The Complete Amino Acid Sequence of Both Subunits of C-Phycocyanin from the Cyanobacterium<i>Mastigocladus laminosus</i>

Frank, Gerhard; Sidler, Walter; Widmer, Herbert; Zuber, Herbert

doi:10.1515/bchm2.1978.359.2.1491

Cited by 130 publications

(17 citation statements)

References 13 publications

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“…a-C-PE a-C-PE a-B-PE a-B-PE a-C-PE a-B-PE a-PE-I1 a-PE a-PEC a-PEC a-R-PC-I a-R-PC-I1 a-C-PC-I a-C-PC-I1 a-C-PC-111 a-C-PC a-C-PC Anderson andGrossman (1990) Fiiglistaller et al (1983), Eberlein and Kufer (1990) Swanson et al (1992) this work, submitted to data banks (1994) De Lorimier et al (1993, Conley et al (1988) Capuano et al (1988), Conley et al (1988, Mazel and Marliere (1989) Belknap andHaselkorn (1987) Offner et al (1981) Frank et al (1978), Kufer, W., Hoenger, A., Eberlein, M., Mayer, K.,…”

Section: Supplementmentioning

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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Section: Supplementmentioning

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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“…A number of PBP structures have been determined for proteins isolated from thermophiles-organisms that thrive at up to 65°C. 9,10 It has been previously shown that the ability to resist thermal denaturation is a property inherent to PBPs [30][31][32][33][34][35][36] and thus must be explained by various changes to the protein sequence, which are then translated into subtle changes in the tertiary/ quaternary structures. Many of these studies did not have the advantage of the wealth of structural information now available; 10 however, overall values of thermodynamic parameters could be estimated and comparisons made between thermophilic and mesophilic species.…”

Section: Introductionmentioning

confidence: 99%

Allophycocyanin Trimer Stability and Functionality Are Primarily Due to Polar Enhanced Hydrophobicity of the Phycocyanobilin Binding Pocket

McGregor

Klartag

David

et al. 2008

Journal of Molecular Biology

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“…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%

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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The Complete Amino Acid Sequence of Both Subunits of C-Phycocyanin from the CyanobacteriumMastigocladus laminosus

Cited by 130 publications

References 13 publications

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

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

Allophycocyanin Trimer Stability and Functionality Are Primarily Due to Polar Enhanced Hydrophobicity of the Phycocyanobilin Binding Pocket

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

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