Molecular cloning and nucleotide sequence of the alpha and beta subunits of allophycocyanin from the cyanelle genome of Cyanophora paradoxa.

Bryant, Donald A.; Lorimier, Robert de; Lambert, D. H.; Dubbs, James M.; Stirewalt, Veronica L.; Stevens, S. E.; Porter, Ronald D.; Tam, Johnny; Jay, Ernest

doi:10.1073/pnas.82.10.3242

Cited by 78 publications

(25 citation statements)

References 43 publications

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“…3A. For comparison, the analogous amino acid sequences from a eukaryotic alga, C. paradoxa (16,19) are shown. The intergenic region is 69 base pairs (bp) with stop codons present in two of the three reading frames.…”

Section: Identification and Characterization Of X-embl3 Genomicmentioning

confidence: 99%

“…Each phycobiliprotein is composed of two related subunits, a and ,B, to which one or more tetrapyrole chromophores are attached (4), conferring upon each phycobiliprotein a characteristic light-absorption and emission spectrum. Amino acid (6)(7)(8)(9)(10)(11)(12)(13) and DNA (14)(15)(16) sequence data show considerable sequence conservation among the various phycobiliproteins (APC, PC, and phycoerythrin) as well as between the a and P3 subunits of a given phycobiliprotein. These findings suggest that phycobiliprotein genes arose via duplications of an ancestral sequence (8).…”

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confidence: 99%

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Genes encoding major light-harvesting polypeptides are clustered on the genome of the cyanobacterium Fremyella diplosiphon.

Conley¹,

Lemaux²,

Lomax³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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The polypeptide composition of the phycobilisome, the major light-harvesting complex of prokaryotic cyanobacteria and certain eukaryotic algae, can be modulated by different light qualities in cyanobacteria exhibiting chromatic adaptation. We have identified genomic fragments encoding a cluster of phycobilisome polypeptides (phycobiliproteins) from the chromatically adapting cyanobacterium Fremyella diplosiphon using previously characterized DNA fragments of phycobiliprotein genes from the eukaryotic alga Cyanophora paradoxa and from F. diplosiphon. Characterization of two A-EMBL3 clones containing overlapping genomic fragments indicates that three sets of phycobiliprotein genesthe a-and j3-allophycocyanin genes plus two sets of a-and j3-phycocyanin genes-are clustered within 13 kilobases on the cyanobacterial genome and transcribed off the same strand. The gene order (a-allophycocyanin followed by (3-allophycocyanin and ,B-phycocyanin followed by a-phycocyanin) appears to be a conserved arrangement found previously in a eukaryotic alga and another cyanobacterium. We have reported that one set of phycocyanin genes is transcribed as two abundant red light-induced mRNAs (1600 and 3800 bases). We now present data showing that the allophycocyanin genes and a second set of phycocyanin genes are transcribed into major mRNAs of 1400 and 1600 bases, respectively. These transcripts are present in RNA isolated from cultures grown in red and green light, although lower levels of the 1600-base phycocyanin transcript are present in cells grown in green light. Furthermore, a larger transcript of 1750 bases hybridizes to the allophycocyanin genes and may be a precursor to the 1400-base species.In prokaryotic cyanobacteria and eukaryotic red algae, phycobilisomes are macromolecular complexes that harvest light energy and transfer this energy to the photosynthetic reaction centers (1). They can provide 30-50o of the lightharvesting capacity of the cells and can comprise 60% of the total soluble protein (2). Although functionally analogous to light-harvesting chlorophyll-protein complexes in higher plants, the phycobilisome is water soluble and only peripherally associated with photosynthetic membranes. The complex is composed of chromophoric and nonchromophoric polypeptides arranged into two domains: a central core anchored to the photosynthetic membranes and rods that radiate from the core (3, 4). There are three major chromophoric proteins (phycobiliproteins) in the phycobilisomeallophycocyanin (APC), phycocyanin (PC), and phycoerythrin-as well as nonchromophoric linker polypeptides that maintain the structure and allow efficient energy transfer among the components of the complex (5). Each phycobiliprotein is composed of two related subunits, a and ,B, to which one or more tetrapyrole chromophores are attached (4), conferring upon each phycobiliprotein a characteristic light-absorption and emission spectrum. Amino acid (6-13) and DNA (14-16) sequence data show considerable sequence conservation among the various phyco...

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Section: Identification and Characterization Of X-embl3 Genomicmentioning

confidence: 99%

mentioning

confidence: 99%

Genes encoding major light-harvesting polypeptides are clustered on the genome of the cyanobacterium Fremyella diplosiphon.

Conley¹,

Lemaux²,

Lomax³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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“…, Pilot and Fox (1984) Walsh et al (1980) Lau et al (1987a), Kalla et al (1988) Wilson et al (1991) Anderson and Grossman (1990) Apt and Grossman (1993b) Minami et al (1985) Offner and Pilot and Fox (1984), Glazer (1987) Freidenreich et al (1978), Williams and Glazer (1978), Glazer (1987) Lau et al (1987b), Kalla et al (1988) Wilson et al (1991 Anderson and Grossman (1990) Sidler et al (1990) Apt and Grossman (1993b) Minami et al (1985) Offner and Troxler (1983) Bryant et al (1985) Sidler et al (1981, Riimbeli et al (1987) Houmard et al (1986, Klotz et al (1986) Su et al (1992 Some cyanobacteria are found under several names depending on the publications and the data banks. For clarity, only the most common used strain designations (from the point of view of the authors) have been used for the table above.…”

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confidence: 99%

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

Ducret¹,

Sidler²,

Frank³

et al. 1994

European Journal of Biochemistry

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We present here the complete primary structure of R-phycocyanin-I a and p subunits from the red alga Porphyridium cruentum. The a chain is composed of 162 amino acid residues (18049Da, calculated from sequence, including chromophore) and carries a phycocyanobilin pigment covalently linked to Cys84. The p chain contains 172 amino acids (19344Da, calculated from sequence, including chromophores) and carries a phycocyanobilin pigment covalently linked at Cys82 and a phycoerythrobilin pigment at Cys153. A y-N-methyl asparagine residue was also characterised at position ,872 similar to other phycobiliprotein , 6 subunits. R-phycocyanin-I from Porphyridium cruentum shares high sequence identity with C-phycocyanins (69 -83%), R-phycocyanins (66-70%) and in a less extent with phycoerythrocyanins (57-65%) from various sources.The presented phylogenetic trees are based on a comparison of all phycobiliprotein amino acid sequences known so far and confirm the clear affiliation of the R-phycocyanins in the phycocyanin family. In spite of their particular phycobilin pattern, they do not represent intermediate forms between the phycocyanin and the phycoerythrin family. Phycoerythrocyanin, a phycocyanin-related phycobiliprotein adapted to green light harvesting, is also shown to belong to the phycocyanin family. However, the phycoerythrocyanins diverge from phycocyanins in their different function and it is suggested that they should be assigned to a separate group within the phycocyanin family.Phycobilisomes represent the main accessory light-harvesting antenna of cyanobacteria and red algae (Cohen-Bazire and Bryant, 1982;Zuber, 1983Glazer, 1984Glazer, , 1985Gantt, 1988;Bryant, 1991; Sidler, 1994). Their major components, the phycobiliproteins, are constituted of a and p subunits (16-18 kDa and 18-20 kDa respectively) carrying one, two or three open-chain tetrapyrroles (bilins) per subunit as prosthetic groups. Both subunits are aggregated in vivo to heterotrimers (an3 or hexamers (anb. Electron microscopy and crystal structure analysis show that the trimer complex is the basic building block of the phycobilisome (Schirmer et al., 1985). The ap monomer aggregates in a disc-shaped complex with a diameter of 11 nm and a length of 3 nm. A hexamer is built up of two trimers stacked face-to-face (Schirmer et al., 1986). The formation of higher aggregatesCorrespondence to H.

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“…DNA ligations, plasmid transformations, nick translations, and Southern (43) and plaque hybridizations were done by using standard procedures (27). All hybridizations included at least a 6-h prehybridization in 6x SET (lx SET is 150 mM NaCl, 30 (4,9).…”

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confidence: 99%

Molecular cloning and characterization of the recA gene from the cyanobacterium Synechococcus sp. strain PCC 7002

Murphy¹,

Bryant²,

Porter³

et al. 1987

J Bacteriol

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The recA gene of Synechococcus sp. strain PCC 7002 was detected and cloned from a lambda gtwes genomic library by heterologous hybridization by using a gene-internal fragment of the Escherichia coli recA gene as the probe. The gene encodes a 38-kilodalton polypeptide which is antigenically related to the RecA protein of E. coli. The nucleotide sequence of a portion of the gene was determined. The translation of this region was 55% homologous to the E. coli protein; allowances for conservative amino acid replacements yield a homology value of about 74%. The cyanobacterial recA gene product was proficient in restoring homologous recombination and partial resistance to UV irradiation to recA mutants of E. coli. Heterologous hybridization experiments, in which the Synechococcus sp. strain PCC 7002 recA gene was used as the probe, indicate that a homologous gene is probably present in all cyanobacterial strains.

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Molecular cloning and nucleotide sequence of the alpha and beta subunits of allophycocyanin from the cyanelle genome of Cyanophora paradoxa.

Cited by 78 publications

References 43 publications

Genes encoding major light-harvesting polypeptides are clustered on the genome of the cyanobacterium Fremyella diplosiphon.

Genes encoding major light-harvesting polypeptides are clustered on the genome of the cyanobacterium Fremyella diplosiphon.

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

Molecular cloning and characterization of the recA gene from the cyanobacterium Synechococcus sp. strain PCC 7002

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