Phycocyanin 612: a biochemical and photophysical study

MacColl, Robert; Guard-Friar, Deborah

doi:10.1021/bi00293a018

Cited by 30 publications

(21 citation statements)

References 23 publications

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“…Four different phycobiliprotein families have been differentiated on the base of immunological studies (Berns, 1967 ;MacColl and Guard-Friar, 1987;Zilinskas and Howell, 1987) : the phycoerythrins, which are mainly localised peripherally in the rod structures, the phycocyanins, typically present at the core-proximal periphery, the allophycocyanins, only detected in the phycobilisome core and the core-membrane linkers, a polyvalent protein which primarily organises the phycobilisome and anchors it to the photosystern 11. A comparison of the 15 phycocyanin amino acid sequences characterised so far illustrates the features common to this family:…”

Section: The Phycocyanin Familymentioning

confidence: 99%

“…Conversely, it will fail to react with representatives of the phycoerythrin and allophycocyanin families (MacColl and Guard-Friar, 1987). Thus phycocyanin-645, isolated from the cryptomonad Chroomonas sp., was shown to belong to the phycoerythrin rather than to the phycocyanin family, as a subunits Fig.…”

Section: The Phycocyanin Familymentioning

confidence: 99%

“…strain WH8501, carries two phycocyanobilins and one phycourobilin which drastically blue-shifts the absorption spectrum of this phycobiliprotein (Swanson et al, 1991). These new data have raised the question of whether the R-phycocyanins are related phylogenetically to the phycocyanin family (to whom they belong if one considers their immunological properties, MacColl and Guard-Friar, 1987) in spite of their unusual bilin content, or whether they constitute a new sub-family that would represent an intermediate form between phycocyanins and phycoerythrins (Glazer and Hixson, 1975). The availability of the amino acid sequences of numerous phycobiliproteins from various rhodophytan algae and cyanobacteria gives us now the opportunity to compare the primary structures of R-and C-phycocyanins in relation to all other phycobiliproteins and to determine whether some relationships may be found between primary structure, functions and spectral properties.…”

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confidence: 99%

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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: The Phycocyanin Familymentioning

confidence: 99%

Section: The Phycocyanin Familymentioning

confidence: 99%

mentioning

confidence: 99%

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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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“…Its immunochemistry is thus clearly distinctive from C-phycocyanin and R-phycocyanin to which it has some spectral resemblance. In addition to these immunochemical studies on phycocyanin 612, recently its biochemical and spectroscopic properties were evaluated (14,17). Its chromophore content is unique and differs from that of C-phycocyanin in that its ,B subunit has a cryptoviolin chromophore in addition to the usual two phycocyanobilins.…”

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confidence: 99%

“…Its a subunit, however, has the same chromophore content as C-phycocyanin but differs from that found for cryptomonad phycocyanin 645 (15,18). A common feature in the chromophore contents of cryptomonad biliproteins is that cryptoviolin is always present ( 14,(17)(18)(19).…”

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confidence: 99%

Immunochemistry on Cryptomonad Biliproteins

Guard-Friar¹,

Eisenberg²,

Edwards³

et al. 1986

Plant Physiol.

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ABSTRACIA survey is made of the immunochemical behavior of four of the six known types of cryptomonad biliproteins: phycocyanins 612 and 645 and phycoerythrins 545 and 566. They were compared both among themselves and to selected biliproteins isolated from blue-green and red algae. All the cryptomonad biliproteins were shown to be closely related to each other by Ouchterlony double diffusion technics. An antigenic relationship among all the cryptomonad biliproteins and B-phycoerythrin (red alp) and C-phycoerythrin (blue-green alga) was established. Only a very marginal cross-reactivity was found between C-phycocyanin (blue-green algae) and the cryptomonad biliproteins. These results suggest a common ancestor for the photosynthetic units of all three biliprotein-containing phyla.Biliproteins are light harvesting and excitation energy transfer chromoproteins that function as accessory pigments for PSII in the photosynthesis of blue-green (cyanobacterial), red, and cryptomonad algae. Cryptomonad biliproteins are unusual in that they apparently do not form phycobilisomes and in the cryptomonads no analog of allophycocyanin has yet been detected. There are six biliproteins in the cryptomonads, phycocyanins 612, 630, 645, and phycoerythrins 545, 555, 566, with only one type usually found in each alga.Immunochemical studies on biliproteins have greatly emphasized blue-green and red algal examples. By 1967 four publications had established in a very extensive and decisive manner three basic rules governing the immunochemical behavior of these two types of algal biliproteins (1-3, 29). These three generalizations are: all phycocyanins from both blue-green (procaryotes) or red (eucaryotes) algae are immunochemically very similar; all phycoerythrins of all spectral types (C-, R-, B-) are immunochemically closely related whether they are from bluegreen or red algae; no phycocyanin is related immunochemically to any phycoerythrin. This last rule holds even when the phycocyanin and phycoerythrin are isolated from the same alga. These first two results were most important because of the great differences in structure between procaryotic blue-green algae and eucaryotic red algae. The immunochemical results then established the principle that, although major cellular changes have occurred in the evolution from procaryotes to eucaryotes, the individual proteins could remain virtually unaltered. Subsequent research has shown that the two subunits of phycoerythrin are immunochemically related (27) Research on the immunochemistry of cryptomonad biliproteins, has been much less extensive and then usually only a fragment of a larger study. It is therefore not too surprising that unlike the comparison of blue-green and red algal biliproteins, cryptomonad results have been so far perhaps inconclusive and controversial (2,4,12,13,16,26,29). We, therefore, undertook an immunochemical investigation using Ouchterlony doublediffusion and four different cryptomonad biliproteins. Two different phycoerythrins and two different phycocyanins ...

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Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives

1998

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Phycoerythrin 545 from the cryptomonad alga, Rhodomonas lens, has been crystallized under a wide variety of conditions. Although this type of photosynthetic light-harvesting protein is water soluble, detergents were always required for crystallization. The crystals were typically poorly ordered, or ordered in only two dimensions. However, crystals that were well-ordered in three dimensions could be obtained under two different conditions. Both used polyethylene glycol as precipitant and the detergent lauryldimethylaminoxide, but the additives that were critical for obtaining well-ordered crystals were propionamide in one case and Csf/Br-in the other. Crystals obtained in the presence of propionamide have the space group P212121, with cell constants of a = 85.6 A, b = 108.2 A, and c = 131.0 A, and contain two dimers [i.e., 2 X (a2p2)] in the asymmetric unit. They show diffraction to at least 3.0 8, resolution. The crystals grown with Csf/Br-are nearly isomorphous. Both types of crystals show intense, strongly polarized fluorescence, suggesting that energy transfer in the crystals is highly efficient. This should provide a basis for quantitative investigation of the role of exciton interactions in energy transfer in cryptomonad phycobiliproteins. Keywords:Cryptophyceae; detergent; light-harvesting protein; photosynthesis; phycobiliprotein; propionamide; protein crystal; X-ray diffraction Photosynthetic light-harvesting proteins contain pigments that absorb photons and transfer excited-state energy to photosynthetic reaction centers, where the captured energy initiates an excited-state oxidation reaction of a specialized set of pigments that leads to charge separation across the photosynthetic membrane. In most organisms, light harvesting is performed mainly by chlorophyll-containing membrane proteins. However, cyanobacteria, red algae, and cryptomonad algae possess additional light-harvesting proteins, called phycobiliproteins, which are water-soluble and contain covalently bound open-chain tetrapyroles as pigments (MacColl & Guard-Friar, 1987;Glazer, 1989 bis-Tris, bis-(2-hydroxyethyl)imino-tris-(hydroxymethyl)me~ane; DEAEAbbreviations: Am, absorption maximum; P-ME, P-mercaptoethanol; cellulose, diethylaminoethyl-cellulose; EDTA, ethylenediaminitetraacetic acid; HEPES, N-(2-hydroxyethyl)-piperazine-N'-(2-ethane-sulfonic acid); IEF, isoelectric focusing; LDAO, lauryldimethylaminoxide; PC645, phycocyanin 645; PE545, phycoerythrin 545; PEG, polyethylene glycol; UDAO, undecyldimethylaminoxide; V,, Matthews parameter.The phycobiliproteins of the cyanobacteria and the red algae have been well characterized. There are four main types: phycoerythrin (Amm -550 nm), phycoerythrocyanin (Amm = 575 nm), phycocyanin (A,,, = 620 nm), and allophycocyanin (Am,, = 650 nm). They are all similar in that their monomeric units consist of two subunits, called a and p, which are highly homologous to each other, and which are highly homologous between different types of proteins. Each subunit has a molecular weight of about 16-20...

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Phycocyanin 612: a biochemical and photophysical study

Cited by 30 publications

References 23 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

Immunochemistry on Cryptomonad Biliproteins

Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives

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