in chloroplast differentiation in vivo. Our results provide detailed insights into the regulation of enzyme activity by ACT domains and establish that it has a role in binding amino acid ligands during chloroplast biogenesis.

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Dissertations / Theses on the topic "STN8 kinase"

1

Cutolo, Edoardo Andrea [Verfasser]. "The chloroplast calcium sensor protein CAS is part of the STN7/STN8 kinase phosphorylation network and is required for photoacclimation / Edoardo Andrea Cutolo." Bonn : Universitäts- und Landesbibliothek Bonn, 2020. http://d-nb.info/1207923753/34.

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Schönberg, Anna Verfasser], Sacha [Gutachter] [Baginsky, Kristina [Gutachter] Kühn, and Michel [Gutachter] Goldschmidt-Clermont. "On the influence of the protein kinases pCKII, STN7 and STN8 on chloroplast phosphorylation networks in Arabidopsis thaliana : [kumulative Dissertation] / Anna Schönberg ; Gutachter: Sacha Baginsky, Kristina Kühn, Michel Goldschmidt-Clermont." Halle (Saale) : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2019. http://nbn-resolving.de/urn:nbn:de:gbv:3:4-1981185920-140061.

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Schönberg, Anna [Verfasser], Sacha [Gutachter] Baginsky, Kristina [Gutachter] Kühn, and Michel [Gutachter] Goldschmidt-Clermont. "On the influence of the protein kinases pCKII, STN7 and STN8 on chloroplast phosphorylation networks in Arabidopsis thaliana : [kumulative Dissertation] / Anna Schönberg ; Gutachter: Sacha Baginsky, Kristina Kühn, Michel Goldschmidt-Clermont." Halle (Saale) : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2019. http://d-nb.info/1210728605/34.

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4

Lamberti, Giorgia. "Characterization of the Arabidopsis thaliana STY8, STY17 and STY46 protein kinase family." Diss., lmu, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-138039.

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Lamberti, Giorgia [Verfasser], and Jürgen [Akademischer Betreuer] Soll. "Characterization of the Arabidopsis thaliana STY8, STY17 and STY46 protein kinase family / Giorgia Lamberti. Betreuer: Jürgen Soll." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2011. http://d-nb.info/1018615954/34.

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Wunder, Tobias [Verfasser], and Dario Michael [Akademischer Betreuer] Leister. "STN7/8 - a study on the regulation and function of the major thylakoid protein kinases [[Elektronische Ressource]] / Tobias Wunder. Betreuer: Dario Leister." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2013. http://d-nb.info/1050095111/34.

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Book chapters on the topic "STN8 kinase"

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Nath, Krishna, Sujata R. Mishra, Ismayil S. Zulfugarov, Sharif-Ar-Raffi, Chin-Bum Lee, Gynheung An, and Choon-Hwan Lee. "Characterization of a T-DNA Inserted STN8 Kinase Mutant of Oryza sativa L." In Photosynthesis. Energy from the Sun, 1307–11. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6709-9_282.

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