Structures of Anabaena Calcium-binding Protein CcbP

Hu, Yunfei; Zhang, Xinxin; Shi, Yunming; Zhou, Yanfeng; Zhang, Wei; Xia, Bin; Zhao, Jindong; Jin, Changwen

doi:10.1074/jbc.m110.201186

Cited by 23 publications

(13 citation statements)

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“…An outstanding question relates to the evolution of CSE, which appears almost exclusively in filamentous, N-fixing cyanobacteria. Changes in [Ca 2+ ]i in Anabaena have been linked to the differentiation of vegetative cells into heterocysts under N-deficient conditions [48,53], and appear to play a role in communicating C:N homeostasis [30]. The current work shows that CSE overabundance does not affect normal heterocyst differentiation and nitrogenase activity; however, the observed effects on photosynthetic activity may be expected to downregulate carbon metabolism and thereby impact C:N balance.…”

Section: Discussionmentioning

confidence: 59%

“…Figure S2). It was reported previously that NaCl can inhibit Ca 2+ -binding of the Anabaena Ca 2+ -binding protein CcbP [48], therefore the Ca 2+ -and Mg 2+ -binding properties of asr1131 were examined in the absence/presence of NaCl. In absence of NaCl, titration of asr1131 with ∼5 µM CaCl2 per injection yielded exothermic calorimetric signals that saturated at a molar ratio of 1.11 ( Figure 2D).…”

Section: In Vitro Biochemical Properties Of Recombinant Asr1131 Proteinmentioning

confidence: 99%

See 1 more Smart Citation

A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

Walter

Selim

Leganés

et al. 2019

Preprint

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Ca 2+ is a potent signalling molecule that regulates many cellular processes. In cyanobacteria, Ca 2+ has been linked to cell growth, stress response and photosynthesis, and to the development of specialist heterocyst cells in certain nitrogen-fixing species. Despite this, the pathways of calcium signal transduction in cyanobacteria are poorly understood, and only a few protein components are known. The current study describes a previously unreported calcium-binding protein which was called the Calcium Sensor EF-hand (CSE), which is conserved in filamentous, nitrogen-fixing cyanobacteria. CSE is shown to bind calcium, which induces a conformational change in the protein structure. Poor growth of a strain of Anabaena sp. PCC 7120 overexpressing CSE was attributed to diminished photosynthetic performance. Transcriptomics, biophysics and proteomics analyses revealed modifications in the light-harvesting phycobilisome and photosynthetic reaction centerprotein complexes, and downregulated respiration. thylakoid membrane, with a special type of PBS being connected to PSI [20]. In Synechocystis sp.PCC 6803, even a megacomplex composed of PBS-PSII-PSI has been reported [21]. PBS are composed of different phycobilin pigment-binding proteins (PBP) and linker proteins, which are organised in allophycocyanin (APC) core cylinders connected to the photosystem reaction centres, and peripheral rod-shaped antennae linked to the APC core. The rods consist of core-connected phycocyanin (PC) discs, while some strains have additional phycoerythrocyanin (PEC) discs at the distal end of each rod [reviewed in 22]. Depending on the cyanobacterial species, the PBS composition and structure can differ in the number and type of PBPs, the type of bound chromophores (pigments) and the number of rods and core cylinders per PBS. In the multicellular model organism Nostoc sp. PCC 7120 (herein referred to as Anabaena), the APC core contains five cylinders from which eight rods radiate. APC, PC and PEC bind different numbers of the chromophore phycocyanobilin (PCB), resulting in different spectral features for each PBP. PEC absorbs light of shorter wavelengths (absorption maximum at 570 nm), whereas APC absorbs light of longer wavelengths (absorption maximum at 650 nm) [23]. Excitation energy is transferred from PEC via PC and APC to the terminal emitter ApcE, which is a pigmented core-membrane linker protein (LCM) connected to the PSII reaction centre in close proximity to CP43 [21,24,25]. Similarly, the terminal emitter ApcD connects PBS to PSI via hydrophobic interactions at the interface of two PSI monomers [20,21,26].Other linker proteins that do not bind pigments connect the discs, rods and cores within the PBS, to form complexes of around 6 000 kDa [24,27,28].In this study, we present a previously undescribed EF-hand protein that is highly conserved in filamentous cyanobacteria. Based on demonstrations of Ca 2+ -binding, we called the protein "Ca 2+ sensor EF-hand" (CSE). Over-expression of CSE in Anabaena was shown to affect photosynthetic...

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Section: Discussionmentioning

confidence: 59%

Section: In Vitro Biochemical Properties Of Recombinant Asr1131 Proteinmentioning

confidence: 99%

A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

Walter

Selim

Leganés

et al. 2019

Preprint

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“…Calcium would therefore serve as one of the factors involved in differentiation required for life on the scales [ 6 ]. Consistent with this, in bacteria: (1) calcium is essential for heterocyst formation [ 82 ] and for sporulation 69, (2) calcium affects growth rate via ATP levels [ 83 ] thereby putting it in a position to generate metabolic heterogeneity within a population [ 6 ], (3) calcium is involved in biofilm formation and dispersal [ 84 - 86 ], (4) calcium increases the expression of genes or the functioning of proteins involved in chemotaxis, swarming, virulence and motility [ 87 - 89 ], (5) calcium is implicated in the response to nitrogen starvation [ 90 ] and to environmental pollutants [ 91 ].…”

Section: Presentation Of the Hypothesismentioning

confidence: 60%

Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells

et al. 2014

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BackgroundFundamental problems faced by the protocells and their modern descendants include how to go from one phenotypic state to another; escape from a basin of attraction in the space of phenotypes; reconcile conflicting growth and survival strategies (and thereby live on ‘the scales of equilibria’); and create a coherent, reproducible phenotype from a multitude of constituents.Presentation of the hypothesisThe solutions to these problems are likely to be found with the organic and inorganic molecules and inorganic ions that constituted protocells, which we term SUMIs for Simple Universal Molecules and Ions. These SUMIs probably included polyphosphate (PolyP) as a source of energy and of phosphate; poly-(R)-3-hydroxybutyrate (PHB) as a source of carbon and as a transporter in association with PolyP; polyamines as a source of nitrogen; lipids as precursors of membranes; as well as peptides, nucleic acids, and calcium. Here, we explore the hypothesis that the direct interactions between PHB, PolyP, polyamines and lipids – modulated by calcium – played a central role in solving the fundamental problems faced by early and modern cells.Testing the hypothesisWe review evidence that SUMIs (1) were abundant and available to protocells; (2) are widespread in modern cells; (3) interact with one another and other cellular constituents to create structures with new functions surprisingly similar to those of proteins and RNA; (4) are essential to creating coherent phenotypes in modern bacteria. SUMIs are therefore natural candidates for reducing the immensity of phenotype space and making the transition from a “primordial soup” to living cells.Implications of the hypothesisWe discuss the relevance of the SUMIs and their interactions to the ideas of molecular complementarity, composomes (molecular aggregates with hereditary properties based on molecular complementarity), and a prebiotic ecology of co-evolving populations of composomes. In particular, we propose that SUMIs might limit the initial phenotype space of composomes in a coherent way. As examples, we propose that acidocalcisomes arose from interactions and self-selection among SUMIs and that the phosphorylation of proteins in modern cells had its origin in the covalent modification of proteins by PHB.ReviewersThis article was reviewed by Doron Lancet and Kepa Ruiz-Mirazo.

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“…This group of proteins includes, in particular, the CcbP protein from cyano bacteria Anabaena sp. A specific feature of this protein is the presence, in addition to two Ca 2+ binding sites, of a subdomain that resembles the SH3 (Src homology 3) domain of the signal proteins involved in protein-protein interactions [63]. Another calcium binding protein detected in B. subtilis, YycH, regulates the activity of the YycG histidine kinase and is a part of the signaling pathway responsible for cell viability and growth [64].…”

Section: Calcium Intake By Bacterial Cellsmentioning

confidence: 99%

Ca2+ signaling in prokaryotes

Шемарова

Нестеров²

2014

Microbiology

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431In both higher and lower eukaryotes, Ca 2+ ions are common intracellular signaling messengers. Along with cyclic nucleotides, diacylglycerol, nitric oxide, signaling oligopeptides, and some other active mole cules and ions, Ca 2+ cations are involved in the regula tion of numerous processes in eukaryotic cells, such as cell cycle, nuclear division, nerve impulse conduction, muscle contraction, and others [1][2][3].In prokaryotes, the role of Ca 2+ in intracellular sig naling is considerably less studied. Only a few works have considered Ca 2+ ions as potential regulators of such cellular processes as ion transport, spore germi nation, heterocyst differentiation, gene expression, cell motility, adaptation to low or high temperatures, virulence, etc. [5][6][7][8][9][10]. For a long time, investigation of Ca 2+ signaling in microbial cells was hindered by methodological problems in determining intracellular calcium concentrations ([Ca 2+ ] i ), calcium contami nation, reagent toxicity, and difficulties in handling individual cells; these questions were discussed in [11][12][13]. However, the unique optical methods and other approaches to investigation of individual bacte rial cells developed in the 1990s, which made it possi ble to register the changes in Ca 2+ levels in microbial cytosol in response to various external stimuli [14][15][16], boosted the studies of the regulatory functions of Ca 2+ in prokaryotic signaling.In the present review, we discuss the historical development of ideas concerning Ca 2+ signaling in prokaryotic cells and the current concepts of the related research in evolutionary biology. FUNCTIONS OF Ca 2+ IN PROKARYTIC CELLSThe first studies concerning the role of Ca 2+ as a secondary messenger in prokaryotic organisms date back to the 1970s, when Ordal found that decreased Ca 2+ intake by bacterial cells affected the chemotactic behavior in Bacillus subtilis [17]. Further research confirmed his observations in other microorganisms. A study on Escherichia coli showed that a decrease in [Ca 2+ ] i could alter the swimming mode in flagellate bacteria. Specifically, the characteristic slow and directed swimming changed to chaotic disordered motion [18]. Measurements of [Ca 2+ ] i levels in E. coli performed using the Fura 2 fluorescent Ca 2+ indicator revealed that bacterial repellents caused a temporary increase in [Ca 2+ ] i (to over 100 nM) and inhibited chemotaxis, whereas attractants, in contrast, tempo rarily decreased [Ca 2+ ] i levels and stimulated chemot axis [18].Experiments on blocking the voltage gated Ca 2+ channels (Cav) of different types (L, P/Q, and R) showed that inhibitors added to the incubation medium impaired the chemotactic behavior of bacte ria. In prokaryotes, it was expected that the stimuli inducing chemotactic reactions may increase the intake of extracellular Ca 2+ through the ion channels opened in response to membrane depolarization, as it occurs in protists and even in multicellular eukaryotes. However, there was no direct correlation between the extracellular...

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Structures of Anabaena Calcium-binding Protein CcbP

Cited by 23 publications

References 46 publications

A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells

Ca2+ signaling in prokaryotes

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Structures of Anabaena Calcium-binding Protein CcbP

Cited by 23 publications

References 46 publications

A novel Ca2+-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

A novel Ca2+-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells

Ca2+ signaling in prokaryotes

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A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120

A novel Ca²⁺-binding protein influences photosynthetic electron transport inAnabaenasp. PCC 7120