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PubMed1996

The sigA gene encoding the major sigma factor of RNA polymerase from the marine cyanobacterium Synechococcus sp. strain PCC 7002: cloning and characterization.

The gene encoding the principal sigma factor from Synechococcus sp. strain PCC 7002 was isolated and characterized. The Synechococcus sp. strain PCC 7002 sigA gene encodes a protein of 375 amino acids (43 center dot 7 kDa) that is required for viability under normal growth conditions. The SigA protein was overproduced in Escherichia coli and the purified protein was used to raise polyclonal antiserum in rabbits. This antiserum was used in immunoblot analyses of partially purified RNA polymerase from Synechococcus sp. strain PR6000. The probable in vivo translational start site was identified by a comparison of amino acid sequencing results obtained with SigA proteins overproduced in E. coli with immunoblot analyses of SigA protein in crude preparations of RNA polymerase from the cyanobacterium. The sigA gene is encoded on a transcript of 1700 bases that initiates 496 nucleotides upstream from the probable in vivo translational start site. The abundance of sigA transcripts decreases rapidly after the removal of combined nitrogen from the growth medium.

Amino Acid Sequence↗

PubMed1996

Inactivation of the petE gene for plastocyanin lowers photosynthetic capacity and exacerbates chilling-induced photoinhibition in the cyanobacterium Synechococcus.

We describe the identification and expression of a petE gene in Synechococcus sp. PCC 7942, a cyanobacterium previously thought to lack plastocyanin. The petE gene is a 420-bp open reading frame that encodes a protein 70 to 75% similar to plastocyanins from other cyanobacteria. Synechococcus possesses a single genomic copy of petE located immediately upstream of the clpB gene. It is transcribed as a single mRNA (550 bases) and, in contrast to most other photobionts, the level of petE expression in Synechococcus is unaffected by variable copper concentrations during acclimated growth. Inactivation of petE does not prevent photoautotrophic growth, but does induce a dramatic increase in mRNA for the alternative electron carrier cytochrome C6. Despite this adjustment, loss of plastocyanin results in slower growth, lower photosystem I content, and a decreased maximum capacity for photosynthetic electron transport. The mutant is also more susceptible to chilling-induced photoinhibition during a shift from 37 to 25 degrees C, at which temperature its inherently lower photosynthetic capacity exacerbates the normal slowing of electron transfer reactions at low temperatures. Under similar conditions, the amount of petE message in the wild type decreases by 50% in the 1st h, but then increases dramatically to almost three times the 37 degrees C level by 9 h.

Amino Acid Sequence↗

PubMed1983

Ionic Osmoregulation during Salt Adaptation of the Cyanobacterium Synechococcus 6311.

The mechanisms of salt adaptation were studied in the cyanobacterium Synechococcus 6311. Intracellular volumes and ion concentrations were measured before and after abrupt increases of external NaCl concentrations up to 0.6 molar NaCl. Equilibrium volumes, measured with a rapid and accurate electron spin resonance spin probe method, showed that at low NaCl concentrations the cells did not shrink as expected for an impermeable solute. However, when the NaCl concentration exceeded a critical value, volume losses occurred. These losses were not fully reversed by hypoosmotic treatment, suggesting membrane damage. The critical value of irreversible volume loss paralleled the increase in salinity during cell growth. Rapid mixing experiments showed that exposure of Synechococcus 6311 to non-damaging NaCl concentrations caused water extrusion from the cells; the volume decreases were time resolved to about 200 milliseconds. Subsequently, volumes increased rapidly as NaCl moved into the cells. Controls recovered their volumes within 15 seconds, while salt-adapted cells grown at 0.6 molar NaCl required 1 minute for volume equilibration. This decrease in the rate of cell volume recovery indicates that salt adaptation is accompanied by changes in cell membrane properties. Subsequent to these initial rapid volume changes, a more gradual sequence of ion movement and sugar accumulation was observed. Under conditions for photoautotrophic growth, significant Na(+) extrusion was observed 30 min after salt shock. Sucrose accumulation reached a maximum value after 16 hours and K(+) accumulation reached equilibrium after 40 hours. The final concentrations of K(+) and Na(+) and sucrose and glucose inside the 0.6 molar NaCl-grown cells indicate that the inorganic ions and organic ;compatible' solutes are the major osmotic species which account for the adaptation of Synechococcus 6311 to salt.

Journal Article↗

PubMed1984

Novel Phycoerythrins in Marine Synechococcus spp. : Characterization and Evolutionary and Ecological Implications.

Four clones of the marine, unicellular, cyanobacteria Synechococcus spp., were examined for the spectral and biochemical features of their phycoerythrins (PE) and their photosynthetic characteristics. Two spectral types of PE which are distinct from known PEs were found. One PE type possessed absorption maxima at 500 and 545 nm and a fluorescence emission at 560 nm. Upon denaturation in acid-urea, two chromophore absorption maxima were obtained, one corresponding to phycourobilin (A(max) 500 nm) and one at 558 nm, ascribed to a phycoerythrobilin-like chromophore. The ratio of phycoerythrobilin-like to phycourobilin chromophores was 4.9:1.3. This PE possessed two subunits of M(r)s of 17.0 and 19.5 kD for the alpha and beta subunits, respectively. The other PE possessed a single symmetrical absorption at 551 nm and a fluorescence emission at 570 nm. This phycobiliprotein showed a single chromophore absorption band (A(max) 558 nm) and yielded two polypeptides, an alpha of 17.5 kD and a beta subunit of 20.8 kD. Both PEs showed a (alpha, beta)(n) structure. The presence of phycoerythrobilin-like chromophores (A(max) 558 nm) appears to be diagnostic of this marine cyanobacterial group. The features of these PEs combined with additional biochemical data, suggest a possible evolutionary link between the PE-containing marine Synechococcus group and the red algal chloroplast. When the Synechococcus clones were grown under low light intensity the PE-containing clones showed higher photosynthetic performance, larger photosynthetic units sizes, reaction center I to II ratios near unity, and steeper initial slopes of photosynthesis versus irradiance curves than a non-PE-containing clone. These findings demonstrate the high photosynthetic efficiency of PE-containing clones in low light environments common to middepth neritic and oceanic habitats.

Journal Article↗

PubMed1989

Expression of Human Carbonic Anhydrase in the Cyanobacterium Synechococcus PCC7942 Creates a High CO(2)-Requiring Phenotype : Evidence for a Central Role for Carboxysomes in the CO(2) Concentrating Mechanism.

Active human carbonic anhydrase II (HCAII) protein was expressed in the cyanobacterium Synechococcus PCC7942 by means of transformation with the bidirectional expression vector, pCA. This expression was driven by the bacterial Tac promoter and was regulated by the IacIQ repressor protein, which was expressed from the same plasmid. Expression levels reached values of around 0.3% of total cell protein and this protein appeared to be entirely soluble in nature and located within the cytosol of the cell. The expression of this protein has dramatic effects on the photosynthetic physiology of the cell. Induction of expression of carbonic anhydrase (CA) activity in both high dissolved inorganic carbon (C(i)) and low C(i) grown cells leads the creation of a high C(i) requiring phenotype causing: (a) a dramatic increase in the K(0.5) (C(i)) for photosynthesis, (b) a loss of the ability to accumulate internal C(i), and (c) a decrease in the lag between the initial C(i) accumulation following illumination and the efflux of CO(2) from the cells. In addition, the effects of the expressed CA can largely be reversed by the carbonic anhydrase inhibitor ethoxyzolamide. As a result of the above findings, it is concluded that the CO(2) concentrating mechanism in Synechococcus PCC7942 is largely dependent on (a) the absence of CA activity from the cytosol, and (b) the specific localization of CA activity in the carboxysome. A theoretical model of photosynthesis and C(i) accumulation is developed in which the carboxysome plays a central role as both the site of CO(2) generation from HCO(3(-) ) and a resistance barrier to CO(2) efflux from the cell. There is good qualitative agreement between this model and the measured physiological effects of expressed cytosolic CA in Synechococcus cells.

Journal Article↗

PubMed1990

Sequencing and Modification of the Gene Encoding the 42-Kilodalton Protein in the Cytoplasmic Membrane of Synechococcus PCC 7942.

A 42-kilodalton cytoplasmic membrane protein is synthesized when high CO(2)-grown cells of Synechococcus PCC 7942 (Anacystis nidulans R2) are exposed to low CO(2). The structural gene for this protein (cmpA) has been cloned and sequenced and shown to encode a 450 amino acid polypeptide with a molecular mass of 49 kilodalton. A deletion mutant lacking the 42-kilodalton protein was obtained by transformation of Synechococcus PCC 7942 following in vitro mutagenesis of the cloned gene. There were no significant differences between the mutant and wild-type cells in their growth rates under either low or high CO(2) conditions. The activity of inorganic carbon (C(i)) transport in the mutant was as high as that in the wild-type strain. In both types of cells, CO(2) was the main species of C(i) transported and the activities of CO(2) and HCO(3) (-) transport increased when high CO(2)-grown cells were exposed to low CO(2). We conclude that the 42-kilodalton protein is not directly involved in the C(i)-accumulating mechanism of Synechococcus PCC 7942.

Journal Article↗

PubMed1992

Na-Independent HCO(3) Transport and Accumulation in the Cyanobacterium Synechococcus UTEX 625.

The active transport and intracellular accumulation of HCO(3) (-) by air-grown cells of the cyanobacterium Synechococcus UTEX 625 (PCC 6301) was strongly promoted by 25 millimolar Na(+).Na(+)-dependent HCO(3) (-) accumulation also resulted in a characteristic enhancement in the rate of photosynthetic O(2) evolution and CO(2) fixation. However, when Synechococcus was grown in standing culture, high rates of HCO(3) (-) transport and photosynthesis were observed in the absence of added Na(+). The internal HCO(3) (-) pool reached levels up to 50 millimolar, and an accumulation ratio as high as 970 was observed. Sodium enhanced HCO(3) (-) transport and accumulation in standing culture cells by about 25 to 30% compared with the five- to eightfold enhancement observed with air-grown cells. The ability of standing culture cells to utilize HCO(3) (-) from the medium in the absence of Na(+) was lost within 16 hours after transfer to air-grown culture and was reacquired during subsequent growth in standing culture. Studies using a mass spectrometer indicated that standing culture cells were also capable of active CO(2) transport involving a high-affinity transport system which was reversibly inhibited by H(2)S, as in the case for air-grown cells. The data are interpreted to indicate that Synechococcus possesses a constitutive CO(2) transport system, whereas Na(+)-dependent and Na(+)-independent HCO(3) (-) transport are inducible, depending upon the conditions of growth. Intracellular accumulation of HCO(3) (-) was always accompanied by a quenching of chlorophyll a fluorescence which was independent of CO(2) fixation. The extent of fluorescence quenching was highly dependent upon the size of the internal pool of HCO(3) (-) + CO(2). The pattern of fluorescence quenching observed in response to added HCO(3) (-) and Na(+) in air-grown and standing culture cells was highly characteristic for Na(+)-dependent and Na(+)-independent HCO(3) (-) accumulation. It was concluded that measurements of fluorescence quenching provide an indirect means for following HCO(3) (-) transport and the dynamics of intracellular HCO(3) (-) accumulation and dissipation.

Journal Article↗

PubMed2003

The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803.

The PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803 have been crystallized and high-resolution structures have been obtained using X-ray crystallography. The core of these new structures is similar to that of the PII proteins from Escherichia coli, although the structures of the T- and C-loops differ. The T-loop of the Synechococcus protein is ordered, but appears to be stabilized by crystal contacts. The same loop in the Synechocystis protein is disordered. The C-terminus of the Synechocystis protein is stabilized by hydrogen bonding to the same region of a crystallographically related molecule. The same terminus in the Synechococcus protein is stabilized by coordination with a metal ion. These observations are consistent with the idea that both the T-loop and the C-terminus of PII proteins are flexible in solution and that this flexibility may be important for receptor recognition. Sequence comparisons are used to identify regions of the sequence unique to the cyanobacteria.

Amino Acid Sequence↗

PubMed1989

Genetic analysis of phycobilisome mutants in the cyanobacterium Synechococcus species PCC 6301.

The chromophoric protein phycocyanin is the major protein in the phycobilisome rod of the cyanobacterium Synechococcus 6301 (formerly designated Anacystis nidulans sp. UTEX 625). The gene clusters coding for the beta- and alpha-subunits of phycocyanin are duplicated on the chromosome of Synechococcus 6301 and separated by an intergenic region 2.5 kb long. The structure of the phycocyanin operons of the phycobilisome mutant strains AN112 and AN135 was compared to that of wild-type Synechococcus 6301. Both mutants have an altered phycobilisome structure resulting in the appearance of rods of a shorter overall length. Genetic mapping indicated that the mutant strain AN112 completely lacked the intergenic region and carried only one set of phycocyanin subunit genes. No gross structural difference in the genetic organization of the corresponding region of mutant strain AN135 was detected. Northern blot analysis and primer extension experiments were used to monitor the transcriptional pattern of the phycocyanin rod operon. It was found that AN112 had lost the 3.7kb minor mRNA, which covers the intergenic region, and only produced two major 1.3 and 1.4kb mRNA species. These transcripts were identified as fusion products of the 5' end of the transcriptional unit originating from the promoter region of the left-hand phycocyanin gene cluster and the 3' end of the transcriptional unit covering the right-hand phycocyanin gene cluster. The mutant strain AN135 had a transcriptional pattern very similar to that of the wild type. The level of transcription of the major transcripts covering the phycocyanin gene clusters was similar in the wild-type and mutant strains.(ABSTRACT TRUNCATED AT 250 WORDS)

Blotting, Northern↗

PubMed1992

NtcA, a global nitrogen regulator from the cyanobacterium Synechococcus that belongs to the Crp family of bacterial regulators.

The gene ntcA is required for full expression of proteins subject to ammonium repression in the cyanobacterium Synechococcus. A 3.1 kb DNA fragment able to complement an ntcA mutant was digested with exonuclease III, and deleted fragments of different size were tested for complementation of that mutant, allowing the localization of its mutation within a BamHI-HindIII genomic fragment of c. 0.4 kb. Insertion of a chloramphenicol-resistance-encoding gene cassette into both the BamHI and the HindIII sites of wild-type Synechococcus resulted in a pleiotropic, nitrogen-assimilation-minus phenotype, corroborating the presence of the ntcA gene in that genomic region. Sequencing of DNA in this region showed the presence of an open reading frame that included both the BamHI and the HindIII sites. The ntcA gene product, NtcA, is a protein of 24817 Da which belongs to a family of bacterial transcriptional activators that, among others, includes Crp and Fnr from Escherichia coli. Of special biological significance, it appears, is the presence of a conserved helix-turn-helix motif in the sequence close to the C-terminal end of all the proteins in the family. The gene ntcA is proposed to encode a transcriptional activator of genes subject to nitrogen control in Synechococcus.

Amino Acid Sequence↗

PubMed1993

The response of the picoplanktonic marine cyanobacterium Synechococcus species WH7803 to phosphate starvation involves a protein homologous to the periplasmic phosphate-binding protein of Escherichia coli.

During phosphate-limited growth the marine phycoerythrin-containing picoplanktonic cyanobacterium Synechococcus sp. WH7803 synthesizes novel polypeptides, including two abundant species of 100 kDa and 32 kDa. The 32 kDa polypeptide was localized to the cell wall, although in a related strain, Synechococcus sp. WH8103, it could be detected in both the cell wall fraction and the periplasm. The gene (designated pstS) encoding this polypeptide was cloned and shown to be present in a single copy. The deduced amino acid sequence indicated a polypeptide consisting of 326 amino acids with a calculated M(r) of 33,763. Comparison of this sequence with that obtained by microsequencing the N-terminus of the 32 kDa polypeptide showed that the mature protein was synthesized as a precursor, the first 24 amino acid residues being cleaved between two alanine residues at positions 24 and 25. The amino acid sequence of the mature polypeptide showed 35% identity and 52% similarity to the periplasmic phosphate-binding protein (PstS) from Escherichia coli, including three regions of much stronger homology which, by comparison with E. coli PstS, are directly involved in phosphate binding. Northern blot analysis revealed a pstS transcript of 1.2 kb in RNA extracted from cells grown in Pi-replete conditions and one of 1.4 kb in considerably increased abundance under Pi-depleted conditions. Homologues of the pstS gene were detected in other marine phycoerythrin-containing Synechococcus strains, but not in freshwater or halotolerant species.

Amino Acid Sequence↗

PubMed1993

Sensor and regulator proteins from the cyanobacterium Synechococcus species PCC7942 that belong to the bacterial signal-transduction protein families: implication in the adaptive response to phosphate limitation.

A 1.2kb DNA fragment was cloned from Synechococcus sp. PCC7942, which is able phenotypically to complement a phoR creC Escherichia coli mutant for the expression of alkaline phosphatase. A 2.5 kb DNA fragment encompassing the putative gene was then cloned and its complete nucleotide sequence determined. Nucleotide sequencing revealed that the intact gene encodes a protein of 46,389 Da, and that the deduced amino acid sequence shows a high degree of homology to those of the bacterial sensory kinase family. In the determined nucleotide sequence, another gene was adjacently located, which encodes a protein of 29,012 Da. This protein shows a high degree of homology to those of the response regulator family. Thus, we succeeded in the cloning of a pair of genes encoding the sensory kinase and response regulator, respectively, in a cyanobacterium. Mutant strains that lack these genes were constructed, and demonstrated to be defective in their ability to produce alkaline phosphatase and some inducible proteins in response to phosphate-limitation in the medium. These results are probably involved, either directly or indirectly, in the signal-transduction mechanism underlying regulation of the phosphate regulon in Synechococcus sp. PCC7942. Hence, the genes encoding the sensory kinase and response regulator were designated as sphS and sphR, respectively (Synechococcus phosphate regulon). The SphS protein was demonstrated in vitro to undergo phosphorylation in the presence of ATP.

Adaptation, Physiological↗

PubMed1993

Integration of a cyanobacterial protein involved in nitrate reduction (narB) into isolated Synechococcus but not into pea thylakoid membranes.

Chimeric genes comprised of Rubisco small subunit transit peptide fused in frame with full-length and truncated sequences of a nitrate reductase (narB) structural gene of Synechococcus were constructed. Fusion proteins were synthesized in a rabbit reticulocyte system. In thylakoido integration of synthetic proteins resulted in the association of the full-length narB-coded protein to the Synechococcus photosynthetic membranes. The membrane-associated protein was sensitive to trypsin treatment but could not be removed by washing in the presence of NaBr. Trypsin pretreatment of thylakoids abolished the capability for association. The association of the narB-coded protein with thylakoids might require another membrane protein whose identity is not known. It is proposed that the Synechococcus narB polypeptide is a peripheral, membrane bound protein anchored to the thylakoids via a short hydrophobic domain while the major part of the protein resides on the outer side of the thylakoid membranes. The chimeric narB proteins were processed and imported by intact pea chloroplasts in vitro; however, the mature proteins were found localized in the stroma and not in the thylakoid membrane fraction. Similarly, the attempt to integrate the protein in vitro into isolated pea thylakoid membranes failed although these membranes incorporate early light-inducible proteins.

Animals↗

PubMed1993

Resistance to co-occurring phages enables marine synechococcus communities to coexist with cyanophages abundant in seawater.

Recent reports documenting very high viral abundances in seawater have led to increased interest in the role of viruses in aquatic environments and a resurgence of the hypothesis that viruses are significant agents of bacterial mortality. Synechococcus spp., small unicellular cyanobacteria that are important primary producers at the base of the marine food web, were used to assess this hypothesis. We isolated a diverse group of Synechococcus phages that at times reach titers of between 10 and 10 cyanophages per ml in both inshore and offshore waters. However, despite their diversity and abundance, we present evidence in support of the hypothesis that lytic phages have a negligible effect in regulating the densities of marine Synechococcus populations. Our results indicate that these bacterial communities are dominated by cells resistant to their co-occurring phages and that these viruses are maintained by scavenging on the relatively rare sensitive cells in these communities.

Journal Article↗

PubMed1993

Effect of promoter modification on mosquitocidal cryIVB gene expression in Synechococcus sp. strain PCC 7942.

The impact of promoter modification on the expression of the mosquitocidal Bacillus thuringiensis subsp. israelensis cryIVB gene when used to transform the cyanobacterium Synechococcus sp. strain PCC 7942 has been examined. Maximal transcript and protein abundances were achieved by the addition of the lacZ promoter upstream of the cryIVB sequence. Replacement of the endogenous corresponding Bacillus sequences with the Synechococcus petF1 promoter, ribosome binding site, and initiation codon also resulted in increased expression of the cryIVB gene relative to the expression obtained with the Bacillus promoter alone but decreased expression relative to the expression achieved with the tandem array of the Bacillus and lacZ promoters. Synechococcus cells carrying plasmids in which the expression of the cryIVB gene was regulated by either the lacZ or the petF1 promoter were readily consumed by first-instar Culex restuans larvae and proved to be toxic for these organisms.

Bacillus thuringiensis↗

PubMed1995

Cell Cycle Regulation in Marine Synechococcus sp. Strains.

The cell cycle behavior of four marine strains of the unicellular cyanobacterium Synechococcus sp. was analyzed by examining the DNA frequency distributions of exponentially growing and dark-blocked populations and by considering the patterns of change in these distributions during growth under a diel light-dark cycle. The two modes of cell cycle regulation previously identified in a freshwater and coastal marine Synechococcus isolate, respectively, were represented among the three open-ocean strains we examined. The first of these modes of regulation is consistent with the slow-growth case of the widely accepted prokaryotic cell cycle paradigm. The second appears to involve asynchronous initiation of chromosome replication, the presence of multiple chromosome copies at low growth rates, and variability in chromosome copy number among cells in the population. These characteristics suggest the involvement of a large probabilistic component in cell cycle regulation which could make the application of cell cycle-based estimators of in situ growth rate to Synechococcus populations problematic.

Journal Article↗

PubMed1996

Effect of Phosphorus on the Synechococcus Cell Cycle in Surface Mediterranean Waters during Summer.

The effect of phosphorus (P) and nitrogen (N) additions on the Synechococcus cell cycle was tested with natural populations from the Mediterranean Sea in summer. In the absence of stimulation, the Synechococcus cell cycle was synchronized to the light-dark cycle. DNA synthesis began around 1600, a maximum of S-phase cells was observed at around dusk (2100), and a maximum of G(inf2)-phase cells was observed at around 2400. Addition of P (as PO(inf4)(sup3-)) caused, in all cases, a decrease in the fraction of cells in G(inf2) at around 1800, no change at around 2400, and an increase at around 1200 the next day, while addition of N (as NO(inf3)(sup-)) had no effect. We hypothesize that P addition induced a shortening of the G(inf1) phase, resulting in cells entering and leaving the S and G(inf2) phases earlier. These data suggest very strongly that the Synechococcus cells were P limited rather than N limited during this period of the year. In most cases, additions as low as 20 nM P induced a cell cycle response. From dose-response curves, we established that the P concentration inducing a 50% change in the percentage of cells in G(inf2) was low, close to 10 nM, at the beginning of the sampling period (30 June) and increased to about 50 nM by the end (9 July), suggesting a decrease in the severity of P limitation. This study extends recent observations that oligotrophic systems may be P rather than N limited at certain times of the year.

Journal Article↗

PubMed2000

Evolution of thermotolerance in hot spring cyanobacteria of the genus Synechococcus.

The extension of ecological tolerance limits may be an important mechanism by which microorganisms adapt to novel environments, but it may come at the evolutionary cost of reduced performance under ancestral conditions. We combined a comparative physiological approach with phylogenetic analyses to study the evolution of thermotolerance in hot spring cyanobacteria of the genus Synechococcus. Among the 20 laboratory clones of Synechococcus isolated from collections made along an Oregon hot spring thermal gradient, four different 16S rRNA gene sequences were identified. Phylogenies constructed by using the sequence data indicated that the clones were polyphyletic but that three of the four sequence groups formed a clade. Differences in thermotolerance were observed for clones with different 16S rRNA gene sequences, and comparison of these physiological differences within a phylogenetic framework provided evidence that more thermotolerant lineages of Synechococcus evolved from less thermotolerant ancestors. The extension of the thermal limit in these bacteria was correlated with a reduction in the breadth of the temperature range for growth, which provides evidence that enhanced thermotolerance has come at the evolutionary cost of increased thermal specialization. This study illustrates the utility of using phylogenetic comparative methods to investigate how evolutionary processes have shaped historical patterns of ecological diversification in microorganisms.

Biological Evolution↗