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PubMed1986

Assembly of cyanobacterial and higher plant ribulose bisphosphate carboxylase subunits into functional homologous and heterologous enzyme molecules in Escherichia coli.

The genes for the large (rbcL) and small (rbcS) subunits of ribulose-1,5 bisphosphate carboxylase-oxygenase (RuBPCase) from the cyanobacterium Synechococcus PCC 6301, and the rbcS gene of wheat, have been expressed in Escherichia coli in order to study homologous and heterologous enzyme assembly. Synechococcus L subunits expressed in E. coli in the absence of S subunits assemble into oligomeric structures without detectable enzyme activity. Co-expression of L and S subunits, achieved after infection with an M13 recombinant phage containing the rbcS gene, restores enzyme activity, thus demonstrating the essential role of S in the formation of an active RuBPCase. The S subunit, however, is neither required for the solubility nor for the assembly of the L subunits into oligomeric forms. The specific activity of the homologous Synechococcus RuBPCase can be modulated by changing the intracellular pool size of S by phage infection. Heterologous assembly between L subunits of Synechococcus and S subunits of wheat can be demonstrated and results in a functional enzyme. The hybrid RuBPCase has approximately 10% of the activity of the homologous Synechococcus enzyme.

Journal Article↗

PubMed2003

Toward an understanding of cell growth and the cell division cycle of unicellular photoautotrophic cyanobacteria.

The cell division cycle of Synechococcus sp. strain PCC 6301 in light is characterized by the sequential and orderly appearance of macromolecular synthesis periods. In the dark, macromolecular synthesis and cell division are severely curtailed. When dark-incubated cultures are reexposed to light, a new cell cycle is initiated. The pattern of the cell events displayed by Synechococcus in light and the absence of sustained growth in dark incubation conditions suggests that light-activated regulatory molecules control macromolecular synthesis and the cell division cycle. For example, ribosomal RNA synthesis is stimulated by a light-activated DNA binding factor in light but not in the dark. Light/dark conditions induce cell synchrony in Prochlorococcus. Distinct G1, S and G2 phases characterize cell cycles of marine Synechococcus and Prochlorococcus. Cell division in Synechococcus elongatus PCC 7942 and marine Synechococcus is controlled by circadian oscillators.

Cell Cycle↗

PubMed2001

Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: evidence for rapid evolution of genetic heterogeneity.

Prochlorococcus is a major photosynthetic prokaryote in nutrient-limited, open ocean environments and an important participant in the global carbon cycle. This phototroph is distinct from other members of the cyanobacterial lineage to which it belongs because it utilizes a chlorophyll a2/b(2) light-harvesting complex as its major antenna, instead of phycobilisomes. Recently, genes encoding the phycobiliprotein phycoerythrin were identified in several Prochlorococcus isolates, thus making it the only extant photosynthetic prokaryote to possess a chlorophyll a/b antenna as well as phycobiliprotein genes. In order to understand the evolution of phycobiliproteins in this genus, the authors have sequenced the phycoerythrin genes of two isolates that are the most deeply branching in the Prochlorococcus lineage and share the highest degree of 16S rDNA sequence similarity to phycobilisome-containing marine SYNECHOCOCCUS: Sequence analyses suggest that within the Prochlorococcus lineage, the selective forces shaping the evolution of the phycoerythrin gene set have not been uniform. Although strains that are most closely related to marine Synechococcus possess genes (cpeB, cpeA) encoding both subunits of phycoerythrin, a more recently evolved strain is shown to lack cpeA and to possess a degenerate form of cpeB. Differences in phycoerythrin gene sequences between Prochlorococcus and Synechococcus appear to be consistent with a model of elevated mutation rates rather than relaxed selection. This suggests that although phycoerythrin is not a major constituent of the light-harvesting apparatus in Prochlorococcus, as it is in Synechococcus, the cpeB and cpeA genes are still under selection, albeit a different type of selection than in Synechococcus. The evolution of the Prochlorococcus light-harvesting antenna complex provides an important system for understanding the origins and scope of phylogenetic diversity in ocean ecosystems.

Amino Acid Sequence↗

PubMed1983

Identification and enumeration of marine chroococcoid cyanobacteria by immunofluorescence.

We used an indirect immunofluorescence technique to permit the identification and enumeration of individual or closely related strains of chroococcoid cyanobacteria of the general Synechococcus and Synechocystis in natural seawater samples. Antisera directed against each of five strains (two phycoerythrin-containing Synechococcus strains, two phycocyanin-containing Synechococcus strains, and one Synechocystis strain) were produced and tested for cross-reactions with cultures of a variety of cyanobacteria and representatives of other algae and bacteria. Each antiserum was relatively specific. The observed cross-reactions occurred between strains that were isolated from similar oceanic environments. We were able, therefore, to apply this technique to field samples. Preliminary results for April to December 1982 in Great South Bay, New York, show that Synechocystis populations are present only during spring and summer, phycocyanin-containing Synechococcus strains are only a minor component in the spring and summer, and phycoerythrin-containing Synechococcus populations become significant in summer and remain so until late fall or winter.

Journal Article↗

PubMed1994

Nucleation of celestite and strontianite on a cyanobacterial s-layer.

Synechococcus strain GL24 is a unicellular cyanobacterium that was isolated from Fayetteville Green Lake, New York, a meromictic lake which has high Ca and SO(4) concentrations. Epicellular mineralization of Synechococcus cells in the lake is the mechanism by which extensive calcitic bioherms (or microbial reefs) have been formed on the lake's shore and a marl sediment has been built on the lake bottom. Previous studies have shown that calcium carbonate (calcite) formation on the Synechococcus surface is dependent upon an alkaline pH, which is produced in the cellular microenvironment by the cells as their activity increases with seasonal warming of the lake water. At the circumneutral pH of bulk lake water, calcium sulfate (gypsum) is formed. In this study, we show that Synechococcus mediates a similar sulfate-to-carbonate transformation when Sr is the major divalent cation present, forming celestite and strontianite. In experimental systems to which equimolar amounts of Ca and Sr, Ca or Sr and Mg, or all three ions together were added to artificial lake water, Ca and Sr were incorporated equally into mineral formation to form CaSr(CO(3))(2). No Mg -containing carbonates were formed when either or both of the other two ions were present. Mineral formation takes place on a hexagonally arranged proteinaceous template (an S-layer) which forms the outermost surface of the Synechococcus cell. Our results provide evidence that the S-layer exhibits selectivity with respect to the ions bound and subsequently incorporated into carbonate minerals and that celestite and strontianite, previously thought to be purely evaporitic minerals, can be biogenically formed.

Journal Article↗

PubMed2025

Picocyanobacteria in the Chesapeake Bay: isolation, diversity, and adaptation.

Tiny unicellular cyanobacteria or picocyanobacteria (0.5-3 µm) are important due to their ecological significance. Chesapeake Bay is a temperate estuary that contains abundant and diverse picocyanobacteria. Studies of Chesapeake Bay picocyanobacteria in the past 20 years led to the finding of new members of subcluster 5.2 Synechococcus. They laid the foundation for revealing the ecophysiology, biogeography, genomics, and molecular evolution of picocyanobacterial in the Chesapeake Bay and other coastal estuaries. The Bay picocyanobacteria are known to better tolerate the changes in temperature, salinity, and heavy metals compared to their coastal and open-ocean counterparts. Many picocyanobacteria isolated from the Bay contain rich toxin-antitoxin (TA) genes, suggesting that the TA system may provide them with a genetic advance to cope with variable estuarine environments. Distinct winter and summer picocyanobacteria are present in the Bay, suggesting a dynamic seasonal shift of the picocyanobacterial community in the temperate estuary. While the Bay contains subcluster 5.2 Synechococcus, it also contains freshwater Synechococcus, Cyanobium, and marine Synechococcus due to river influx and the ocean's tidal influence. Some Chesapeake Bay picocyanobacterial clades were found in the Bering Sea and Chukchi Sea, showing a link between the Bay and polar picocyanobacteria. Genomic sequences of estuarine picocyanobacteria provide new insight into the taxonomy and evolution of freshwater, estuarine, and marine unicellular cyanobacteria. Estuaries connect freshwater and marine ecosystems. This overview attempts to extend what we learned from Chesapeake Bay picocyanobacteria to picocyanobacteria in freshwater and marine waters.

Chesapeake Bay↗

PubMed2005

The distribution of cyanobacteria across physical and chemical gradients in hot springs in northern Thailand.

We mapped the distribution of mat forming cyanobacteria along the thermal gradient from 30 to 80 degrees C, in nine hot spring districts in northern Thailand. Nineteen genera and 36 species were identified by morphometric analysis. Water temperature was the predominant determinant of community structure in the springs. The diversity of cyanobacterial morphotypes fell as temperature increased. Water chemistry (pH, alkalinity and ammonia concentration) was a much weaker descriptor of the floral similarity between the springs. The morphotypes which dominated all springs were Synechococcus lividus and Synechococcus sp. (>40 and <80 degrees C) and Phormidium boryanum (>30 and <60 degrees C). The occurrence of Synechococcus lividus and Synechococcus sp. in every spring at 70 degrees C or more, implied there was no regional barrier to the distribution of these highly thermophilic taxa. Conversely, there were regional differences in the diversity of mat communities growing below 60 degrees C. The most depauperate flora were in the northernmost springs (SKP, TPN, PD, JS) and the springs further south around Chiang Mai had more diverse flora, suggestive of barriers to the dispersal of some taxa. More discriminating analyses using molecular tools will be required to determine whether the ubiquitous distribution Synechoccoccus morphotypes above 60 degrees C masks a genotypic diversity, comparable to the morphotype diversity observed below 60 degrees C.

Cyanobacteria↗

PubMed1994

Identification of conserved domains in the delta 12 desaturases of cyanobacteria.

Cyanobacterial genes for enzymes that desaturate fatty acids at the delta 12 position, designated desA, were isolated from Synechocystis PCC6714, Synechococcus PCC7002 and Anabaena variabilis by cross-hybridization with a DNA probe derived from the desA gene of Synechocystis PCC6803. The genes of Synechocystis PCC6714, Synechococcus PCC7002 and A. variabilis encode proteins of 349, 347 and 350 amino acid residues, respectively. The transformation of Synechococcus PCC7942 with the desA genes from Synechocystis PCC6714, Synechococcus PCC7002 and A. variabilis was associated with the ability to introduce a second double bond at the delta 12 position of fatty acids. The amino acid sequence of the products of the desA genes revealed the presence of four conserved domains. Since one of the conserved domains was also found in the amino acid sequences of omega 3 desaturases of Brassica napus and mung bean, this domain may play an essential role in the introduction of a double bond into fatty acids bound to membrane lipids.

Amino Acid Sequence↗

PubMed1996

Regulation, unique gene organization, and unusual primary structure of carbon fixation genes from a marine phycoerythrin-containing cyanobacterium.

Marine phycoerythrin-containing cyanobacteria are major contributors to the overall productivity of the oceans. The present study indicates that the structural genes of the carbon assimilatory system are unusually arranged and possess a unique primary structure compared to previously studied cyanobacteria. Southern blot analyses of Synechococcus sp. strain WH7803 chromosomal DNA digests, using the ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit gene from Synechococcus sp. strain PCC6301 as a heterologous probe, revealed the presence of a 6.4 kb HindIII fragment that was detectable at only low stringency. Three complete open reading frames (ORFs) were detected within this fragment. Two of these ORFs potentially encode the Synechococcus sp. strain WH7803 rbcL and rbcS genes. The third ORF, situated immediately upstream from rbcL, potentially encodes a homologue of the ccmK gene from Synechococcus sp. strain PCC7942. The deduced amino acid sequences of each of these ORFs are more similar to homologues among the beta/gamma purple bacteria than to existing cyanobacterial homologues and phylogenetic analysis of the Rubisco large and small subunit sequences confirmed an unexpected relationship to sequences from among the beta/gamma purple bacteria. This is the first instance in which the possibility has been considered that an operon encoding three genes involved in carbon fixation may have been laterally transferred from a purple bacterium. Analysis of mRNA extracted from cells grown under diel conditions indicated that rbcL, rbcS and ccmK were regulated at the transcriptional level; specifically Rubisco transcripts were highest during the midday period, decreased at later times during the light period and eventually reached a level where they were all but undetectable during the dark period. Primer extension analysis indicated that the ccmK, rbcL and rbcS genes were co-transcribed.

Amino Acid Sequence↗

PubMed1999

Mechanisms of dominance: coexistence of picocyanobacterial genotypes in a freshwater ecosystem

The autotrophic picoplankton of the pelagic zone of the mesotrophic Lake Constance is dominated by phycoerythrin-rich unicellular cyanobacteria phylogenetically related to the marine Synechococcus and Prochlorococcus cluster. In Lake Constance, the abundance of picocyanobacteria shows a recurrent pattern of seasonal variations. Evidence of diverse subpopulations was obtained by electron-microscopic examination of natural water samples and isolated strains that unveiled different surface structures of picocyanobacteria. Further evidence was obtained by DNA analysis of 26 clonal isolates representing 12 different genotypes. Variations in light and nutrient supply revealed distinct abilities of the genetically different strains to cope with these stress situations. Furthermore, cultured heterotrophic nanoflagellates exhibited differential feeding preferences for certain Synechococcus strains. The findings imply that growth and loss rates of the natural cyanobacterial community may be influenced by its genetic composition. Phylogenetic analyses of isolated strains indicated that the physiological diversification of pelagic Synechococcus spp. has occurred during a recent adaptive radiation. An example for genetic mechanisms underlying physiological diversification is indicated by mobile DNA elements found in a Synechocystis strain also isolated from the pelagic zone of Lake Constance. The observations suggest that dominance of Synechococcus spp. was achieved by evolutionary adaptation and coexistence of numerous genotypes generating a physiologically highly diversified population.

Journal Article↗

PubMed1990

Phycobiliprotein methylation. Effect of the gamma-N-methylasparagine residue on energy transfer in phycocyanin and the phycobilisome.

The phycobiliproteins contain a conserved unique modified residue, gamma-N-methylasparagine at beta-72. This study examines the consequences of this methylation for the structure and function of phycocyanin and of phycobilisomes. An assay for the protein asparagine methylase activity was developed using [methyl-3H]S-adenosylmethionine and apophycocyanin purified from Escherichia coli containing the genes for the alpha and beta subunits of phycocyanin from Synechococcus sp. PCC 7002 as substrates. This assay permitted the partial purification, from Synechococcus sp. PCC 6301, of the activity that methylates phycocyanin and allophycocyanin completely at residue beta-72. Using the methylase assay, two independent nitrosoguanidine-induced mutants of Synechococcus sp. PCC 7942 were isolated that do not exhibit detectable phycobiliprotein methylase activity. These mutants, designated pcm 1 and pcm 2, produce phycocyanin and allophycocyanin unmethylated at beta-72. The phycobiliproteins in these mutants are assembled into phycobilisomes and can be methylated in vitro by the partially purified methylase from Synechococcus sp. PCC 6301. The mutants produce phycobiliproteins in amounts comparable to those of wild-type and the mutant and wild-type phycocyanins are equivalent with respect to thermal stability profiles. Monomeric phycocyanins purified from these strains show small spectral shifts that correlate with the level of methylation. Phycobilisomes from the mutant strains exhibit defects in energy transfer, both in vivo and in vitro, that are also correlated with deficiencies in methylation. Unmethylated or undermethylated phycobilisomes show greater emission from phycocyanin and allophycocyanin and lower fluorescence emission quantum yields than do fully methylated particles. The results support the conclusion that the site-specific methylation of phycobiliproteins contributes significantly to the efficiency of directional energy transfer in the phycobilisome.

Asparagine↗

PubMed2003

Phages of the marine cyanobacterial picophytoplankton.

Cyanobacteria of the genera Synechococcus and Prochlorococcus dominate the prokaryotic component of the picophytoplankton in the oceans. It is still less than 10 years since the discovery of phages that infect marine Synechococcus and the beginning of the characterisation of these phages and assessment of their ecological impact. Estimations of the contribution of phages to Synechococcus mortality are highly variable, but there is clear evidence that phages exert a significant selection pressure on Synechococcus community structure. In turn, there are strong selection pressures on the phage community, in terms of both abundance and composition. This review focuses on the factors affecting the diversity of cyanophages in the marine environment, cyanophage interactions with their hosts, and the selective pressures in the marine environment that affect cyanophage evolutionary biology.

Bacteriophages↗

PubMed2002

Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies.

Prochlorococcus and Synechococcus are abundant unicellular cyanobacteria and major participants in global carbon cycles. Although they are closely related and often coexist in the same ocean habitat, they possess very different photosynthetic light-harvesting antennas. Whereas Synechococcus and the majority of cyanobacteria use phycobilisomes, Prochlorococcus has evolved to use a chlorophyll a(2)/b(2) light-harvesting complex. Here, we present a scenario to explain how the Prochlorococcus antenna might have evolved in an ancestral cyanobacterium in iron-limited oceans, resulting in the diversification of the Prochlorococcus and marine Synechococcus lineages from a common phycobilisome-containing ancestor. Differences in the absorption properties and cellular costs between chlorophyll a(2)/b(2) and phycobilisome antennas in extant Prochlorococcus and Synechococcus appear to play a role in differentiating their ecological niches in the ocean environment.

Biological Evolution↗

PubMed1992

A hybrid ribulosebisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor.

Two hybrid ribulose-1,5 bisphosphate carboxylase/oxygenase (RubisCO) enzymes were constructed using RubisCO small subunit genes (rbcS) from two eucaryotic marine organisms, Cylindrotheca sp. N1 and Olisthodiscus luteus, cloned downstream of the RubisCO large subunit gene (rbcL) of the cyanobacterium Synechococcus PCC 6301. The expression products synthesized by Escherichia coli JM107 (pVTAC223 and pANOLI) were purified and examined by polyacrylamide gel electrophoresis and compared to the purified products generated by E. coli MV1190 (pBGL710), containing cyanobacterial rbcL and rbcS genes. Both Cylindrotheca and Olisthodiscus small subunits were able to assemble in vivo with the Synechococcus large subunit octamer to form heterologous hexadecameric L8S8 enzymes, the pVTAC223 and pANOLI hybrid enzymes, respectively. Like the Synechococcus RubisCO, the hybrid enzymes were rapidly activated by Mg2+ plus HCO3-, even in the presence of RuBP. The hybrid enzymes, however, were considerably more sensitive to the competitive inhibitor 6-phosphogluconate. Detailed kinetic analysis indicated that while the carboxylase activity of both chimeric enzymes was severely reduced, in the case of the pVTAC223 hybrid enzyme, the degree of partitioning between carboxylation and oxygenation was increased nearly 60% relative to the Synechococcus RubisCO. Other kinetic properties, including the Michaelis constants for the gaseous substrates and RuBP, were altered in the hybrid proteins. These studies also led to the finding that the substrate specificity factor of the Cylindrotheca RubisCO is unusually high.

Carbon Dioxide↗

PubMed2006

Translation initiation of cyanobacterial rbcS mRNAs requires the 38-kDa ribosomal protein S1 but not the Shine-Dalgarno sequence: development of a cyanobacterial in vitro translation system.

Little is known about the biochemical mechanism of translation in cyanobacteria though substantial studies have been made on photosynthesis, nitrogen fixation, circadian rhythm, and genome structure. To analyze the mechanism of cyanobacterial translation, we have developed an in vitro translation system from Synechococcus cells using a psbAI-lacZ fusion mRNA as a model template. This in vitro system supports accurate translation from the authentic initiation site of a variety of Synechococcus mRNAs. In Synechococcus cells, rbcL and rbcS encoding the large and small subunits, respectively, of ribulose-1,5-bisphosphate carboxylase/oxygenase are co-transcribed as a dicistronic mRNA, and the downstream rbcS mRNA possesses two possible initiation codons separated by three nucleotides. Using this in vitro system and mutated mRNAs, we demonstrated that translation starts exclusively from the upstream AUG codon. Although there are Shine-Dalgarno-like sequences in positions similar to those of the functional Shine-Dalgarno elements in Escherichia coli, mutation analysis indicated that these sequences are not required for translation. Assays with deletions within the 5'-untranslated region showed that a pyrimidine-rich sequence in the -46 to -15 region is necessary for efficient translation. Synechococcus cells contain two ribosomal protein S1 homologues of 38 and 33 kDa in size. UV cross-linking and immunoprecipitation experiments suggested that the 38-kDa S1 is involved in efficient translation via associating with the pyrimidine-rich sequence. The present in vitro translation system will be a powerful tool to analyze the basic mechanism of translation in cyanobacteria.

Base Sequence↗

PubMed2004

Natural community structure of cyanobacteria in the South China Sea as revealed by rpoC1 gene sequence analysis.

AIMS: To examine the community structure of cyanobacterial populations of the South China Sea on the surface and at depth of 80 m. METHODS AND RESULTS: Direct PCR amplification of RNA polymerase (rpoC1) genes from environmental DNAs extracted from seawater, and cloning of the fragments and sequence analysis were used. A great diversity of Prochlorococcus and Synechococcus were detected at the investigation site. Genetically related Prochlorococcus were found in both layers while Synechococcus were found only on the surface. Prochlorococcus were clustered with the known high-light adapted II genotypes, and further divided into seven groups. Synechococcus could be divided into two groups, and the second group could be further subdivided into several clades. CONCLUSION: The dominant genotype of Prochlorococcus was high-light adapted II genotype, and Synechococcus were distributed basically on the surface. SIGNIFICANCE AND IMPACT OF THE STUDY: This is the first report about the cyanobacterial community structure in the South China Sea, and an important supplement to the current understanding of the relationship between genetic and ecological diversity and environments.

China↗

PubMed1993

Amplification of ribulose biphosphate carboxylase/oxygenase large subunit (RuBisCO LSU) gene fragments from Thiobacillus ferrooxidans and a moderate thermophile using polymerase chain reaction.

Southern blot analysis of DNA from an iron-oxidising moderate thermophile NMW-6 and from Thiobacillus ferrooxidans strain TFI-35 demonstrated sequences homologous to the RuBisCO LSU gene of Synechococcus. DNA fragments (457 bp) encoding part of the RuBisCO LSU gene (amino acids 73-200) were amplified from the genomic DNA of Thiobacillus ferrooxidans and the moderate thermophile NMW-6 using the polymerase chain reaction (PCR) technique (Saiki et al. (1985) Science 233, 1350-1354). A comparison with the LSU sequences from T. ferrooxidans, Alcaligenes eutrophus, Chromatium vinosum, Synechococcus and Spinacea oleracea, which all have RuBisCOs with a hexadecameric structure, showed that the RuBisCO LSU gene sequence from NMW-6 appeared to be most closely related to that of the hydrogen bacterium A. eutrophus which showed 71.9% homology at the amino acid level. Despite its physiological similarity, T. ferrooxidans showed only 64.1% homology to the amino acid sequence from NMW-6 and had the lowest DNA homology (60.9%) of the hexadecameric type RuBisCOs. In the region sequenced, T. ferrooxidans and the RuBisCOs of the phototrophs C. vinosum, Synechococcus and S. oleracea, had 17 residues that were completely conserved which were substituted in both NMW-6 and A. eutrophus, 11 of these being identical substitutions. Comparison of the nucleotide and derived amino acid sequences of the RuBisCO LSU fragment from T. ferrooxidans with other RuBisCO sequences indicated a closer relationship to the hexadecameric type LSU genes of photosynthetic origin than to that of A. eutrophus. The T. ferrooxidans amino acid sequence showed 93.8%, 78.9% and 77.3% homology, respectively, to the C. vinosum, Synechococcus and S. oleracea (spinach) sequences but only 56.2% to A. eutrophus. The DNA sequence from Rhodospirillum rubrum, which has the atypical large subunit dimer RuBisCO structure with no small subunit, showed 39.2% and 42.7% homology, respectively, with the sequences of NMW-6 and T. ferrooxidans, and 25.0% and 29.7% amino acid homology, indicating that the DNA homology was substantially random in nature. PCR fragments (126 bp) that overlaped the last 15 codons of the fragments above were also amplified and sequenced. They showed incomplete homology with the larger fragments, supporting evidence obtained from Southern hybridizations that T. ferrooxidans and the moderate thermophile NMW-6 have multiple copies of RuBisCO LSU genes.

Amino Acid Sequence↗

PubMed1993

Measurement of rRNA Variations in Natural Communities of Microorganisms on the Southeastern U.S. Continental Shelf.

The development of a clear understanding of the physiology of marine prokaryotes is complicated by the difficulties inherent in resolving the activity of various components of natural microbial communities. Application of appropriate molecular biological techniques offers a means of overcoming some of these problems. In this regard, we have used direct probing of bulk RNA purified from selective size fractions to examine variations in the rRNA content of heterotrophic communities and Synechococcus populations on the southeastern U.S. continental shelf. Heterotrophic communities in natural seawater cultures amended with selected substrates were examined. Synechococcus populations were isolated from the water column by differential filtration. The total cellular rRNA content of the target populations was assayed by probing RNA purified from these samples with an oligonucleotide complementing a universally conserved region in the eubacterial 16S rRNA (heterotrophs) or with a 1.5-kbp fragment encoding the Synechococcus sp. strain WH 7803 16S rRNA (cyanobacteria). The analyses revealed that heterotrophic bacteria responded to the addition of glucose and trace nutrients after a 6-h lag period. However, no response was detected after amino acids were added. The cellular rRNA content increased 48-fold before dropping to a value 20 times that detected before nutrients were added. Variations in the rRNA content from Synechococcus spp. followed a distinct diel pattern imposed by the phasing of cell division within the irradiance cycle. The results indicate that careful application of these appropriate molecular biological techniques can be of great use in discerning basic physiological characteristics of selected natural populations and the mechanisms which regulate growth at the subcellular level.

Journal Article↗