Mapping the proteome of thylakoid membranes byde novo sequencing of intermembrane peptide domains

Granvogl, Bernhard; Reisinger, Veronika; Eichacker, Lutz A.

doi:10.1002/pmic.200500924

Cited by 64 publications

(51 citation statements)

References 69 publications

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“…Thylakoids were isolated from wild-type and pam71-1 leaves, solubilized, and fractionated by Blue-Native PAGE. Several prominent bands were assigned to different complexes based on earlier reports (Granvogl et al, 2006;Peng et al, 2006;Armbruster et al, 2010). The abundance of LHCII trimer complexes, as well as CP43-less PSII complexes and PSII monomer complexes, were similar in both genotypes, whereas the amounts of PSII supercomplexes and the PSII dimer/PSI monomer fraction were markedly reduced ( Figure 2A) in pam71-1 in accordance with lower steady state levels of PSII and PSI subunits ( Figure 1D).…”

Section: Changes In Thylakoid Composition and Structure In Pam71supporting

confidence: 58%

The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis

et al. 2016

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In plants, algae, and cyanobacteria, photosystem II (PSII) catalyzes the light-driven oxidation of water. The oxygen-evolving complex of PSII is a Mn 4 CaO 5 cluster embedded in a well-defined protein environment in the thylakoid membrane. However, transport of manganese and calcium into the thylakoid lumen remains poorly understood. Here, we show that Arabidopsis thaliana PHOTOSYNTHESIS AFFECTED MUTANT71 (PAM71) is an integral thylakoid membrane protein involved in Mn 2+ and Ca 2+ homeostasis in chloroplasts. This protein is required for normal operation of the oxygen-evolving complex (as evidenced by oxygen evolution rates) and for manganese incorporation. Manganese binding to PSII was severely reduced in pam71 thylakoids, particularly in PSII supercomplexes. In cation partitioning assays with intact chloroplasts, Mn 2+ and Ca 2+ ions were differently sequestered in pam71, with Ca 2+ enriched in pam71 thylakoids relative to the wild type. The changes in Ca 2+ homeostasis were accompanied by an increased contribution of the transmembrane electrical potential to the proton motive force across the thylakoid membrane. PSII activity in pam71 plants and the corresponding Chlamydomonas reinhardtii mutant cgld1 was restored by supplementation with Mn 2+ , but not Ca 2+ . Furthermore, PAM71 suppressed the Mn 2+ -sensitive phenotype of the yeast mutant Dpmr1. Therefore, PAM71 presumably functions in Mn 2+ uptake into thylakoids to ensure optimal PSII performance.

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Section: Changes In Thylakoid Composition and Structure In Pam71supporting

confidence: 58%

The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis

et al. 2016

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“…A, thylakoid membrane complexes were separated on a continuous sucrose gradient (0.1-1 M) and labeled accordingly (25). B, complexes are labeled according to their identification by mass spectrometry (37). Note slightly reduced levels of PSII supercomplexes in ⌬psbM and the higher accumulation of LHCII-containing complexes.…”

Section: Thermoluminescence Emission Reveal An Increased Ratio For Q mentioning

confidence: 99%

Deletion of PsbM in Tobacco Alters the QB Site Properties and the Electron Flow within Photosystem II

Umate

Schwenkert

Karbat

et al. 2007

Journal of Biological Chemistry

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Photosystem II, the oxygen-evolving complex of photosynthetic organisms, includes an intriguingly large number of low molecular weight polypeptides, including PsbM. Here we describe the first knock-out of psbM using a transplastomic, reverse genetics approach in a higher plant. Homoplastomic ⌬psbM plants exhibit photoautotrophic growth. Biochemical, biophysical, and immunological analyses demonstrate that PsbM is not required for biogenesis of higher order photosystem II complexes. However, photosystem II is highly light-sensitive, and its activity is significantly decreased in ⌬psbM, whereas kinetics of plastid protein synthesis, reassembly of photosystem II, and recovery of its activity are comparable with the wild type. Unlike wild type, phosphorylation of the reaction center proteins D1 and D2 is severely reduced, whereas the redox-controlled phosphorylation of photosystem II light-harvesting complex is reversely regulated in ⌬psbM plants because of accumulation of reduced plastoquinone in the dark and a limited photosystem II-mediated electron transport in the light. Charge recombination in ⌬psbM measured by thermoluminescence oscillations significantly differs from the 2/6 patterns in the wild type. A simulation program of thermoluminescence oscillations indicates a higher Q B /Q B ؊ ratio in dark-adapted mutant thylakoids relative to the wild type. The interaction of the Q A /Q B sites estimated by shifts in the maximal thermoluminescence emission temperature of the Q band, induced by binding of different herbicides to the Q B site, is changed indicating alteration of the activation energy for back electron flow. We conclude that PsbM is primarily involved in the interaction of the redox components important for the electron flow within, outward, and backward to photosystem II.

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“…Proteins are separated by their inherent negative charge (with pI,7) in CN-PAGE or by a negative charge shift provided by the CBB G-250, a negatively charged protein-binding dye in BN-PAGE (for review [144]). The combination of BN/CN-PAGE for the first dimension and denaturing SDS-PAGE in the second dimension has been successfully applied to the analysis of the mitochondrial protein complexes for which the method was designed [157][158][159], as well as to several other membrane preparations [160][161][162]. In-gel activity assays of proteins have been possible, since proteins are kept in their native and enzymatic active state [157,163].…”

Section: Membrane Proteomementioning

confidence: 99%

Two‐dimensional gel electrophoresis and mass spectrometry for biomarker discovery

Penque

2009

Proteomics Clinical Apps

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The proteome project, initiated in 1995, was made possible by 2-DE combined with MS. The project main objective was and remains the identification of all proteins expressed by a cell, tissue or organism in a given time and condition. Following this objective, the global profiling of proteins in health versus pathological state by the 2-DE/MS-based proteomic approach has contributed to the elucidation of the basic mechanisms of disease by discovering candidate disease biomarkers and disease targets for new drug development. This review will briefly summarize the historical evolution of 2-DE up to today, and review 2-DE/MS technology and its specific methods of study of immunoresponse (immunoproteomics), PTM of proteins, complex proteinprotein interactions (interactome), the proteome of cell membrane and intracellular proteome turnover in disease biomarker discovery. 2-DE historical evolutionGlobal profiling of proteins in healthy versus pathological states is a strategy to discover biomarkers for early diagnostics, disease progression, treatment response and novel targets for therapeutic drugs development. The idea of making an inventory of all the proteins in a cell, tissue or organism with normal or abnormal physiology, was (re)initiated in the middle of the 1990s with the proteome project [1]. Since then, many technologies to make the analysis of the proteome a reality have been united.The perfect technological 'marriage' that made the proteome project feasible was between high resolution 2-DE for separation of large numbers of proteins and MS for identification and characterization of the proteins displayed on this gel [2]. However, before this happy union occured, science and technology devoted to protein study had a long journey until 2-DE and MS combination was possible (Fig. 1). It started in the last century, in 1937, when Tiselius [3] introduced electrophoresis technique as a modification of Reiner's early concept (1927) [4] to analyse a complex mixture of proteins such as serum proteins. Only 20 years later, in 1959, electrophoresis on a gel support formed by crosslinked polymerization of Cyanogum 41, a commercial name for two organic monomers, acrylamide and the crosslinking agent, N,N1-methylenebisacrylamide, was shown to be useful and was named PAGE by Raymond and Weintraub [5]. The adaptation of polyacrylamide gel to IEF in a stable pH gradient, developed by Svensson in 1962 [6], was possible by the end of the 1960s [7][8][9]. About this time, the 2-D by combining IEF to separate undenatured proteins according to their charge and gradient SDS-PAGE for a second separation, according to their molecular mass, was for the first time introduced by Kenrick and Margolis (1970) [10]. Only in 1975, was IEF in denaturing conditions, as known today, used to follow the 2-D PAGE and it was described in three independent works [11][12][13]. The most powerful demonstraCorrespondence: Dr. Deborah Penque, Laboratório de Proteó-mica, Departamento de Genética, Instituto Nacional de Saúde, Dr. Ricardo Jorge, I.P., A...

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Mapping the proteome of thylakoid membranes byde novo sequencing of intermembrane peptide domains

Cited by 64 publications

References 69 publications

The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis

The Evolutionarily Conserved Protein PHOTOSYNTHESIS AFFECTED MUTANT71 is Required for Efficient Manganese Uptake at the Thylakoid Membrane in Arabidopsis

Deletion of PsbM in Tobacco Alters the QB Site Properties and the Electron Flow within Photosystem II

Two‐dimensional gel electrophoresis and mass spectrometry for biomarker discovery

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