Biliproteins of cyanobacteria and Rhodophyta: Homologous family of photosynthetic accessory pigments

Glazer, Alexander N.; Apell, Gerald; Hixson, Craig S.; Bryant, Donald A.; Rimon, Sara; Brown, Douglas M.

doi:10.1073/pnas.73.2.428

Cited by 80 publications

(30 citation statements)

References 24 publications

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“…fall into two pigment groups; those with a PE containing both phycoerythrobilin and phycourobilin chromophores (type 1) and those composed of only phycoerythrobilin chromophores (type 2). The type 1 pigment seems to be related to the red algal phycoerythrins and the type 2 shows a close spectral resemblance to C-phycoerythrin (Gantt 198 1;Kursar et al 198 1;Glazer et al 1982;Alberte et al 1984;Ong et al 1984). More than 26 clonal isolates of PE-containing marine Synechococcus spp.…”

Section: Limnolmentioning

confidence: 99%

Discrimination between types of pigments in marine Synechococcus spp. by scanning spectroscopy, epifluorescence microscopy, and flow cytometry1

Wood

Horan²,

Muirhead³

et al. 1985

Limnology & Oceanography

139

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The in vivo spectral properties of nine clonal isolates of marine Synechococcus spp. were compared to identify characteristics associated with intact cells from each of three major pigment groups. In vivo absorption and fluorescence excitation and emission spectra could differentiate between phycoerythrin (PE)‐lacking clones, clones containing a PE composed of phycoerythrobilin and phycourobilin chromophores, and clones containing a PE composed of only phycoerythrobilin chromophores. These differences can be detected analytically by both epifluorescence microscopy and flow cytometry and were observed in clones grown in different environments and at different stages of growth and nutrient limitation. These spectral characters thus reflect intrinsic differences between the three pigment groups and can be used to identify genetically distinct subpopulations of marine Synechococcus spp. in natural waters.

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Section: Limnolmentioning

confidence: 99%

Discrimination between types of pigments in marine Synechococcus spp. by scanning spectroscopy, epifluorescence microscopy, and flow cytometry1

Wood

Horan²,

Muirhead³

et al. 1985

Limnology & Oceanography

139

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“…The red algal phycobiliproteins share antigenic properties and amino sequences with those ofthe cyanobacteria (1,11,17) and, to a lesser extent, with the Cryptomonads (1,6). The blue-colored biliproteins, APC' and PC, are found in all cyanobacteria and red algae.…”

mentioning

confidence: 99%

Light-Harvesting System of the Red Alga Gracilaria tikvahiae

Kursar¹,

Meer²,

Alberte³

1983

Plant Physiol.

146

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ABSTRACIWild type Gracilaria tik'ahiae, a macrophytic red alga, and fourteen genetically characterized pigment mutants were analyzed for their biliprotein and chlorophyll contents. The same three biliproteins, phycoerythrin, phycocyanin, and allophycocyanin, which are found in the wild type are found in all the Mendelian and non-Mendelian mutants examined. Some mutants overproduce R-phycoerythrin while others possess only traces of phycobiliprotein; however, no phycoerythrin minus mutants were found. Two of the mutants are unique; one overproduces phycocyanin relative to allophycocyanin while the nuclear mutant obr synthesizes a phycoerythrin which is spectroscopically distinct from the R-phycoerythrin of the wild type. The phycoerythrin of obr lacks the typical absorption peak at 545 nanometers characteristic of R-phycoerythrin and possesses a phycoerythrobilin to phycourobilin chromophore ratio of 2.6 in contrast to a ratio of 4.2 found in the wild type. Such a lesion provides evidence for the role of nuclear genes in phycoerythrin synthesis. In addition, comparisons are made of the pigment compositions of the Gracilaria strains with those of Neoagardhiella bailyei, a macrophytic red alga which has a high phycoerythrin content, and Anacystis nidulans, a cyanobacterium which lacks phycoerythrin. The mutants described here should prove useful in the study of the genetic control of phycobiliprotein synthesis and phycobilisome structure and assembly.The functional photosynthetic unit of 02-evolving plants is composed of large arrays of light-harvesting pigment-proteins which are associated with the reaction centers and electron transport chains of PSI and PSII. While the reaction centers, electron transport chains, and dark reactions of photosynthesis are probably very similar in the major plant groups, the lightharvesting systems are quite diverse. For example, the antennae pigments fucoxanthin and Chl c are found in the photosynthetic unit of the diatoms and brown algae. In the red algae, Cryptomonads, and cyanobacteria, the phycobiliproteins serve this function while Chl b functions in the green plants (22). These pigments along with the proteins which bind them are major '

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“…However, as genetic studies have not been carried out with P. cruentum, little is known about the primary structure of the different phycobiliproteins present in this red alga. Apart from the amino acid sequence of B-phycoerythrin published by Sidler et al (1989a), only short amino-terminal sequences have been reported (Glazer et al, 1976;Bryant et al, 1978).…”

mentioning

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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Biliproteins of cyanobacteria and Rhodophyta: Homologous family of photosynthetic accessory pigments

Cited by 80 publications

References 24 publications

Discrimination between types of pigments in marine Synechococcus spp. by scanning spectroscopy, epifluorescence microscopy, and flow cytometry1

Discrimination between types of pigments in marine Synechococcus spp. by scanning spectroscopy, epifluorescence microscopy, and flow cytometry1

Light-Harvesting System of the Red Alga Gracilaria tikvahiae

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

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