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Query: UMLS:C1832526 (PCC)
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Cysteine dithiol/disulphide exchange forms the molecular basis for regulation of a wide variety of enzymatic activities and for transduction of cellular signals. Thus, the search for proteins with reactive, accessible cysteines is expected to contribute to the unravelling of new molecular mechanisms for enzyme regulation and signal transduction. Several methods have been designed for this purpose taking advantage of the interactions between thioredoxins and their protein substrates. Thioredoxins comprise a family of redox-active enzymes, which catalyse reduction of protein disulphides and sulphenic acids. Due to the inherent practical difficulties associated with studies of membrane proteins these have been largely overlooked in the many proteomic studies of thioredoxin-interacting proteins. In the present work, we have developed a procedure to isolate membrane proteins interacting with thioredoxin by binding in situ to a monocysteinic His-tagged thioredoxin added directly to the intact membranes. Following fractionation and solubilisation of the membranes, thioredoxin target proteins were isolated by Ni-affinity chromatography and 2-DE SDS-PAGE under nonreducing/reducing conditions. Applying this method to total membranes, including thylakoid and plasma membranes, from the cyanobacterium Synechocystis sp. PCC 6803 we have identified 50 thioredoxin-interacting proteins. Among the 38 newly identified thioredoxin targets are the ATP-binding subunits of several transporters and members of the AAA-family of ATPases.
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PMID:Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. 1792 17

Cyanobacteria respond to environmental stress conditions by adjusting its photosynthesis machinery. When subjected to nutrient and high light stress, Synechococcus sp. PCC 7942 and other non-diazotrophic cyanobacteria degrade their phycobilisome, the light-harvesting complexes for photosynthesis. Phycobilisome degradation requires convergence of multiple signals onto the nblA gene. Despite considerable efforts to identify regulatory proteins involved in acclimation responses, the signal transduction mechanisms involved remain largely unknown. However, we show here that SipA, a protein that binds to the ATP-binding domain of the histidine kinase NblS, counteracts the function of the response regulator NblR in acclimation to stress, and is also involved in downregulation of the nblA gene. The integrity of the HLR1 element overlapping P(nblA-1) and P(nblA-2) promoters is required for downregulation of the nblA gene. Induction by NblR is strongly dependent on DNA sequences located at least 44 bp upstream transcription initiation from P(nblA-2), and is also hampered by point mutations at HLR1. Genetic evidence of the antagonistic roles of NblR and SipA at regulation of the nblA gene, chlorosis and survival from stress is presented.
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PMID:The regulatory factor SipA provides a link between NblS and NblR signal transduction pathways in the cyanobacterium Synechococcus sp. PCC 7942. 1800 83

In vitro incubation of three Kai proteins, KaiA, KaiB, and KaiC, with ATP induces a KaiC phosphorylation cycle that is a potential circadian clock pacemaker in cyanobacterium Synechococcus elongatus PCC 7942. The Kai proteins assemble into large heteromultimeric complexes (periodosome) to effect a robust oscillation of KaiC phosphorylation. Here, we report real-time measurements of the assembly/disassembly dynamics of the Kai periodosome by using small-angle X-ray scattering and determination of the low-resolution shapes of the KaiA:KaiC and KaiB:KaiC complexes. Most previously identified period-affecting mutations could be mapped to the association interfaces of our complex models. Our results suggest that the assembly/disassembly processes are crucial for phase entrainment in the early synchronizing stage but are passively driven by the phosphorylation status of KaiC in the late oscillatory stage. The Kai periodosome is assembled in such a way that KaiA and KaiB are recruited to a C-terminal region of KaiC in a phosphorylation-dependent manner.
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PMID:Assembly and disassembly dynamics of the cyanobacterial periodosome. 1834 62

In the cyanobacterium Synechococcus elongatus PCC 7942, the products of three genes (kaiA, kaiB, and kaiC) have been identified as essential components of the circadian clock. Recently, we reconstituted the self-sustainable circadian oscillation of the KaiC phosphorylation state by incubating purified KaiC with KaiA, KaiB, and ATP. This in vitro oscillation persisted for at least three cycles and the period was compensated against temperature changes. Period lengths observed in vivo in various kaiC mutants were consistent with those measured using in vitro mixtures containing the respective mutant KaiC proteins. These results demonstrate that the oscillation of KaiC phosphorylation is the primary pacemaker of the cyanobacterial circadian clock and reveal a novel function of proteins as timing devices that govern cellular metabolism. We further analyzed four aspects of the KaiC phosphorylation cycle in vitro: the interactions among KaiA, KaiB, and KaiC; the functions of the two phosphorylation sites, the energetics that determine the circadian period, and the mechanisms that synchronize the components of the Kai oscillator. From these analyses, we have proposed a circadian program consisting of the three proteins that keeps biological time in a living cell.
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PMID:A cyanobacterial circadian clock based on the Kai oscillator. 1841 62

Capillary electrophoresis mass spectrometry (CE/MS) was applied for the comprehensive survey of changes in the amounts of metabolites upon the shift from photoautotrophic to photomixotrophic conditions in Synechocystis sp. PCC 6803. When glucose was added to the photoautotrophically grown culture, the increase in the metabolites for the oxidative pentose phosphate (OPP) pathway and glycolysis, together with the decrease in those for the Calvin cycle, was observed. Concomitantly, the increase in respiratory activity and the decrease in photosynthetic activity took place in the wild-type cells. In the pmgA-disrupted mutant that shows growth inhibition under photomixotrophic conditions, lower enzymatic activities of the OPP pathway and higher photosynthetic activity were observed, irrespective of trophic conditions. These defects brought about metabolic disorders such as a decrease in ATP and NADPH contents, a failure in the activation of respiratory activity, and the aberrant accumulation of isocitrate under photomixotrophic but not under photoautotrophic conditions. A delicate balancing of the carbon flow between the Calvin cycle and the OPP pathway seems indispensable for growth specifically under photomixotrophic conditions and PmgA is likely to be involved in the regulation.
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PMID:Difference in metabolite levels between photoautotrophic and photomixotrophic cultures of Synechocystis sp. PCC 6803 examined by capillary electrophoresis electrospray ionization mass spectrometry. 1861 12

Nostoc punctiforme ATCC 29133 is a photoautotrophic cyanobacterium with the capacity to fix atmospheric N 2. Its ability to mediate this process is similar to that described for Nostoc sp. PCC 7120, where vegetative cells differentiate into heterocysts. Quantitative proteomic investigations at both the filament level and the heterocyst level are presented using isobaric tagging technology (iTRAQ), with 721 proteins at the 95% confidence interval quantified across both studies. Observations from both experiments yielded findings confirmatory of both transcriptional studies, and published Nostoc sp. PCC 7120 iTRAQ data. N. punctiforme exhibits similar metabolic trends, though changes in a number of metabolic pathways are less pronounced than in Nostoc sp. PCC 7120. Results also suggest a number of proteins that may benefit from future investigations. These include ATP dependent Zn-proteases, N-reserve degraders and also redox balance proteins. Complementary proteomic data sets from both organisms present key precursor knowledge that is important for future cyanobacterial biohydrogen research.
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PMID:Quantitative overview of N2 fixation in Nostoc punctiforme ATCC 29133 through cellular enrichments and iTRAQ shotgun proteomics. 1901 30

The structure and functional role of the dimeric external stalk of F(o)F(1)-ATP synthases have been very actively researched over the last years. To understand the function, detailed knowledge of the structure and protein packing interactions in the dimer is required. In this paper we describe the application of structural prediction and molecular modeling approaches to elucidate the structural packing interaction of the cyanobacterial ATP synthase external stalk. In addition we present biophysical evidence derived from ESR spectroscopy and site directed spin labeling of stalk proteins that supports the proposed structural model. The use of the heterodimeric bb' dimer from a cyanobacterial ATP synthase (Synechocystis sp. PCC 6803) allowed, by specific introduction of spin labels along each individual subunit, the evaluation of the overall tertiary structure of the subunits by calculating inter-spin distances. At defined positions in both b and b' subunits, reporter groups were inserted to determine and confirm inter-subunit packing. The experiments showed that an approximately 100 residue long section of the cytoplasmic part of the bb'-dimer exists mostly as an elongated alpha-helix. The distant C-terminal end of the dimer, which is thought to interact with the delta-subunit, seemed to be disordered in experiments using soluble bb' proteins. A left-handed coiled coil packing of the dimer suggested from structure prediction studies and shown to be feasible in molecular modeling experiments was used together with the measured inter-spin distances of the inserted reporter groups determined in ESR experiments to support the hypothesis that a significant portion of the bb' structure exists as a left-handed coiled coil.
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PMID:De-novo modeling and ESR validation of a cyanobacterial F(o)F(1)-ATP synthase subunit bb' left-handed coiled coil. 1915 Mar 27

Filamentous, heterocystous cyanobacteria are capable of nitrogen fixation and photoautotrophic growth. Nitrogen fixation takes place in heterocysts that differentiate as a result of nitrogen starvation. Heterocysts uphold a microoxic environment to avoid inactivation of nitrogenase, e.g. by downregulation of oxygenic photosynthesis. The ATP and reductant requirement for the nitrogenase reaction is considered to depend on Photosystem I, but little is known about the organization of energy converting membrane proteins in heterocysts. We have investigated the membrane proteome of heterocysts from nitrogen fixing filaments of Nostoc punctiforme sp. PCC 73102, by 2D gel electrophoresis and mass spectrometry. The membrane proteome was found to be dominated by the Photosystem I and ATP-synthase complexes. We could identify a significant amount of assembled Photosystem II complexes containing the D1, D2, CP43, CP47 and PsbO proteins from these complexes. We could also measure light-driven in vitro electron transfer from Photosystem II in heterocyst thylakoid membranes. We did not find any partially disassembled Photosystem II complexes lacking the CP43 protein. Several subunits of the NDH-1 complex were also identified. The relative amount of NDH-1M complexes was found to be higher than NDH-1L complexes, which might suggest a role for this complex in cyclic electron transfer in the heterocysts of Nostoc punctiforme.
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PMID:Electron transfer protein complexes in the thylakoid membranes of heterocysts from the cyanobacterium Nostoc punctiforme. 1936 13

Anabaena sp. PCC7120 contains a gene, mrpA (all1838), which forms part of a seven gene-cluster (all1843-all1837) with significant sequence similarity to bacterial operons that putatively code for a multicomponent cation/proton antiporter involved in alkaline pH adaptation and salt resistance. We previously showed that growth and photosynthesis were inhibited in a strain mutated in mrpA, denoted as PHB11, particularly at alkaline pH. Here, we show that respiration was also impaired in the mutant independently of the external pH. In addition, at high pH, less ATP and vegetative cell ferredoxin were present in PHB11, which also showed lower levels of ferredoxin-NADP(+) oxidoreductase (FNR). Ferredoxin and FNR are involved in the generation of reductant NADPH in cyanobacteria. These results suggest an energetic role of mrpA (and perhaps of the whole mrp-gene cluster) in Anabaena sp. PCC 7120 that is further supported by the significant similarity of putative Anabaena Mrp proteins to membrane subunits of complex I.
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PMID:mrpA (all1838), a gene involved in alkali and Na(+) sensitivity, may also have a role in energy metabolism in the cyanobacterium Anabaena sp. strain PCC 7120. 1941 Mar 33

The futC gene encodes a subunit of an ATP-binding cassette (ABC)-type iron transporter in Synechocystis sp. strain PCC 6803. In the present study, we have focused on the environmental regulation of futC transcription in the model organism Synechocystis sp. strain PCC 6803 and, moreover, studied the transcriptional regulation of the other transporter subunits, futA1, futA2 and futB. The steady-state amounts of the futA1, futA2, futB and futC transcripts were regulated under several conditions studied including darkness, temperature, alternative nitrogen source, salt and osmotic stresses and iron deficiency. Transcription of all subunits of the FutABC-iron transporter seems to be under similar regulation, which, according to our results, may also apply to genes encoding subunits of other transporters in Synechocystis. The sequence alignment, including sequences from six different organisms, revealed the conserved nature of FutC. Based on the sequence alignment and the structural model of FutC, the monomer consists of a nucleotide-binding domain (NBD) and a regulatory domain. The NBD is well conserved indicating completely functional ATP binding.
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PMID:Transcriptional regulation and structural modeling of the FutC subunit of an ABC-type iron transporter in Synechocystis sp. strain PCC 6803. 1943 Jul 63


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