BBA - Bioenergetics (v.1857, #3)
Editorial Board (i).
Preface to BBA special issue: “Organisation and dynamics of bioenergetic systems in bacteria” by Conrad W. Mullineaux (189).
Supramolecular organization of bacterial aerobic respiratory chains: From cells and back by Ana M.P. Melo; Miguel Teixeira (190-197).
Aerobic respiratory chains from all life kingdoms are composed by several complexes that have been deeply characterized in their isolated form. These membranous complexes link the oxidation of reducing substrates to the reduction of molecular oxygen, in a process that conserves energy by ion translocation between both sides of the mitochondrial or prokaryotic cytoplasmatic membranes. In recent years there has been increasing evidence that those complexes are organized as supramolecular structures, the so-called supercomplexes and respirasomes, being available for eukaryotes strong data namely obtained by electron microscopy and single particle analysis. A parallel study has been developed for prokaryotes, based on blue native gels and mass spectrometry analysis, showing that in these more simple unicellular organisms such supercomplexes also exist, involving not only typical aerobic-respiration associated complexes, but also anaerobic-linked enzymes. After a short overview of the data on eukaryotic supercomplexes, we will analyse comprehensively the different types of prokaryotic aerobic respiratory supercomplexes that have been thus far suggested, in both bacteria and archaea. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof Conrad Mullineaux.
Keywords: Supercomplex; Bacteria; Respiratory chain; Escherichia coli; Bacillus subtilis; Microbiology;
Distribution and dynamics of OXPHOS complexes in the bacterial cytoplasmic membrane by Axel Magalon; François Alberge (198-213).
Oxidative phosphorylation (OXPHOS) is an essential process for most living organisms mostly sustained by protein complexes embedded in the cell membrane. In order to thrive, cells need to quickly respond to changes in the metabolic demand or in their environment. An overview of the strategies that can be employed by bacterial cells to adjust the OXPHOS outcome is provided. Regulation at the level of gene expression can only provide a means to adjust the OXPHOS outcome to long-term trends in the environment. In addition, the actual view is that bioenergetic membranes are highly compartmentalized structures. This review discusses what is known about the spatial organization of OXPHOS complexes and the timescales at which they occur. As exemplified with the commensal gut bacterium Escherichia coli, three levels of spatial organization are at play: supercomplexes, membrane microdomains and polar assemblies. This review provides a particular focus on whether dynamic spatial organization can fine-tune the OXPHOS through the definition of specialized functional membrane microdomains. Putative mechanisms responsible for spatio-temporal regulation of the OXPHOS complexes are discussed. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: OXPHOS complexes; Bacteria; Aerobic and anaerobic OXPHOS; Supercomplexes; Nitrate reductase; Fluorescence microscopy; Functional membrane microdomains;
Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I) by Thorsten Friedrich; Doris Kreuzer Dekovic; Sabrina Burschel (214-223).
Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, couples the electron transfer from NADH to ubiquinone with the translocation of four protons across the membrane. The Escherichia coli complex I is made up of 13 different subunits encoded by the so-called nuo-genes. The electron transfer is catalyzed by nine cofactors, a flavin mononucleotide and eight iron–sulfur (Fe/S)-clusters. The individual subunits and the cofactors have to be assembled together in a coordinated way to guarantee the biogenesis of the active holoenzyme. Only little is known about the assembly of the bacterial complex compared to the mitochondrial one. Due to the presence of so many Fe/S-clusters the assembly of complex I is intimately connected with the systems responsible for the biogenesis of these clusters. In addition, a few other proteins have been reported to be required for an effective assembly of the complex in other bacteria. The proposed role of known bacterial assembly factors is discussed and the information from other bacterial species is used in this review to draw an as complete as possible model of bacterial complex I assembly. In addition, the supramolecular organization of the complex in E. coli is briefly described. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof. Conrad Mullineaux.
Keywords: Escherichia coli; Complex I, NADH dehydrogenase; NADH:ubiquinone oxidoreductase; Assembly; Iron–sulfur cluster;
Single-molecule studies of the dynamics and interactions of bacterial OXPHOS complexes by Tchern Lenn; Mark C. Leake (224-231).
Although significant insight has been gained into biochemical, genetic and structural features of oxidative phosphorylation (OXPHOS) at the single-enzyme level, relatively little was known of how the component complexes function together in time and space until recently. Several pioneering single-molecule studies have emerged over the last decade in particular, which have illuminated our knowledge of OXPHOS, most especially on model bacterial systems. Here, we discuss these recent findings of bacterial OXPHOS, many of which generate time-resolved information of the OXPHOS machinery with the native physiological context intact. These new investigations are transforming our knowledge not only of the molecular arrangement of OXPHOS components in live bacteria, but also of the way components dynamically interact with each other in a functional state. These new discoveries have important implications towards putative supercomplex formation in bacterial OXPHOS in particular. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Fluorescent protein; Supercomplexes; E. coli; Single particle tracking; Localization microscopy; Super-resolution;
Development and dynamics of the photosynthetic apparatus in purple phototrophic bacteria by Robert A. Niederman (232-246).
The purple bacterium Rhodobacter sphaeroides provides a useful model system for studies of the assembly and dynamics of bacterial photosynthetic membranes. For the nascent developing membrane, proteomic analyses showed an ~ 2-fold enrichment in general membrane assembly factors, compared to chromatophores. When the protonophore carbonyl-cyanide m-chlorophenyl-hydrazone (CCCP) was added to an ICM inducing culture, an ~ 2-fold elevation in spectral counts vs. the control was seen for the SecA translocation ATPase, the preprotein translocase SecY, SecD and SecF insertion components, and chaperonins DnaJ and DnaK, which act early in the assembly process. It is suggested that these factors accumulated with their nascent polypeptides, as putative assembly intermediates in a functionally arrested state. Since in Synechocystis PCC 6803, a link has been established between Chl delivery involving the high-light HilD protein and the SecY/YidC-requiring cotranslational insertion of nascent polypeptides, such a connection between BChl biosynthesis and insertion and folding of nascent Rba. sphaeroides BChl binding proteins is likely to also occur. AFM imaging studies of the formation of the reaction center (RC)–light harvesting 1 (LH1) complex suggested a cooperative assembly mechanism in which, following the association between the RC template and the initial LH1 unit, addition of successive LH1 units to the RC drives the assembly process to completion. Alterations in membrane dynamics as the developing membrane becomes filled with LH2-rings were assessed by fluorescence induction/relaxation kinetics, which showed a slowing in RC electron transfer rate thought to mainly reflect alterations in donor side electron transfer. This was attributed to an increased distance for electron flow in cytochrome c 2 between the RC and cytochrome bc 1 complexes, as suggested in the current structural models. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof Conrad Mullineaux.Display Omitted
Keywords: Atomic force microscopy; Bacterial photosynthesis; Light-harvesting; Reaction center; Membrane assembly; Membrane dynamics;
Photosynthetic, respiratory and extracellular electron transport pathways in cyanobacteria by David J. Lea-Smith; Paolo Bombelli; Ravendran Vasudevan; Christopher J. Howe (247-255).
Cyanobacteria have evolved elaborate electron transport pathways to carry out photosynthesis and respiration, and to dissipate excess energy in order to limit cellular damage. Our understanding of the complexity of these systems and their role in allowing cyanobacteria to cope with varying environmental conditions is rapidly improving, but many questions remain. We summarize current knowledge of cyanobacterial electron transport pathways, including the possible roles of alternative pathways in photoprotection. We describe extracellular electron transport, which is as yet poorly understood. Biological photovoltaic devices, which measure electron output from cells, and which have been proposed as possible means of renewable energy generation, may be valuable tools in understanding cyanobacterial electron transfer pathways, and enhanced understanding of electron transfer may allow improvements in the efficiency of power output. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Terminal oxidase; Flavodiiron; Biophotovoltaic; Photoprotection; Photosynthetic electron transfer; Respiration;
Distribution and dynamics of electron transport complexes in cyanobacterial thylakoid membranes by Lu-Ning Liu (256-265).
The cyanobacterial thylakoid membrane represents a system that can carry out both oxygenic photosynthesis and respiration simultaneously. The organization, interactions and mobility of components of these two electron transport pathways are indispensable to the biosynthesis of thylakoid membrane modules and the optimization of bioenergetic electron flow in response to environmental changes. These are of fundamental importance to the metabolic robustness and plasticity of cyanobacteria. This review summarizes our current knowledge about the distribution and dynamics of electron transport components in cyanobacterial thylakoid membranes. Global understanding of the principles that govern the dynamic regulation of electron transport pathways in nature will provide a framework for the design and synthetic engineering of new bioenergetic machinery to improve photosynthesis and biofuel production. This article is part of a Special Issue entitled: Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Cyanobacteria; Electron transport; Membrane protein; Photosynthesis; Protein distribution; Protein dynamics; Respiration; Supramolecular complex; Thylakoid membrane;
Protein translocation and thylakoid biogenesis in cyanobacteria by Kelly M. Frain; Doris Gangl; Alexander Jones; Julie A.Z. Zedler; Colin Robinson (266-273).
Cyanobacteria exhibit a complex form of membrane differentiation that sets them apart from most bacteria. Many processes take place in the plasma membrane, but photosynthetic light capture, electron transport and ATP synthesis take place in an abundant internal thylakoid membrane. This review considers how this system of subcellular compartmentalisation is maintained, and how proteins are directed towards the various subcompartments — specifically the plasma membrane, periplasm, thylakoid membrane and thylakoid lumen. The involvement of Sec-, Tat- and signal recognition particle- (SRP)-dependent protein targeting pathways is discussed, together with the possible involvement of a so-called ‘spontaneous’ pathway for the insertion of membrane proteins, previously characterised for chloroplast thylakoid membrane proteins. An intriguing aspect of cyanobacterial cell biology is that most contain only a single set of genes encoding Sec, Tat and SRP components, yet the proteomes of the plasma and thylakoid membranes are very different. The implications for protein sorting mechanisms are considered. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof Conrad Mullineaux.Display Omitted
Keywords: Cyanobacteria; Protein translocation; Membrane biogenesis; Sec; Tat; SRP;
Analysis of photosystem II biogenesis in cyanobacteria by Steffen Heinz; Pasqual Liauw; Jörg Nickelsen; Marc Nowaczyk (274-287).
Photosystem II (PSII), a large multisubunit membrane protein complex found in the thylakoid membranes of cyanobacteria, algae and plants, catalyzes light-driven oxygen evolution from water and reduction of plastoquinone. Biogenesis of PSII requires coordinated assembly of at least 20 protein subunits, as well as incorporation of various organic and inorganic cofactors. The stepwise assembly process is facilitated by numerous protein factors that have been identified in recent years. Further analysis of this process requires the development or refinement of specific methods for the identification of novel assembly factors and, in particular, elucidation of the unique role of each. Here we summarize current knowledge of PSII biogenesis in cyanobacteria, focusing primarily on the impact of methodological advances and innovations. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Cyanobacteria; Photosystem II assembly; Thylakoid membrane; SPR; Membrane fractionation; CX-MS;
Cyanobacterial high-light-inducible proteins — Protectors of chlorophyll–protein synthesis and assembly by Josef Komenda; Roman Sobotka (288-295).
Cyanobacteria contain a family of genes encoding one-helix high-light-inducible proteins (Hlips) that are homologous to light harvesting chlorophyll a/b-binding proteins of plants and algae. Based on various experimental approaches used for their study, a spectrum of functions that includes regulation of chlorophyll biosynthesis, transient chlorophyll binding, quenching of singlet oxygen and non-photochemical quenching of absorbed energy is ascribed to Hlips. However, these functions had not been supported by conclusive experimental evidence until recently when it became clear that Hlips are able to quench absorbed light energy and assist during terminal step(s) of the chlorophyll biosynthesis and early stages of Photosystem II assembly. In this review we summarize and discuss the present knowledge about Hlips and provide a model of how individual members of the Hlip family operate during the biogenesis of chlorophyll–proteins, namely Photosystem II. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Chlorophyll; Cyanobacteria; High-light-inducible protein; Photosynthesis; Small Cab-like protein; Synechocystis sp. PCC 6803;
Transcriptional and posttranscriptional regulation of cyanobacterial photosynthesis by Annegret Wilde; Yukako Hihara (296-308).
Cyanobacteria are well established model organisms for the study of oxygenic photosynthesis, nitrogen metabolism, toxin biosynthesis, and salt acclimation. However, in comparison to other model bacteria little is known about regulatory networks, which allow cyanobacteria to acclimate to changing environmental conditions. The current work has begun to illuminate how transcription factors modulate expression of different photosynthetic regulons. During the past few years, the research on other regulatory principles like RNA-based regulation showed the importance of non-protein regulators for bacterial lifestyle. Investigations on modulation of photosynthetic components should elucidate the contributions of all factors within the context of a larger regulatory network.Here, we focus on regulation of photosynthetic processes including transcriptional and posttranscriptional mechanisms, citing examples from a limited number of cyanobacterial species. Though, the general idea holds true for most species, important differences exist between various organisms, illustrating diversity of acclimation strategies in the very heterogeneous cyanobacterial clade. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof Conrad Mullineaux.
Keywords: Cyanobacteria; Photosynthesis; Two-component system; RNA regulation; High-light acclimation;
Thylakoid membrane function in heterocysts by Ann Magnuson; Tanai Cardona (309-319).
Multicellular cyanobacteria form different cell types in response to environmental stimuli. Under nitrogen limiting conditions a fraction of the vegetative cells in the filament differentiate into heterocysts. Heterocysts are specialized in atmospheric nitrogen fixation and differentiation involves drastic morphological changes on the cellular level, such as reorganization of the thylakoid membranes and differential expression of thylakoid membrane proteins. Heterocysts uphold a microoxic environment to avoid inactivation of nitrogenase by developing an extra polysaccharide layer that limits air diffusion into the heterocyst and by upregulating heterocyst-specific respiratory enzymes. In this review article, we summarize what is known about the thylakoid membrane in heterocysts and compare its function with that of the vegetative cells. We emphasize the role of photosynthetic electron transport in providing the required amounts of ATP and reductants to the nitrogenase enzyme. In the light of recent high-throughput proteomic and transcriptomic data, as well as recently discovered electron transfer pathways in cyanobacteria, our aim is to broaden current views of the bioenergetics of heterocysts. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.
Keywords: Cyanobacteria; Heterocysts; Nitrogen fixation; Photosystem I; Photosystem II; Phycobilisome;