Centrum Algatech

Mikrobiologický ústav AV ČR, v.v.i. - vědecké pracoviště Třeboň

Publikace

LaboratořCitaceRok
Laboratoř fotosyntézy
Skupina Romana Sobotky

Sobotka, R: Making proteins green; biosynthesis of chlorophyll-binding proteins in cyanobacteria. Photosynthesis Research 119, 223-232, 2014.


2014
Laboratoř fotosyntézy
Skupina Romana Sobotky

Sobotka, R., Komenda, J., Bumba, L., Tichý, M. (2005) Photosystem II assembly in CP47 mutant of Synechocystis sp. PCC 6803 is dependent on the level of chlorophyll precursors regulated by ferrochelatase. Journal of Biological Chemistry 280, 31595-31602.


2005
Laboratoř fotosyntézy
Skupina Romana Sobotky

Sobotka, R., Dühring, U., Komenda, J., Peter, E., Gardian, Z., Tichý, M., Grimm, B., Wilde, A. (2008) Improtance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes. Journal of Biological Chemistry 283, 25794-25802.


2008
Laboratoř fotosyntézy
Skupina Romana Sobotky

Sobotka, R., McLean, S., Žuberová, M., Hunter, C.N., Tichý, M. (2008) The C-Terminal extension of ferrochelatase is critical for enzyme aktivity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803. Journal of Bacteriology 190, 2086-2095.


2008
Laboratoř fotosyntézy
Skupina Romana Sobotky

Dobáková, M., Sobotka, R., Tichý, M., Komenda, J. (2009) Psb28 protein is i volved in the biogenesis of the photosystem II inner antenna CP47 (PsbB) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiology 149, 1076-1086.


2009
Laboratoř fotosyntézy
Skupina Romana Sobotky

Sobotka, R, Tichý, M, Wilde, A, Hunter, AN: Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis1[W]. Plant Physiology 155, 1735-1747, 2011.


2011
Laboratoř fotosyntézy
Skupina Romana Sobotky

Wallner, T, Hagiwara, Y, Bernát, G, Sobotka, R, Reijerse, EJ, Frankenberg-Dinkel, N, Wilde, A: Inactivation of the conserved open reading frame ycf34 of Synechocystis sp. PCC6803 interferes dwith the photosynthetic electron transport chain. Biochimica et Biophysica Acta 1817, 2016-2026, 2012.


2012
Laboratoř fotosyntézy
Skupina Romana Sobotky

Kopečná, J, Komenda, J, Bučinská, L, Sobotka, R: Long-term acclimation of the cyanobacterium Synechocystis PCC6803 to high light is accompanied by an enhanced production of chlorophyll that is preferentially channeled to trimeric PSI. Plant Physiology 160, 2239-2250, 2012.


2012
Laboratoř fotosyntézy
Skupina Romana Sobotky

Kafková, L, Ammerman, ML, Faktorová, D, Fisk, JC, Zimmer, SL, Sobotka, R, Read, LK, Lukeš, J, Hashimi, H: Functional characterization of two paralogs that are novel RNA binding proteins influencing mitochondrial transcripts of Trypanosoma brucei. RNA 18, 1846-1861, 2012.


2012
Laboratoř fotosyntézy
Skupina Romana Sobotky

Hollingshead, S, Kopečná, J, Jackson, PJ, Canniffe, DP, Davidson, PA, Dickman, MJ, Sobotka, R, Hunter, CN: Conserved chloroplast open-reading freame ycf54 is required for activity of the magnesium protoporphyrin  monomethylester oxidative cyclase in Synechocystis PCC 6803. Journal of Biological Chemistry 287, 27823-27833, 2012.


2012
Laboratoř fotosyntézy
Skupina Radka Kani

Kaňa, R., Prášil, O., Komárek, O., Papageorgiou, G.C., Govindjee: Spectral characteristic of luorescence induction in a model cyanobacterium, Synechococcus sp. (PCC 7942). – Biochimica et Biophysica Acta – Bioenergetics 1787, 1170-1178, 2009.


2009
Laboratoř fotosyntézy
Skupina Ondřeje Prášila

Hála J., Vácha M., Dian J., Ambrož M., Adamec F., Prášil O., Komenda J., Nedbal L., Vácha F., Mareš J.: Structure and function of photosynthetic systems studied by hole burning spectroscopy. - J. Luminescence 48 and 49, 295-298, 1991.


1991
Laboratoř fotosyntézy
Skupina Josefa Komendy

Komenda, J., Tichý, M., Prášil, O., Knoppová, J., Kuviková, S., de Vries, R., Nixon, P.J. (2007) The exposed N-terminal tail of the D1 subunit is required for rapid D1 degradation during Photosystem II reapir in Synechocystis sp. PCC 6803. Plant Cell 19, 2839-2854


2007
Laboratoř fotosyntézy
Skupina Josefa Komendy

Komenda, J., Knoppová, J., Krynická, V., Nixon, P.J., Tichý, M.: Role of FtsH2 in the repair of Photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assenmbly or stability of the CaMn4 cluster. – Biochimica et Biophysica Acta 1797, 566-275, 2010.


2010
Laboratoř fotosyntézy
Skupina Josefa Komendy

Kopečná, J, Sobotka, R, Komenda, J: Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem I and Photosystem II in the cyanobacterium Synechocystis PCC 6803. Planta 237, 497-508, 2013.


2013
Laboratoř řasové biotechnologie
Skupina Jiřího Masojídka

Jones H.G., Massacci A., Corlett J., Masojídek J., Hall D.: Use of combined fluorescence and gas-exchange measurements to assess processes limiting photosynthesis under stress. - Bull. Soc. bot., Fr., 137, Actual bot. 1: 67-72, 1990.


1990
Laboratoř řasové biotechnologie
Skupina Jiřího Masojídka

Droppa M., Masojídek J., Horváth G.: Changes of the polypeptide composition in thylakoid membranes during differentiation. - Z. Naturforsch. 45c: 253-257, 1990.


1990
Laboratoř řasové biotechnologie
Skupina Jiřího Masojídka

Knoppová J., Masojídek J., Pokorný J.: Chlorophyll fluorescence quenching caused by inorganic carbon depletion in the green alga Scenedesmus quadricauda. - Photosynthetica 28(4): 541-547, 1993.


1993
Laboratoř fotosyntézy
Skupina Jana Janouškovce

Moore, RB, Oborník, M, Janouškovec, J, Chrudimský, T, Vancová, M, Green, DH, Wright, SW, Davies, NW, Bolch, CJS, Heimann, K, Slapeta, J, Hoegh-Guldberg, O, Logsdon, JM, Carter, DA*: A photosynthetic alveolate closely related to apicomplexan parasites. Nature 451, 959–63, 2008. https://doi.org/10.1038/nature06635


2008
Laboratoř fotosyntézy
Skupina Jana Janouškovce

Zrzavý, J*, Říha, P, Piálek, L, Janouškovec, J: Phylogeny of Annelida (Lophotrochozoa): total-evidence analysis of morphology and six genes. BMC Evolutionary Biology 9, 189, 2009. https://doi.org/10.1186/1471-2148-9-189


2009
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