Výsledky vyhledávání - "Matthias, Plöscher"

Proteomic comparison of etioplast and chloroplast protein complexes

Autor: Veronika Reisinger, Matthias Plöscher, Lutz A. Eichacker

Publikováno v: Journal of Proteomics. 74:1256-1265

Angiosperms grown in darkness develop etioplasts during skotomorphogenesis. It is well known that etioplasts accumulate large quantities of protochlorophyllideoxidoreductase, are devoid of chlorophyll and are the site to assemble the photosynthetic m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::374d1b7256ce4dfb596f71a7b69d9f09
https://doi.org/10.1016/j.jprot.2011.03.020

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Phycourobilin in Trichromatic Phycocyanin from Oceanic Cyanobacteria Is Formed Post-translationally by a Phycoerythrobilin Lyase-Isomerase

Autor: Matthias Plöscher, Kai-Hong Zhao, Ming Zhou, Nicolas Blot, Laurence Garczarek, Jun-Ming Tu, Juan Zhang, Frédéric Partensky, Lutz A. Eichacker, Hugo Scheer, Stephan H. Bohm, Jean-Claude Thomas, Xian-Jun Wu

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (14), pp.9290-8. ⟨10.1074/jbc.M809784200⟩
Journal of Biological Chemistry, 2009, 284 (14), pp.9290-8. ⟨10.1074/jbc.M809784200⟩

International audience; Most cyanobacteria harvest light with large antenna complexes called phycobilisomes. The diversity of their constituting phycobiliproteins contributes to optimize the photosynthetic capacity of these microorganisms. Phycobilip

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d3e6774743b695e09d5d09439d85bf9
https://doi.org/10.1074/jbc.m809784200

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Identification of the N-termini of NADPH : protochlorophyllide oxidoreductase A and B from barley etioplasts (Hordeum vulgare L.)

Autor: Lutz A. Eichacker, Bernhard Granvogl, Matthias Plöscher, Veronika Reisinger

Publikováno v: FEBS Journal. 276:1074-1081

The N-termini of the NADPH : protochlorophyllide oxidoreductase (POR) proteins A and B from barley and POR from pea were determined by acetylation of the proteins and selective isolation of the N-terminal peptides for mass spectrometry de novo sequen

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https://doi.org/10.1111/j.1742-4658.2008.06850.x

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Localization of 13 one-helix integral membrane proteins in photosystem II subcomplexes

Autor: Bernhard Granvogl, Mikael Zoryan, Matthias Plöscher, Lutz A. Eichacker

Publikováno v: Analytical Biochemistry. 383:279-288

Photosystem II is a multimeric protein complex of the thylakoid membrane in chloroplasts. Approximately half of the at least 26 different integral membrane protein subunits have molecular masses lower than 10 kDa. After one-dimensional (1D) or two-di

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https://doi.org/10.1016/j.ab.2008.08.038

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Identification and analysis of four candidate symbiosis genes from ‘Chlorochromatium aggregatum’, a highly developed bacterial symbiosis

Autor: Roland Wenter, Martina Dreßen, Jörg Overmann, Lutz A. Eichacker, Kajetan Vogl, Matthias Plöscher, Martina Schlickenrieder

Publikováno v: Environmental Microbiology. 10:2842-2856

The consortium 'Chlorochromatium aggregatum' currently represents the most highly developed interspecific association between prokaryotes. It consists of green sulfur bacteria, so-called epibionts, which surround a central, motile, chemotrophic bacte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::63ecd866f98aaa57273f871241ca710c
https://doi.org/10.1111/j.1462-2920.2008.01709.x

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Cytochrome b6f is a dimeric protochlorophyll a binding complex in etioplasts

Autor: Matthias Plöscher, Lutz A. Eichacker, Alexander P. Hertle, Veronika Reisinger

Publikováno v: FEBS Journal. 275:1018-1024

The cytochrome b6f complex is a dimeric protein complex that is of central importance for photosynthesis to carry out light driven electron and proton transfer in chloroplasts. One molecule of chlorophyll a was found to associate per cytochrome b6f m

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https://doi.org/10.1111/j.1742-4658.2008.06268.x

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Intermediate binding of phycocyanobilin to the lyase, CpeS1, and transfer to apoprotein

Autor: Kai-Hong Zhao, Stephan H. Bohm, Hugo Scheer, Jun-Ming Tu, Michaela Kupka, Matthias Plöscher, Lutz A. Eichacker

Publikováno v: Photosynthesis Research. 95:163-168

The phycobilin: Cysteine-84-phycobiliprotein lyase, CpeS1, catalyzes phycocyanobilin (PCB) and phycoerythrobilin attachment to nearly all cysteine-84 (consensus sequence) binding sites of phycoerythrin, phycoerythrocyanin, phycocyanin and allophycocy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35e56b361302fa9daad2cbdc8a9c3082
https://doi.org/10.1007/s11120-007-9251-4

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Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins

Autor: Jun-Ming Tu, Lutz A. Eichacker, Bei Yang, Ping Su, Matthias Plöscher, Xing Wang, Ming Zhou, Hui Liu, Kai-Hong Zhao, Hugo Scheer

Publikováno v: Proceedings of the National Academy of Sciences. 104:14300-14305

Phycobilisomes, the light-harvesting complexes of cyanobacteria and red algae, contain two to four types of chromophores that are attached covalently to seven or more members of a family of homologous proteins, each carrying one to four binding sites

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https://doi.org/10.1073/pnas.0706209104

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The proteome of the heterocyst cell wall in Anabaena sp. PCC 7120

Autor: Matthias Berg, Enrique Flores, Suncana Moslavac, Enrico Schleiff, Oliver Vosyka, Oliver Mirus, Veronika Reisinger, Matthias Plöscher, Lutz A. Eichacker

Publikováno v: bchm. 388:823-829

Anabaena sp. PCC 7120 is a filamentous cyanobacterium that serves as a model to analyze prokaryotic cell differentiation, evolutionary development of plastids, and the regulation of nitrogen fixation. The cell wall is the cellular structure in contac

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https://doi.org/10.1515/bc.2007.079

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Sample preparation by in-gel digestion for mass spectrometry-based proteomics

Autor: Matthias Plöscher, Lutz A. Eichacker, Bernhard Granvogl

Publikováno v: Analytical and Bioanalytical Chemistry. 389:991-1002

The proteomic characterization of proteins and protein complexes from cells and cell organelles is the next challenge for investigation of the cell. After isolation of the cell compartment, three steps have to be performed in the laboratory to yield

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c14af00a12fa570c030b4262aa697e5
https://doi.org/10.1007/s00216-007-1451-4

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