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of 18
pro vyhledávání: '"Minna M, Koskela"'
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Autor:
Willy V Bienvenut, Annika Brünje, Jean‐Baptiste Boyer, Jens S Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V Dinh, Minna M Koskela, Vincent Jung, Julian Seidel, Laura K Schyrba, Aiste Ivanauskaite, Jürgen Eirich, Rüdiger Hell, Dirk Schwarzer, Paula Mulo, Markus Wirtz, Thierry Meinnel, Carmela Giglione, Iris Finkemeier
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families o
Externí odkaz:
https://doaj.org/article/d26b41bab41445bf8117bc4fba9d0b24
Autor:
Magdalena Füßl, Ines Lassowskat, Guillaume Née, Minna M. Koskela, Annika Brünje, Priyadarshini Tilak, Jonas Giese, Dario Leister, Paula Mulo, Dirk Schwarzer, Iris Finkemeier
Publikováno v:
Frontiers in Plant Science, Vol 9 (2018)
The reversible acetylation of lysine residues is catalyzed by the antagonistic action of lysine acetyltransferases and deacetylases, which can be considered as master regulators of their substrate proteins. Lysine deacetylases, historically referred
Externí odkaz:
https://doaj.org/article/18de750a09c44f868dc962cf01cbde3d
Autor:
Paula Mulo, Aiste Ivanauskaite, Tiina Blomster, Ari Pekka Mähönen, Kirk Overmyer, Esa Tyystjärvi, Marjaana Rantala, Magda Grabsztunowicz, Meike Burow, Katariina Vuorinen, Minna M. Koskela
Publikováno v:
Grabsztunowicz, M, Rantala, M, Ivanauskaite, A, Blomster, T, Koskela, M M, Vuorinen, K, Tyystjarvi, E, Burow, M, Overmyer, K, Mahonen, A P & Mulo, P 2021, ' Root-type ferredoxin-NADP + oxidoreductase isoforms in Arabidopsis thaliana : Expression patterns, location and stress responses ', Plant, Cell and Environment, vol. 44, no. 2, pp. 548-558 . https://doi.org/10.1111/pce.13932
In Arabidopsis, two leaf-type ferredoxin-NADP(+) oxidoreductase (LFNR) isoforms function in photosynthetic electron flow in reduction of NADP(+), while two root-type FNR (RFNR) isoforms catalyse reduction of ferredoxin in non-photosynthetic plastids.
Autor:
Magda, Grabsztunowicz, Marjaana, Rantala, Aiste, Ivanauskaite, Tiina, Blomster, Minna M, Koskela, Katariina, Vuorinen, Esa, Tyystjärvi, Meike, Burow, Kirk, Overmyer, Ari P, Mähönen, Paula, Mulo
Publikováno v:
Plant, cellenvironmentREFERENCES. 44(2)
In Arabidopsis, two leaf-type ferredoxin-NADP
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Autor:
Julian Seidel, Annika Brünje, Gautier Bernal, Dirk Schwarzer, Iris Finkemeier, Laura K Schyrba, Eric Linster, Thierry Meinnel, Ines Lassowskat, Paula Mulo, Jürgen Eirich, Jens Stephan Mühlenbeck, Minna M. Koskela, Aiste Ivanauskaite, Jean-Baptiste Boyer, Markus Wirtz, Trinh V. Dinh, Carmela Giglione, Willy V. Bienvenut, Vincent A. Jung, Cyril Dian, Rüdiger Hell
Publikováno v:
Molecular Systems Biology
Molecular Systems Biology, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, EMBO Press, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Molecular Systems Biology, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, EMBO Press, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ce91c5e79b99a8e8008cc1856cb5060
https://hal.science/hal-02900691/file/MSB-16-e9464.pdf
https://hal.science/hal-02900691/file/MSB-16-e9464.pdf
Publikováno v:
Bio Protoc
Exploring the structure and function of protein complexes requires their isolation in the native state–a task that is made challenging when studying labile and/or low abundant complexes. The difficulties in preparing membrane-protein complexes are
Autor:
Markus Nurmi, Bettina Bölter, Milagros Medina, Paula Mulo, Nina Lehtimäki, Adrián Velázquez-Campoy, Tiina A. Salminen, Minna M. Koskela, Guillermina Goñi, Käthe M. Dahlström, Guy Hanke
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Plastidic ferredoxin-NADP oxidoreductases (FNRs; EC:1.18.1.2) together with bacterial type FNRs (FPRs) form the plant-type FNR family. Members of this group contain a two-domain scaffold that forms the basis of an extended superfamily of flavin adeni
Autor:
Minna M, Koskela, Annika, Brünje, Aiste, Ivanauskaite, Magda, Grabsztunowicz, Ines, Lassowskat, Ulla, Neumann, Trinh V, Dinh, Julia, Sindlinger, Dirk, Schwarzer, Markus, Wirtz, Esa, Tyystjärvi, Iris, Finkemeier, Paula, Mulo
Publikováno v:
The Plant cell. 30(8)
The amount of light energy received by the photosynthetic reaction centers photosystem II (PSII) and photosystem I (PSI) is balanced through state transitions. Reversible phosphorylation of a light-harvesting antenna trimer (L-LHCII) orchestrates the
Autor:
Bettina Bölter, Jürgen Soll, Thomas Brylok, Elisabeth Ankele, Andreas Richter, Irene L. Gügel, Sabine Nick von Braun, Bernhard Grimm, Minna M. Koskela, Manuela Urbischek, Serena Schwenkert, Paula Mulo
Publikováno v:
Planta. 242:733-746
The extreme Alb3 C terminus is important for Alb3 stability in a light dependent manner, but is dispensable for LHCP insertion or D1 synthesis. YidC/Oxa1/Alb3 dependent insertion of membrane proteins is evolutionary conserved among bacteria, mitochon
Publikováno v:
Plant Physiology. 168:768-775
Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their importance, they are still poorly understood in plants. Although numerous reports have revealed th