Effect of berry maturity stages on the germination and protein constituents of African nightshade (Solanum scabrum) seeds.

African nightshade (Solanum scabrum) is a vegetable of great importance in several African countries. Production by seed is constrained by limited access to high quality seed, leaving farmers unable to meet the growing demand. The aim of this study was to investigate effects of berry maturity stages (mature green and purple) on germination and protein components of African nightshade seeds.

Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum.

Marine photosynthetic (micro)organisms drive multiple biogeochemical cycles and display a large diversity. Among them, the bloom-forming, free-living dinoflagellate Prorocentrum cordatum CCMP 1329 (formerly P. minimum) stands out with its distinct cell biological features.

The enigmatic nucleus of the marine dinoflagellate .

The marine, bloom-forming dinoflagellate CCMP 1329 (formerly ) has a genome atypical of eukaryotes, with a large size of ~4.15 Gbp, organized in plentiful, highly condensed chromosomes and packed in a dinoflagellate-specific nucleus (dinokaryon). Here, we apply microscopic and proteogenomic approaches to obtain new insights into this enigmatic nucleus of axenic .

Cryo-EM structure of the respiratory I + III supercomplex from Arabidopsis thaliana at 2 Å resolution.

Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.

Changes in leaf ecophysiological traits and proteome profile provide new insights into variability of salt response in the succulent halophyte .

Natural variability of stress tolerance in halophytic plants is of significance both ecologically and in view of identifying molecular traits for salt tolerance in plants. Using ecophysiological and proteomic analyses, we address these phenomena in two Tunisian accessions of the oilseed halophyte, Cakile maritima Scop., thriving on arid and semi-arid Mediterranean bioclimatic stages (Djerba and Raoued, respectively), with a special emphasis on the leaves.

The gene space of European mistletoe (Viscum album).

European mistletoe (Viscum album) is a hemiparasitic flowering plant that is known for its very special life cycle and extraordinary biochemical properties. Particularly, V. album has an unusual mode of cellular respiration that takes place in the absence of mitochondrial complex I.

A ferredoxin bridge connects the two arms of plant mitochondrial complex I.

Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp.

One C-to-U RNA Editing Site and Two Independently Evolved Editing Factors: Testing Reciprocal Complementation with DYW-Type PPR Proteins from the Moss () and the Flowering Plants and Arabidopsis.

Cytidine-to-uridine RNA editing is a posttranscriptional process in plant organelles, mediated by specific pentatricopeptide repeat (PPR) proteins. In angiosperms, hundreds of sites undergo RNA editing. By contrast, only 13 sites are edited in the moss () Some are conserved between the two species, like the mitochondrial editing site nad5eU598RC.

Recovery aptitude of the halophyte Cakile maritima upon water deficit stress release is sustained by extensive modulation of the leaf proteome.

Among the most intriguing features characterizing extremophile plants is their ability to rapidly recover growth activity upon stress release. Here, we investigated the responses of the halophyte C. maritima to drought and recovery at both physiological and leaf proteome levels.

Comparative analysis of salt-induced changes in the root proteome of two accessions of the halophyte Cakile maritima.

NaCl stress is a major abiotic stress factor limiting the productivity and the geographical distribution of many plant species. Although halophytes are able to withstand and even to require salt in the rhizosphere, roots are the most sensitive organs to salinity. Here, we investigate the variability of salt tolerance in two Tunisian accessions of the halophyte Cakile maritima (Raoued and Djerba, harvested from the semi-arid and arid Mediterranean bioclimatic stages, respectively) with a special emphasis on the proteomic changes in roots.

Absence of Complex I Implicates Rearrangement of the Respiratory Chain in European Mistletoe.

The mitochondrial oxidative phosphorylation (OXPHOS) system, which is based on the presence of five protein complexes, is in the very center of cellular ATP production. Complexes I to IV are components of the respiratory electron transport chain that drives proton translocation across the inner mitochondrial membrane. The resulting proton gradient is used by complex V (the ATP synthase complex) for the phosphorylation of ADP.

Structure and function of complex I in animals and plants - a comparative view.

The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40-50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position.

SDH6 and SDH7 Contribute to Anchoring Succinate Dehydrogenase to the Inner Mitochondrial Membrane in Arabidopsis thaliana.

The succinate dehydrogenase complex (complex II) is a highly conserved protein complex composed of the SDH1 to SDH4 subunits in bacteria and in the mitochondria of animals and fungi. The reason for the occurrence of up to four additional subunits in complex II of plants, termed SDH5 to SDH8, so far is a mystery. Here, we present a biochemical approach to investigate the internal subunit arrangement of Arabidopsis (Arabidopsis thaliana) complex II.

The mitochondrial complexome of Arabidopsis thaliana.

Mitochondria are central to cellular metabolism and energy conversion. In plants they also enable photosynthesis through additional components and functional flexibility. A majority of those processes relies on the assembly of individual proteins to larger protein complexes, some of which operate as large molecular machines.

Differential proteomics analysis of Frankliniella occidentalis immune response after infection with Tomato spotted wilt virus (Tospovirus).

Tomato spotted wilt virus (TSWV) is mainly vectored by Frankliniella occidentalis Pergande, and it potentially activates the vector's immune response. However, molecular background of the altered immune response is not clearly understood. Therefore, using a proteomic approach, we investigated the immune pathways that are activated in F.

Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex.

The mitochondrial NADH dehydrogenase complex (complex I) is of particular importance for the respiratory chain in mitochondria. It is the major electron entry site for the mitochondrial electron transport chain (mETC) and therefore of great significance for mitochondrial ATP generation. We recently described an Arabidopsis thaliana double-mutant lacking the genes encoding the carbonic anhydrases CA1 and CA2, which both form part of a plant-specific 'carbonic anhydrase domain' of mitochondrial complex I.

The carbonic anhydrase domain of plant mitochondrial complex I.

The mitochondrial NADH dehydrogenase complex (complex I) consists of several functional domains which independently arose during evolution. In higher plants, it contains an additional domain which includes proteins resembling gamma-type carbonic anhydrases. The Arabidopsis genome codes for five complex I-integrated gamma-type carbonic anhydrases (γCA1, γCA2, γCA3, γCAL1, γCAL2), but only three copies of this group of proteins form an individual extra domain.