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PubMed1989

Cloning and expression of the branching enzyme gene (glgB) from the cyanobacterium Synechococcus sp. PCC7942 in Escherichia coli.

Using the glgB gene from Escherichia coli as a hybridization probe, the gene encoding the branching enzyme of the cyanobacterium Synechococcus sp. PCC7942 has been identified on a 3.9-kb PstI fragment which was cloned into plasmid pUC9. Two types of plasmids have been isolated. Plasmid pKVN1 was expressing the Synechococcus sp. gene as was shown by complementation of the glgB mutation of E. coli KV832. Plasmid pKVN2, which carried the same insert in the opposite orientation was unable to complement E. coli KV832, indicating that the promoter of the cloned gene was either absent or was not recognized in E. coli. Determination of branching activity in extracts of Synechococcus sp. and E. coli KV832[pKVN1] showed that the enzyme was optimally active at approximately 35 degrees C. No significant activity was present at temperatures higher than 55 degrees C, reflecting the mesophilic nature of the cloned enzyme. In a cell-free coupled transcription-translation system the cloned gene specified two proteins of 84 kDa and 72 kDa, respectively, which are probably translated independently from the same gene by initiation at two different start codons.

1,4-alpha-Glucan Branching Enzyme↗

PubMed2004

Energy transfer and trapping in the Photosystem I complex of Synechococcus PCC 7942 and in its supercomplex with IsiA.

The cyanobacterium Synechococcus PCC 7942 grown under iron starvation assembles a supercomplex consisting of a trimeric Photosystem I (PSI) complex encircled by a ring of 18 CP43' or IsiA complexes. It has previously been shown that PSI of Synechococcus PCC 7942 contains less special long-wavelength ('red') chlorophylls than PSI of most other cyanobacteria. Here we present a comparative analysis by time-resolved absorption difference and fluorescence spectroscopy of the processes of energy transfer and trapping in trimeric PSI and PSI-IsiA supercomplexes from Synechococcus PCC 7942. All experiments were performed with the primary electron donor of PSI (P700) in the oxidized state. Our data suggest that in the PSI complex the excitation energy is equilibrated with a lifetime of 0.6 ps among the so-called bulk chlorophylls, is distributed in 3-4 ps between the bulk and red chlorophylls, and is trapped in the reaction center in 19 ps. This trapping time is shorter than that observed for other cyanobacteria, which we attribute to the lower content of red chlorophylls in PSI of this organism. In the PSI-IsiA supercomplexes, the distribution of excited states is blue-shifted compared to that in PSI, leading to a lengthening of the equilibration processes. We attributed a phase of about 1 ps to initial energy equilibration steps among the IsiA and PSI core bulk chlorophylls, a 5-7 ps phase to equilibration between bulk and red chlorophylls within the PSI core, and a 38 ps phase to trapping in the reaction center. The data suggest that the excitation energy is equilibrated among the IsiA and PSI core antenna chlorophylls before trapping occurs. Data analysis based on a simple kinetic model revealed an intrinsic rate constant for energy transfer from IsiA to PSI in the range of 2+/-1 ps. Based on this value we suggest the presence of one or more linker chlorophylls between the IsiA and PSI core complexes. These results confirm that IsiA acts as an effective light-harvesting antenna for PSI.

Bacterial Proteins↗

PubMed1997

Nitrogen source-dependent expression of a 126 kDa protein in the plasma membrane of the cyanobacterium Synechococcus PCC 7942.

The expression of a 126 kDa protein in the cytoplasmic membrane of Synechococcus PCC 7942 is shown to be dependent on the nitrogen source. It is absent in ammonium-grown cells and its quantity is inversely related to the concentration of nitrate or nitrite in the growth medium. Addition of ammonium-grown cells to a medium containing nitrate or L-methionine-DL-sulfoximine results in the expression of this protein. It is present in the plasmalemma of the Synechococcus NC3 mutant (nrtC gene deleted) and absent in the NA3 mutant (nrtABCD genes deleted). These results may suggest involvement of the 126 kDa protein in nitrate transport through Synechococcus cytoplasmic membrane.

Adenosine Triphosphate↗

PubMed1998

Cloning and characterization of the genes coding for two porins in the unicellular cyanobacterium Synechococcus PCC 6301.

The genes somB and somA (Synechococcus outer membrane), lying in tandem organization in the genome of Synechococcus PCC 6301, encode two porins in the outer membrane of this unicellular cyanobacterium. Northern blot and primer extension experiments revealed that somA and somB are not comprising an operon, as each gene encodes a transcript of 1.7 kb length and has a distinct transcriptional start site. The deduced SomA and SomB protein sequences include typical N-terminal signal peptides and reveal 60% homology (50% identical residues) to each other as well as significant homology to six protein sequences deduced from open reading frames sequenced in the genome of the unicellular cyanobacterium Synechocystis PCC 6803. Furthermore, SomA possesses an overall identity of 97% to the functionally not yet characterized outer-membrane protein SomA from the closely related cyanobacterial strain Synechococcus PCC 7942. Analyses performed on the sequences suggest that SomA and SomB form 14- or 16-stranded porin-like beta-barrels. Moreover, all sequences share an N-terminal motif with significant homology to 'S-layer homology' domains, which might form a periplasmic extension. SomA and SomB therefore may, in addition to their porin function, act as linkers connecting the outer membrane with the peptidoglycan layer.

Amino Acid Sequence↗

PubMed1993

Organization and sequences of genes for the subunits of ATP synthase in the thermophilic cyanobacterium Synechococcus 6716.

The sequences of the genes for the nine subunits of ATP synthase in the thermophilic cyanobacterium Synechococcus 6716 have been determined. The genes were identified by comparison of the encoded proteins with sequences of ATP synthase subunits in other species, and confirmed for subunits alpha, beta, delta and epsilon, by determining their N-terminal sequences. They are arranged at three separate loci. Six of them are in one cluster in the order a: c: b': b: delta: alpha, and those for the beta and epsilon subunits form a second and separate cluster. The gene for the gamma-subunit is at a third site. As in other bacteria, the gene for subunit a is immediately preceded by a gene coding for a small hydrophobic protein of unknown function, known as uncI in Escherichia coli. The gene orders in Synechococcus 6716 are related to the orders of ATP synthase genes in the plastid genomes of higher plants, and particularly of a red alga and a diatom. The sequences of the subunits are similar to those of chloroplast ATP synthase, the alpha, beta and c subunits being particularly well conserved. Differences in the primary structures of the Synechococcus 6716 and chloroplast gamma subunits probably underlie different mechanisms of activation of ATP synthase. The nucleotide sequences that are presented also contain 12 other open reading frames. One of them encodes a protein sequence related to the E. coli DNA repair enzyme, photolyase, and another codes for a protein that contains internal repeats related to sequences in the myosin heavy chain.

Amino Acid Sequence↗

PubMed1998

The ATP-dependent Clp protease is essential for acclimation to UV-B and low temperature in the cyanobacterium Synechococcus.

ClpP is the proteolytic subunit of the ATP-dependent Clp protease in eubacteria, mammals and plant chloroplasts. Cyanobacterial ClpP protein is encoded by a multigene family, producing up to four distinct isozymes. We have examined the importance of the first ClpP protein (ClpP1) isolated from the cyanobacterium Synechococcus sp. PCC 7942 for acclimation to ecologically relevant UV-B and low-temperature regimens. When the growth light of 50 mumol photons m-2 s-1 was supplemented with 0.5 W m-2 UV-B for 8 h, the constitutive level of ClpP1 rose eightfold after an initial lag of 1 h. Wild-type cells readily acclimated to this UV-B level, recovering after the initial stress to almost the same growth rate as that before UV-B exposure. Growth of a clpP1 null mutant (delta clpP1), however, was severely inhibited by UV-B, being eight times slower than the wild type after 8 h. In comparison, ClpP1 content increased 15-fold in wild-type cultures shifted from 37 degree C to 25 degree C for 24 h. Wild-type cultures readily acclimated to 25 degree C after 24 h, whereas the delta clpP1 strain did not and eventually lost viability with prolonged cold treatment. During acclimation to either UV-B or cold, photosynthesis in the wild type was initially inhibited upon the shift but then recovered. Photosynthesis in delta clpP1 cultures, however, was more severely inhibited by the stress treatment and failed to recover. Acclimation was also monitored by examining the exchange of photosystem II reaction centre D1 proteins that occurs in wild-type Synechococcus during conditions of excitation stress. During both cold and UV-B shifts, wild-type cultures replaced the acclimative form of D1 (D1:1) with the alternative D1 form 2 (D1:2) within the first hours. Once acclimated to either 25 degree C or 0.5 W m-2 UV-B, D1:2 was exchanged back for D1:1. In delta clpP1 cultures, this second exchange between D1 forms did not occur, with D1:2 remaining the predominant D1 form. Our results demonstrate that the ATP-dependent Clp protease is an essential component of the cold and UV-B acclimation processes of Synechococcus.

Acclimatization↗

PubMed1998

A genetically engineered increase in fatty acid unsaturation in Synechococcus sp. PCC 7942 allows exchange of D1 protein forms and sustenance of photosystem II activity at low temperature.

Photosystem II (PSII)-reaction-center protein D1 is encoded by three psbA genes in Synechococcus sp. PCC 7942. The psbAI gene encodes D1 form I (D1:1) and the psbAII and psbAIII genes encode the transiently expressed D1 form II (D1:2). We have studied the role of membrane-lipid unsaturation in the expression of psbA genes at low temperature, using a Synechococcus transformant with an increased unsaturation level of membrane lipids. Transfer of the cells from 32 degrees C to 25 degrees C under growth light resulted in the exchange of D1:1, the prevailing form, for D1:2 in the wild-type bacterium and the transformant, with no loss of PSII activity. Lowering the temperature further to 18 degrees C caused a drastic decrease in PSII activity in the wild-type bacterium, whereas the transformant was much less affected. Similar decreases in psbAI transcripts and loss of D1:1 occurred in both strains at 18 degrees C, with concomitant accumulation of psbAII/III transcripts, the latter event being especially prominent in the wild-type bacterium. However, the wild-type bacterium was incapable of accumulating D1:2 to compensate for the loss of D1:1, which resulted in disassembly of PSII at low temperature. These results imply translational rather than transcriptional regulation of psbA gene expression in Synechococcus 7942 at low temperature, and demonstrate the crucial role of the degree of membrane-lipid unsaturation in promotion of exchange of the D1 protein forms and thus the sustenance of PSII function at low temperature.

Chlorophyll↗

PubMed2004

Role of KaiC phosphorylation in the circadian clock system of Synechococcus elongatus PCC 7942.

In the cyanobacterium Synechococcus elongatus PCC 7942, KaiA, KaiB, and KaiC are essential proteins for the generation of a circadian rhythm. KaiC is proposed as a negative regulator of the circadian expression of all genes in the genome, and its phosphorylation is regulated positively by KaiA and negatively by KaiB and shows a circadian rhythm in vivo. To study the functions of KaiC phosphorylation in the circadian clock system, we identified two autophosphorylation sites, Ser-431 and Thr-432, by using mass spectrometry (MS). We generated Synechococcus mutants in which these residues were substituted for alanine by using site-directed mutagenesis. Phosphorylation of KaiC was reduced in the single mutants and was completely abolished in the double mutant, indicating that KaiC is also phosphorylated at these sites in vivo. These mutants lost circadian rhythm, indicating that phosphorylation at each of the two sites is essential for the control of the circadian oscillation. Although the nonphosphorylatable mutant KaiC was able to form a hexamer in vitro, it failed to form a clock protein complex with KaiA, KaiB, and SasA in the Synechococcus cells. When nonphosphorylatable KaiC was overexpressed, the kaiBC promoter activity was only transiently repressed. These results suggest that KaiC phosphorylation regulates its transcriptional repression activity by controlling its binding affinity for other clock proteins.

Bacterial Proteins↗

PubMed1996

An abundant cell-surface polypeptide is required for swimming by the nonflagellated marine cyanobacterium Synechococcus.

Certain marine unicellular cyanobacteria of the genus Synechococcus exhibit a unique and mysterious form of motility characterized by the ability to swim in liquid in the absence of flagella. An abundant cell-surface-associated polypeptide that is required for swimming motility by Synechococcus sp. strain WH8102 has been identified, and the gene encoding it, swmA, has been cloned and sequenced. The predicted SwmA protein contains a number of Ca2+-binding motifs as well as several potential N-glycosylation sites. Insertional inactivation of swmA in Synechococcus sp. strain WH8102 results in a loss of the ability to translocate, although the mutant strain, Swm-1, generates torque. This suggests that SwmA functions in the generation of thrust.

Amino Acid Sequence↗

PubMed1995

The DpsA protein of Synechococcus sp. Strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families.

The Dps family of proteins are a diverse group of bacterial stress-inducible polypeptides that bind DNA and likely confer resistance to peroxide damage during periods of oxidative stress and long term nutrient limitation. Some members of the Dps protein family have been shown to form large (approximately 150-kDa), hexameric complexes that bind chromosomal DNA with little sequence specificity. In this paper we report the nucleotide sequence of the dpsA gene from Synechococcus sp. PCC7942 encoding a cyanobacterial Dps homolog. The deduced amino acid sequence of the Synechococcus sp. DpsA protein revealed that a carboxyl-terminal domain of the protein was > 60% homologous to the COOH-terminal half of bacterioferritin. Other known Dps family members lack such high similarity to the bacterioferritins. Purification and spectroscopic analysis of the Synechococcus sp. DpsA protein complex revealed that the complex contains heme and has a weak catalase activity in vitro. Activity staining of nondenaturing polyacrylamide gels showed that the protein complex comigrated with both the heme and the catalase activity, and O2 evolution measurements yielded a maximal specific activity of 1.7 mumol of H2O2 consumed/micrograms of protein-1 min-1. We speculate that the protein may have a peroxide-consuming mechanism located on the chromosomal DNA, and we also suggest that this activity may be a necessary feature to handle the endogenous oxidative stresses associated with oxygenic photosynthesis. Last, the evolutionary link between the Dps protein family and the bacterioferritins is discussed.

Amino Acid Sequence↗

PubMed2001

Structural and regulatory properties of pyruvate kinase from the Cyanobacterium synechococcus PCC 6301.

Pyruvate kinase (PK) from the cyanobacterium Synechococcus PCC 6301 was purified 1,300-fold to electrophoretic homogeneity and a final specific activity of 222 micromol of pyruvate produced/min/mg of protein. The enzyme was shown to have a pI of 5.7 and to exist as a 280-kDa homotetramer composed of 66-kDa subunits. This PK appears to be immunologically related to Bacillus PK and a green algal chloroplast PK, but not to rabbit muscle PK, or vascular plant cytosolic and plastidic PKs. The N-terminal amino acid sequence of the Synechococcus PK exhibited maximal (67%) identity with the corresponding region of a putative PK-A sequence deduced from the genome of the cyanobacterium, Synechocystis PCC 6803. Synechococcus PK was relatively heat-labile and displayed a broad pH optimum around pH 7.0. Its activity was not influenced by K(+), but required high concentrations of Mg(2+), and was relatively nonspecific with respect to the nucleoside diphosphate substrate. Potent allosteric regulation by various effectors was observed (activators: hexose monophosphates, ribose 5-phosphate, glycerol 3-phosphate, and AMP; inhibitors: fructose 1,6-bisphosphate, inorganic phosphate, ATP, and several Krebs' cycle intermediates). The enzyme exhibited marked positive cooperativity for phosphoenolpyruvate, which was eliminated or reduced by the presence of the allosteric activators. The results are discussed in terms of the phylogeny and probable central role of PK in the control of cyanobacterial glycolysis.

Amino Acid Sequence↗

PubMed1998

Effects of ultraviolet-B radiation on phycobilisomes of Synechococcus PCC 7942: alterations in conformation and energy transfer characteristics.

Phycobilisomes (PBS), the major light harvesting antenna of the cyanobacterium Synechococcus contain phycocyanin (PC) and allophycocyanin (APC) as major pigment-protein complexes. PBS also absorb ultraviolet-B (280-320 nm) radiation. Exposure of Synechococcus PBS to low dose of UV-B (approximately 0.28 mw.cm-2) for 90 min induced change in absorption, emission and excitation characteristics of PBS and these changes got enhanced after 3 h of exposure. Room temperature excitation and emission spectra clearly indicated uncoupling of energy transfer from PC to APC on exposure to UV-B. Also, the 77K emission spectra suggested that F682 emission originating from APC decreased by 42% after 3 h of exposure. Circular dichroism (CD) spectra of UV-B exposed PBS indicated changes (14% decrease) in the alpha-helical content after 90 min treatment. SDS-PAGE analysis indicated degradation of a 75 kDa polypeptide (which appear to be a linker polypeptide) on UV-B treatment. The degradation of this polypeptide seems to induce changes in pigment-protein interaction and decoupling of energy transfer within the PBS. Our results for the first time clearly indicate that the PBS of Synechococcus are targets for UV-B damage.

Bacterial Proteins↗

PubMed1994

A novel expression vector for the cyanobacterium, Synechococcus PCC 6301.

A cyanobacterial expression vector was constructed using ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) promoter and terminator sequences derived from Synechococcus PCC 6301. recombinant plasmid, designated pARUB19, has an ampicillin-resistant (ApR) gene as a selectable marker and four unique restriction sites to allow the insertion of foreign genes. Using this vector, the luciferase gene from the firefly, Photinus pyralis, was introduced into Synechococcus PCC 6301 cells. The luciferase expression vector could be maintained stably in the host cells. Light production of luciferin/luciferase was detected in the transformants. Luciferase amounted to 1.2% of the total soluble protein. This plasmid may facilitate higher levels of foreign gene expression in Synechococcus PCC 6301.

Bacterial Proteins↗

PubMed1998

Promoters of the phycocyanin gene clusters of the cyanobacterium Synechococcus sp. strain PCC 7942.

The cyanobacterium Synechococcus sp. strain PCC 7942 has duplicated phycocyanin subunit gene clusters cpcB1A1 and cpcB2A2, which are identical to each other and to those of Synechococcus sp. strain PCC 6301 (Anacystis nidulans). Nucleotide sequences of the 428 and 286 bases of the 5' non-coding regions of the cpcB1A1 and cpcB2A2 clusters, respectively, of strain PCC 7942 were identical to those of strain PCC 6301. As in strain PCC 6301, cpcB1A1 yielded two major transcripts of 1.4 and 1.3 kb and cpcB2A2 yielded a single transcript of 1.3 kb in strain PCC 7942. Thus, the structure and expression of cpcBA gene clusters in the two strains are essentially the same. Using bacterial luciferase encoded by luxAB as a reporter, cpcB1A1 was shown to have two promoters corresponding to the two major transcripts. Luminescence from the Synechococcus reporter strains carrying the fusions of the cpcBA promoters to luxAB showed circadian oscillation. Similar to the promoter of psbA1 encoding the D1 protein of PSII, the two cpcB1A1 promoters and the cpcB2A2 promoter showed the peak of activity at the end of the subjective day and the trough at the end of the subjective night.

Base Sequence↗

PubMed2003

Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942.

We isolated and characterized a gene encoding phosphoribulokinase (PRK) from Synechococcus sp. PCC 7942. The isolated sequence consisted of a 999 bp open reading frame encoding 333 amino acid residues of PRK. The PRK contained a pair of cysteinyl residues corresponding to Cys16 and Cys55 of spinach PRK regulated by a ferredoxin-thioredoxin system. However, there were seventeen amino acid residues lacking between the two cysteinyl residues compared with those of the chloroplastic enzyme in higher plants. The recombinant PRK of Synechococcus sp. PCC 7942 accounted for about 6-13% of the total soluble protein in the Escherichia coli. The specific activity of the enzyme was 230 micro mol min(-1) (mg protein)(-1). The enzyme activity was completely inactivated by treatment with 5,5'-dithiobis (2-nitrobenzoic acid) (cysteinyl residue-specific oxidant) or was decreased by treatment with H(2)O(2), but was more tolerant to oxidation than that of chloroplast. The oxidized PRK was fully activated by treatment with excessive dithiothreitol. Furthermore, incubation with 3 mM ATP protected the oxidation of the enzyme by either 5,5'-dithiobis (2-nitrobenzoic acid) or H(2)O(2). These results suggest Synechococcus sp. PCC 7942 PRK can be regulated by reversible oxidation/reduction in vitro, but might be resistant to oxidative inactivation in vivo.

Amino Acid Sequence↗

PubMed1992

Amplification and rearrangement of a prokaryotic metallothionein locus smt in Synechococcus PCC 6301 selected for tolerance to cadmium.

Metal-tolerant cyanobacteria have been isolated from metal-polluted aquatic environments and also selected in culture, but no genes which confer metal tolerance have been described. To investigate the possibility that amplification of a prokaryotic metallothionein gene (smtA), or rearrangement of the smt locus, could be involved in the development of Cd tolerance in Synechococcus PCC 6301, Cd-tolerant lines were selected by stepwise adaptation of a Synechococcus culture. An increase in smtA gene copy number and the appearance of unique additional smtA restriction fragments (both larger and smaller) were detected in these tolerant lines (tolerant to 0.8 microM Cd, 1.3 microM Cd and 1.7 microM Cd). Stepwise adaptation was repeated by using a culture of Synechococcus PCC 6301 inoculated from a single plated colony to obtain four new lines (tolerant to 1.4 microM Cd, 1.8 microM Cd, 2.6 microM Cd and 3.2 microM Cd). Amplification of the smtA gene and development of unique smtA restriction fragments (larger and smaller) were once again detected in these tolerant lines. Amplification and rearrangement of the smt locus were only detected in the seven Cd-tolerant lines, with no evidence of amplification or rearrangement in the non-tolerant lines from which they were derived. As a control, another gene, psaE, was also monitored in these cell lines. There was no evidence of amplification or rearrangement of psaE in the non-tolerant or any of the Cd-tolerant lines.

Base Sequence↗

PubMed1997

The gshB gene in the cyanobacterium Synechococcus sp. PCC 7942 encodes a functional glutathione synthetase.

The gene homologous to glutathione synthetase of Escherichia coli was inactivated in the cyanobacterium Synechococcus sp. PCC 7942. The region of genomic DNA including the mutation site was isolated from the mutant by plasmid rescue and the native gene of the wild-type was cloned from a genomic DNA library of the wild-type using the flanking DNA as a probe. The wild-type gene, designated gshB, encodes a polypeptide of 323 amino acids with a molecular mass of 35 kDa. The deduced amino acid sequence resembles glutathione synthetases of bacteria, but not those of higher organisms. When gshB was overexpressed in E. coli, glutathione synthetase activity was increased markedly in the E. coli extract. In addition, the Synechococcus sp. PCC 7942 gshB mutants had lost their ability to synthesize glutathione. These findings demonstrate that the gshB gene of Synechococcus sp. PCC 7942 is a structural gene for glutathione synthetase and is involved in the biosynthesis of glutathione.

Amino Acid Sequence↗

PubMed2002

The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus.

In the cyanobacterium Synechococcus sp. strain PCC 7942 a multigene family of three different isozymes encodes the proteolytic subunit ClpP of the ATP-dependent Clp protease. In contrast to the monocistronic clpPI gene, clpPII and clpPIII are part of two bicistronic operons with clpX and clpR, respectively. Unlike most bacterial Clp proteins, the Synechococcus ClpP2, ClpP3, ClpR and ClpX proteins were not highly inducible by high temperatures, or by other stresses such as cold, high light or oxidation, although slower gradual rises occurred for all four proteins during high light, and for ClpP3, ClpR and ClpX at low temperature. Attempts to inactivate the clpPII, clpIII, clpR or clpX genes were only successful for clpPII, suggesting the others are essential for Synechococcus cell viability. The DeltaclpPII mutant exhibited no significant phenotypic changes from the wild-type, including no change in ClpX content. Despite the apparent bicistronic arrangement of both clpPII-clpX and clpR-clpPIII, all four genes primarily produce monocistronic transcripts, although polycistronic transcripts were detected. Mapping of 5' ends for the clpX and clpPIII monocistronic transcripts revealed promoters situated within the 3' region of clpPII and clpR, respectively. Transcriptional and translational studies further showed differences in the expression and regulation between the clpP-clpR-clpX genes. Inactivation of clpPI caused a significant decrease in ClpP2 protein concomitant to small increases in both ClpP3 and ClpR. Inactivation of clpPII resulted in a large rise in clpPI transcripts but to a lesser extent in ClpP1 protein. Similar small increases in ClpP3, ClpR and ClpX proteins also occurred in DeltaclpPII. These results highlight the regulatory complexity of these multiple clp genes and their functional importance in cyanobacteria.

ATPases Associated with Diverse Cellular Activitie↗