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PubMed2003

Monomeric NarB is a dual-affinity nitrate reductase, and its activity is regulated differently from that of nitrate uptake in the unicellular diazotrophic cyanobacterium Synechococcus sp. strain RF-1.

Synechococcus sp. strain RF-1 is a unicellular freshwater cyanobacterium that fixes N(2) aerobically and exhibits a circadian rhythm for nitrogenase activity under a light-dark regimen. Synechococcus sp. strain RF-1 also utilizes nitrate, nitrite, or ammonium for growth. Under the diazotrophic growth, the nitrate uptake in Synechococcus sp. strain RF-1 was induced by nitrate or nitrite but repressed by ammonium. In contrast, a prominent nitrate reductase (NR) activity was detected in diazotrophically grown cells using the reduced methyl viologen assay. The NR activity was not inhibited by ammonium and only slightly enhanced by nitrate. The different expression patterns of nitrate uptake and NR in Synechococcus sp. strain RF-1 were reflected in general at the transcript level determined by reverse transcriptase PCR. Under both nitrate-induced and uninduced conditions, the in situ NR activity exhibited similar biphasic kinetics for nitrate. The recombinant NR encoded by the narB gene of Synechococcus sp. strain RF-1, expressed in E. coli, also showed the biphasic kinetics with similar pH and temperature profiles. By in-gel NR activity assay, the recombinant NarB was found to exist as a single form. Both the high- and low-affinity NR activities of the recombinant NarB showed the same thermostability. When modified at the N terminus by a polyhistidine tag, the recombinant NR activity was shifted from biphasic to hyperbolic kinetics and showed only a single K(m) for nitrate, indicating the functional importance of the NarB N-terminal structure in NR kinetics.

Bacterial Proteins↗

PubMed2001

Properties of hybrid enzymes between Synechococcus large subunits and higher plant small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase in Escherichia coli.

To explore the function of small subunits of Rubisco, three hybrid enzymes were synthesized in Escherichia coli by construction of a transcriptionally coupled expression system in which the synthetic small subunit gene of rice, tobacco, and wheat, respectively, was cloned downstream from the large subunit gene of Synechococcus sp. PCC6301. These coexpression products were detected by utilizing SDS-PAGE and confirmed by immunoblotting. The amount of carboxylase activity from the intact cells revealed that each higher plant small subunit was able to assemble with the Synechococcus large subunit octamer core to form an active heterologous enzyme in E. coli. However, in these heterologous enzymes, the interaction between large subunits and small subunits was very weak, the small subunit readily dissociated from the large subunit octamer core. A detailed kinetic assay was carried out with the partially purified hybrid enzymes. Compared to Synechococcus Rubisco, the activity of rice, tobacco, and wheat hybrid Rubisco decreased to 37, 61, and 37% of the original activity, respectively. These hybrid enzymes showed a greater affinity for CO2 and RuBP than Synechococcus Rubisco. The specificity factor of the three hybrid Rubiscos was 98, 84, and 76%, respectively, of the original. These results indicate for the first time that the small subunit contributes to the stability, catalytic efficiency, and CO2/O2 specificity of Rubisco together, which suggests that small subunits may be fruitful targets for engineering an improved Rubisco. Meanwhile, we found that sorbitol in the culture of induced cells promoted the production of active assembled enzyme and shortened the time to reach maximal expression.

Cyanobacteria↗

PubMed1996

The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants.

The Clp family consists of large, ubiquitous proteins that function as molecular chaperones and/or regulators of ATP-dependent proteolysis. A single copy gene coding for one of these proteins, ClpC, was cloned from the unicellular cyanobacterium Synechococcus sp. PCC 7942. The predicted polypeptide is most similar (ca. 88%) to the chloroplast-localized ClpC protein from higher plants. Using degenerate PCR primers specific for the two distinct ATP-binding domains characteristic of all ClpA-C proteins, partial sequences homologous to clpC from Synechococcus were also identified in five other cyanobacterial strains. The Synechococcus clpC gene is transcribed under standard growth conditions as a monocistronic message of around 2.7 kb. The level of this message, however, decreases slightly after a shift from 37 to 47.5 degrees C for 2 h, similar to expression previously observed for clpC mRNA from heat-shocked higher plants. At the protein level, the amount of ClpC remains relatively unchanged during the high temperature shift, while that of the known heat shock protein GroEL rises considerably. In contrast, the constitutive level of ClpC in Synechococcus increases considerably under conditions of rapid growth, both with increasing light intensities or CO2 concentrations. This, and the fact that attempts to inactivate clpC expression fail to produce a viable phenotype, suggest that ClpC activity is essential for growth in this obligate photoautotrophic cyanobacterium.

Adenosine Triphosphatases↗

PubMed1992

A nitrate reductase gene of the cyanobacterium Synechococcus PCC6301 inferred by heterologous hybridization, cloning and targeted mutagenesis.

DNA probes from the narG gene of Escherichia coli, which encodes the large polypeptide of respiratory nitrate reductase, show cross-hybridization at low stringency to a single region of the genome of the cyanobacterium Synechococcus PCC6301. This segment of cyanobacterial DNA was cloned as the insert of plasmid pDN1 and characterized. RNA complementary to pDN1 was shown to be substantially more abundant in nitrate grown cells of Synechococcus PCC6301 than in ammonium grown cells, thus parallelling the nitrate induction and ammonium repression of nitrate reductase activity in cultures of this cyanobacterium. A mutant of Synechococcus PCC6301 deficient in nitrate reductase activity was obtained after a potentially mutagenic transformation treatment using pDN1 as a donor. This mutant was restored to the wild type phenotype following stable integrative transformation with pDN1 DNA. Taken together these data suggest that pDN1 might encode a polypeptide of nitrate reductase. pDN1 is distinct from three clones of genes involved in nitrate assimilation that were isolated previously from the related cyanobacterium Synechococcus PCC7942 (Kuhlemeier et al., 1984a, J. Bact. 159, 36-41, and 1984b, Gene 31, 109-116).

Amino Acid Sequence↗

PubMed1998

Rapid diversification of marine picophytoplankton with dissimilar light-harvesting structures inferred from sequences of Prochlorococcus and Synechococcus (Cyanobacteria).

Cultured isolates of the unicellular planktonic cyanobacteria Prochlorococcus and marine Synechococcus belong to a single marine picophytoplankton clade. Within this clade, two deeply branching lineages of Prochlorococcus, two lineages of marine A Synechococcus and one lineage of marine B Synechococcus exhibit closely spaced divergence points with low bootstrap support. This pattern is consistent with a near-simultaneous diversification of marine lineages with divinyl chlorophyll b and phycobilisomes as photosynthetic antennae. Inferences from 16S ribosomal RNA sequences including data for 18 marine picophytoplankton clade members were congruent with results of psbB and petB and D sequence analyses focusing on five strains of Prochlorococcus and one strain of marine A Synechococcus. Third codon position and intergenic region nucleotide frequencies vary widely among members of the marine picophytoplankton group, suggesting that substitution biases differ among the lineages. Nonetheless, standard phylogenetic methods and newer algorithms insensitive to such biases did not recover different branching patterns within the group, and failed to cluster Prochlorococcus with chloroplasts or other chlorophyll b-containing prokaryotes. Prochlorococcus isolated from surface waters of stratified, oligotrophic ocean provinces predominate in a lineage exhibiting low G + C nucleotide frequencies at highly variable positions.

Animals↗

PubMed1998

Nucleic acid content of synechococcus spp. during growth in continuous light and light/dark cycles

Light-limited batch cultures of Synechococcus spp. strains PCC 6301 and WH 8103 exhibited a positive correlation between the specific growth rate and the cellular content of both RNA and DNA. The ratio of RNA to DNA increased with the growth rate in Synechococcus sp. strain WH 8103, as it does in heterotrophic bacteria, but remained constant in Synechococcus sp. strain PCC 6301. The cellular content of nucleic acids decreased during light periods and increased during dark periods in Synechococcus sp. strain PCC 6301 entrained by 12-h light/ 12-h dark (diurnal) cycles. This result was unexpected in light of experiments demonstrating a circadian increase in transcriptional activity during the subjective light periods and a decrease in transcriptional activity during subjective dark periods. The cyclical variation in cellular nucleic acid content during diurnal cycles appears to be in part a function of the timing of cell division and will influence estimates of in situ growth rates or relative abundances of cyanobacteria using oligonucleotide probes complementary to 16S rRNA.

Journal Article↗

PubMed1998

The Effect of Cyanophages on the Mortality of Synechococcus spp. and Selection for UV Resistant Viral Communities.

Abstract Viruses that cause lysis of Synechococcus spp. are present throughout the year in the western Gulf of Mexico. The effect of sunlight on loss rates of cyanophage infectivity was determined by incubating natural cyanophage communities and cyanophage isolates (strains S-PWM1 and S-PWM3) in UV-transparent bags at the surface, and at depth, on several occasions throughout the year. Decay rates of infectivity of natural cyanophage communities at the surface, at Port Aransas, Texas, USA, ranged from undetectable to 0.335 h-1, with the highest rates occurring during the summer. During the spring and winter, decay rates of cyanophage isolates and natural cyanophage communities were generally similar, but during summer, decay rates of isolates were as much as twofold higher than the natural communities. In situ incubations at two offshore stations during a bloom of Synechococcus spp. produced decay rates of 0.53 and 0.75 d-1, integrated over the mixed layer and averaged over 24 h. Based on a burst size of 81 viruses produced per lysed cell (measured for natural cyanobacterial communities in the Gulf of Mexico), cyanophages imposed mortality rates of 1 and 8%, respectively, on Synechococcus spp. In contrast, in nearshore incubations in the winter and spring, cyanophages were responsible for removing <1% of the Synechococcus cells on a daily basis. Only an estimated 2 to 3% of contacts led to viral infections (based on theoretical contact rates between host cells and cyanophages, and estimates of cyanophage mortality), regardless of the time of year or concentrations of viruses and hosts. These results indicate that natural cyanophage communities tolerate damage by solar radiation better in summer than in winter. Moreover, net decay rates of cyanophage infectivity in sunlight were similar, whether host cells were present or not, indicating that detectable cyanophage production did not occur during daytime in situ incubations.

Journal Article↗

PubMed1996

Construction and partial characterization of an L-amino acid oxidase-free Synechococcus PCC 7942 mutant and localization of the L-amino acid oxidase in the corresponding wild type.

The gene (aoxA) coding for an L-amino acid oxidase (L-AOX) with high specificity for basic L-amino acids (L-arginine being the best substrate) in the cyanobacterium Synechococcus PCC 6301 has previously been identified, sequenced and analysed (Bockholt, R., Masepohl, M., Kruft, V., Wittmann-Liebold, B. and Pistorius, E.K. (1995) Biochim. Biophys. Acta 1264, 289-293). Here we report on the inactivation of the aoxA gene in the closely related Synechococcus PCC 7942 by interrupting the gene with a kanamycin resistance cassette from Tn5. The mutant called D6 has no detectable L-AOX activity and no detectable L-AOX protein. Characterization of the mutant showed that in contrast to Synechococcus PCC 7942 wild-type (WT) cells the mutant cells can not grow on L-arginine as sole N-source, suggesting that the L-AOX is essential for growth on L-arginine. Mutant cells can grow on nitrate or ammonium as N-source under photoautotropic conditions with a growth rate of about 75% of the WT rate. Under these conditions the photosynthetic O2 evolving activity is reduced by about the same amount, and the pigment content, especially the phycobiliprotein content, is much lower than in WT cells, indicating that the mutant suffers from some type of deficiency. Immunocytochemical investigations and extraction of the soluble proteins from periplasma after plasmolysing the cell wall gave evidence that the L-AOX is predominantly located in the periplasma with only a small amount being intracellularly located. A model of the possible function of the L-AOX in Synechococcus PCC 6301/7942 will be given.

Amino Acid Oxidoreductases↗

PubMed1990

Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene (glgB): expression in Bacillus subtilis.

The nucleotide sequence of the Synechococcus sp. PCC7942 glgB gene has been determined. The gene contains a single open reading frame (ORF) of 2322 bp encoding a polypeptide of 774 amino acids (aa) with an Mr of 89,206. Extensive sequence similarity exists between the deduced aa sequence of the Synechococcus sp. glgB gene product and that of the Escherichia coli branching enzyme in the middle portions of the proteins (62% identical aa). In contrast, the N-terminal portions shared little homology. The sequenced region which follows glgB contains an ORF encoding 79 aa of the N terminus of a polypeptide that shares extensive sequence similarity (41% identical aa) with human and rat uroporphyrinogen decarboxylase. This suggests that the region downstream from glgB contains the hemE gene and, therefore, that the organization of genes involved in glycogen biosynthesis in Synechococcus sp. is different from that described for E. coli. A fusion gene was constructed between the 5' end of the Bacillus licheniformis penP gene and the Synechococcus sp. glgB gene. The fusion gene was efficiently expressed in the Gram+ micro-organism Bacillus subtilis and specified a branching enzyme with an optimal temperature for activity similar to the wild-type enzyme.

1,4-alpha-Glucan Branching Enzyme↗

PubMed1993

Cloning of a sensory-kinase-encoding gene that belongs to the two-component regulatory family from the cyanobacterium Synechococcus sp. PCC7942.

A screening method employing Escherichia coli was adopted to clone a sensory-kinase (SK)-encoding gene directly from a phylogenetically distant species, the phototrophic cyanobacterium Synechococcus sp. PCC7942. From the Synechococcus chromosomal DNA, we searched for DNA clones which are able to complement phenotypically not only an E. coli envZ mutant for the expression of ompC, but also an E. coli phoR/creC mutant for the expression of alkaline phosphatase. These E. coli genes are known to encode SK. A 0.75-kb DNA fragment was thus cloned under the control of the E. coli lac promoter carried on an E. coli plasmid vector. A larger DNA fragment encompassing an entire open reading frame was then cloned and its complete nucleotide (nt) sequence determined. The nt sequence corresponds to a gene that encodes a 43,280-Da protein of 387 amino acids with a high degree of homology to the bacterial SK. Thus, we succeeded in cloning a SK-encoding gene, which most likely functions in signal transduction in Synechococcus sp. PCC7942. Hence, the gene was designated sasA (Synechococcus adaptive-response SK A). The purified SasA protein was demonstrated in vitro to undergo autophosphorylation.

Adaptation, Physiological↗

PubMed1999

Molybdopterin guanine dinucleotide cofactor in Synechococcus sp. nitrate reductase: identification of mobA and isolation of a putative moeB gene.

The narC locus required for assimilatory nitrate reduction in the cyanobacterium Synechococcus sp. strain PCC 7942 was found to carry a mobA gene for molybdopterin guanine dinucleotide biosynthesis. Insertional inactivation of this gene blocked production of nitrate reductase in Synechococcus cells. We have previously described Synechococcus genes encoding homologues to molybdopterin biosynthesis proteins including MoaA, MoaC/MoaB, MoaD, MoaE, and MoeA, but not to MoeB. A cyanobacterial gene putatively encoding a protein composed of an amino-terminal domain of 260 amino acids homologous to Escherichia coli MoeB and of a carboxy-terminal extension of 130 amino acids was identified. Synechococcus mutants bearing only inactive versions of this putative moeB gene could not be isolated suggesting that it has function(s) additional to molybdopterin biosynthesis.

Bacterial Proteins↗

PubMed2000

Heterologous expression of clostridial hydrogenase in the Cyanobacterium synechococcus PCC7942.

The Clostridium pasteurianum hydrogenase I has been expressed in the cyanobacterium Synechococcus PCC7942. The Shine-Dalgarno sequence of the structural gene encoding hydrogenase I from C. pasteurianum was changed to that of the cat (chloramphenicol acetyltransferase) gene. The hydrogenase gene was cloned downstream of a strong promoter, isolated from Synechococcus PCC7942, with the cat gene as a reporter gene. Expression of clostridial hydrogenase was confirmed by Western and Northern blot analyses in Synechococcus and Escherichia coli, whereas in vivo/in vitro measurements and activity staining of soluble proteins separated on non-denaturing polyacrylamide gels revealed functional expression of hydrogenase only in cyanobacterial cells. The changed Shine-Dalgarno sequence appeared to be essential for the functional expression of clostridial hydrogenase in Synechococcus, but had no influence on the expression and activity of clostridial hydrogenase expressed in E. coli.

Blotting, Northern↗

PubMed1996

Enzymic and molecular characterization of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942: resistance of the enzyme to hydrogen peroxide.

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been purified to electrophoretic homogeneity from Synechococcus PCC 7942 cells. The native enzyme had a molecular mass of 160 kDa and consisted of four subunits with a molecular mass of 41 kDa. The activity was 6-fold higher with NADPH than with NADH; the apparent Km values for NADPH and NADH were 62 +/- 4.5 and 420 +/- 10.5 microM respectively. The gene encoding NADP-dependent GAPDH was cloned from the chromosomal DNA of Synechococcus 7942. A 1140 bp open reading frame, encoding an enzyme of 380 amino acid residues (approx.molecular mass of 41.3 kDa) was observed. The deduced amino acid sequence of the gene had a greater sequence similarity to the NADP-dependent and chloroplastic form than to the NAD-dependent and cytosolic form. The Synechococcus 7942 enzyme lacked one of the cysteines involved in the light-dependent regulation of the chloroplast enzymes of higher plants. The recombinant enzyme expressed in Escherichia coli as well as the native enzyme purified from Synechococcus 7942 cells were resistant to 1 mM H2O2.

Amino Acid Sequence↗

PubMed1986

Double-stranded gap repair in the photosynthetic prokaryote Synechococcus R2.

The photosynthetic cyanobacterium Synechococcus R2 is transformed by chimeric donor molecules lacking a functional replication origin but containing a region of homology to the recipient chromosome. These integrating donor molecules consist of a fragment of Synechococcus R2 chromosomal DNA cloned in the Escherichia coli vector pBR322 and interrupted by a piece of foreign DNA. During integration, this interrupting DNA is often lost by nonreciprocal exchange between homologous regions of donor and recipient. When transformed with donor molecules containing in vitro-generated double-stranded gaps or deletions as large as 20 kilobase pairs in the fragment homologous to the recipient chromosome, Synechococcus R2 can repair these lesions by using recipient information. Chromosomal DNA of the resulting transformants contains direct repeats of the recipient copy on either side of integrated pBR322 DNA. Homologous recombination between these repeats generates a circular molecule that can be recovered by transformation to E. coli. Plasmids recovered in E. coli contain the entire copy of information initially present in the region of the Synechococcus recipient corresponding to the donor gap or deletion. We suggest applications of this mechanism for cloning of genes identified by transposon mutagenesis.

Journal Article↗

PubMed1983

The nucleotide sequence for the large subunit of ribulose 1,5-bisphosphate carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301.

The gene for the large subunit (LSU) of ribulose 1,5-bisphosphate carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301, was cloned using the spinach LSU gene as a hybridization probe. The coding region of the Synechococcus LSU gene consists of 1419 nucleotides and shows 70% homology to the spinach nucleotide sequence. The derived amino acid sequence (472 amino acids) shows 81% homology to the spinach LSU and 78% to the maize LSU. Regions containing active-site residues are highly conserved among spinach, maize, and Synechococcus. In contrast, the first 13 amino acids are poorly conserved (30% homology), supporting the hypothesis that this region is proteolytically removed. The 5'-flanking region of the Synechococcus LSU gene contains sequences which correspond to bacterial consensus sequences for the -35 region and Pribnow box. Two 11-bp sequences in the 5' region show high homology to sequences in spinach and maize. One of these encompasses a possible ribosome-binding site. The 3'-flanking region contains a 35-bp sequence capable of giving rise to a terminator structure.

Base Sequence↗

PubMed1996

IdiA, a 34 kDa protein in the cyanobacteria Synechococcus sp. strains PCC 6301 and PCC 7942, is required for growth under iron and manganese limitations.

In the cyanobacteria Synechococcus PCC 6301 and PCC 7942 a protein with an apparent molecular mass of about 34 kDa (called IdiA for iron-deficiency-induced protein A) accumulates under iron and managanese limitation. IdiA from Synechococcus PCC 6301 was partially sequenced, showing that the N-terminal amino acid is an alanine. Moreover, the gene encoding this protein in Synechococcus PCC 6301 has been identified and completely sequenced. The idiA gene codes for a protein starting with valine and consisting of 330 amino acid residues. Thus, IdiA is apparently synthesized as a precursor protein of 36.17 kDa and cleaved to its mature form of 35.01 kDa between two alanine residues at positions 9 and 10. IdiA is a highly basic protein having an isoelectric point of 10.55 (mature protein). Comparison of the amino acid sequence of IdiA with protein sequences in the database revealed that IdiA has similarities to two basic bacterial iron-binding proteins, SfuA from Serratia marcescens and Fbp from Neisseria gonorrhoeae. Insertional inactivation of the idiA gene in Synechococcus PCC 7942 resulted in a mutant which was unable to grow under iron- or manganese-limiting conditions. Manganese limitation of the mutant strain led to a drastic reduction of photosystem II activity (O2 evolution) within less than 48 h, while wild-type cells required a prolonged cultivation in Mn-deficient medium before an effect on photosystem II was observed. Thus, IdiA is a protein involved in the process of providing photosystem II with manganese.

Amino Acid Sequence↗

PubMed1999

The marine cyanobacterium Synechococcus sp. WH7805 requires urease (urea amidohydrolase, EC 3.5.1.5) to utilize urea as a nitrogen source: molecular-genetic and biochemical analysis of the enzyme.

Cyanobacteria assigned to the genus Synechococcus are an important component of oligotrophic marine ecosystems, where their growth may be constrained by low availability of fixed nitrogen. Urea appears to be a major nitrogen resource in the sea, but little molecular information exists about its utilization by marine organisms, including Synechococcus. Oligonucleotide primers were used to amplify a conserved fragment of the urease (urea amidohydrolase, EC 3.5.1.5) coding region from cyanobacteria. A 5.7 kbp region of the genome of the unicellular marine cyanobacterium Synechococcus sp. strain WH7805 was then cloned, and genes encoding three urease structural subunits and four urease accessory proteins were sequenced and identified by homology. The WH7805 urease had a predicted subunit composition typical of bacterial ureases, but the organization of the WH7805 urease genes was unique. Biochemical characteristics of the WH7805 urease enzyme were consistent with the predictions of the sequence data. Physiological data and sequence analysis both suggested that the urease operon may be nitrogen-regulated by the ntcA system in WH7805. Inactivation of the large subunit of urease, ureC, prevented WH7805 and Synechococcus WH8102 from growing on urea, demonstrating that the urease genes cloned are essential to the ability of these cyanobacteria to utilize urea as a nitrogen source.

Amino Acid Sequence↗

PubMed1999

Molecular characterization of idiA and adjacent genes in the cyanobacteria Synechococcus sp. strains PCC 6301 and PCC 7942.

IdiA (iron-deficiency-induced protein A) is a protein expressed at highly elevated levels in Synechococcus sp. strains PCC 6301 and PCC 7942 under Fe- or Mn-limiting growth conditions. Besides being similar to two bacterial Fe-binding proteins, SfuA and FbpA, IdiA shows similarity to two ORFs (slr0513 and sir1295) of Synechocystis sp. PCC 6803. Northern blot analysis detected one transcript of about 1300 nt in RNA extracted from Synechococcus sp. PCC 6301 and PCC 7942 grown under Fe deficiency. The intensity of this transcript was considerably reduced in Fe-sufficient culture. It could be further shown that the regulation of IdiA expression is at the transcriptional level and that transcription and translation of IdiA are closely linked. Primer extension analysis indicated a single transcriptional start site 193 nt upstream of the first presumed translational start codon. Moreover, molecular characterization of the entire 5.8 kb chromosomal HindIII DNA fragment carrying the idiA gene from Synechococcus sp. PCC 6301 led to the identification of six long ORFs in addition to idiA. The two genes adjacent to idiA, and dpsA located 2018 nt downstream of idiA, were insertionally inactivated in Synechococcus sp. PCC 7942 and the corresponding mutants were partially characterized. These experiments provide evidence that the gene products of idiB, located immediately downstream of idiA, and of dpsA are involved in the activation of IdiA expression, since the absence of each of these two gene products prevents the greatly elevated expression of IdiA under nutrient deficiency.

Amino Acid Sequence↗