Characterization of cryptomonad phycoerythrin and phycocyanin

MacColl, Robert; Berns, Donald S.; Gibbons, Olga

doi:10.1016/0003-9861(76)90436-7

Cited by 74 publications

(46 citation statements)

References 37 publications

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“…Phycobiliproteins in the pigment mixture were identified by their fluorescence excitation and emission spectra characteristics by comparison with published spectra for cryptomonads and cyanobacteria (MacColl et al 1976, Gantt 1979, Kursar & Alberte 1983, Alberte et al 1984, Stewart & Farmer 1984, Haxo et al 1987. Spectra were measured in a Perkin Elmer Fluorescence Spectrophotometer Model MFP-44A.…”

Section: Methodsmentioning

confidence: 99%

Adaptation of Synechococcus in situ determined by variability in intracellular phycoerythrin-543 at a coastal station off the Southern California coast, USA

Vernet¹,

Mitchell²,

Holm‐Hansen³

1990

Mar. Ecol. Prog. Ser.

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Concentrations of extracted phycobiliproteins were measured a t a station off the Southern California coast, USA, from November 1985 to March 1986. The main pigment found was phycoerythrin-543 (PE) from Synechococcus spp. as described by Alberte et al. (1984). Concentrations of PE in water column, between 3 and 40 m, varied between 0.01 and 1 60 pg 1-' Maximum values were found between 3 and 22 m. In situ concentrations of PE were posit~vely correlated with cell numbers of Synechococcusspp., which ranged from 1.4 to 116 X 106 cells I-', and showed maximal values between 3 and 13 m. Because no other types of PE were detected, all PE measured was considered to come from Synechococcus-type cells. Cellular concentrations of PE varied between 2.1 and 40.3 X 10-' pg PE cell-', with an average value of 10 5?4.1 X IO-' vg PE cell-' above the 1 % isolume for PAR (Photosynthetically Available Radiation). Pigment per cell increased consistently with depth dunng autumn and spring and had low and relatively constant values in the winter. High PE:cell (>20 X lO-' pg PE cell-') was observed only below the 1 % isolume for PAR. For all samples, cellular concentration of PE was inversely correlated with incident PAR and was positively correlated to dissolved inorganic nitrogen (nitrate) concentration. Cyanobactena were not a dominant component of phytoplankton standing stock during this study, contributing an estimated 4 to 15 O/O of total chlorophyll in the water column, but had high specific growth rates, with maximal values of >0.75 d-' close to the surface. Absorption of light at 540 nm, as measured by in vivo absorption spectra of phytoplankton, was not correlated with PE concentration in the water column.

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Section: Methodsmentioning

confidence: 99%

Adaptation of Synechococcus in situ determined by variability in intracellular phycoerythrin-543 at a coastal station off the Southern California coast, USA

Vernet¹,

Mitchell²,

Holm‐Hansen³

1990

Mar. Ecol. Prog. Ser.

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“…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.…”

mentioning

confidence: 99%

“…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.…”

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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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“…Cryptophyte phycobiliproteins are immunochemically related to cyanobacteria and rhodophyte phycobiliproteins (MacColl et al 1976), suggesting a common evolutionary ancestry to the 3 pigment groups. However, the phylogenetic status of cryptophyte phycobiliproteins is complicated by their distinct physical properties and molecular structures (Glazer 1981), and especially by the unique way in which they are organized within the chloroplast .…”

Section: Introductionmentioning

confidence: 99%

“…Whereas it had been well-established that cyanobacteria and rhodophytes mobilize phycobiliproteins as an endogenous nitrogen source in response to nitrogen deprivation Chapman et al, 1978;Yamanaka and Glazer, 1980;Lapointe, 1981;Stevens et al, 1981;Kost et al, 1984;Schenk et al, 1987;Levy and Gantt, 1990), this response had not been examined in cryptophytes. Given the immunochemical relatedness between cyanobacteria, rhodophyte, and cryptophyte phycobiliproteins (MacColl et al, 1976; and the overwhelming evidence that the cryptophyte chloroplast evolved from a rhodophyte endosymbiont (Greenwood et al, 1977;Gillot and Gibbs, 1980;Whatley, 1981;Gibbs, 1985, 1989;Hansmann et al, 1986;Hansmann, 1988) it seemed likely that, similar to cyanobacteria and rhodophytes, the catabolism of phycobiliproteins may be an early response to nitrogen depletion in cryptophytes. Therefore, this study examined the hypothesis that P. salina mobilizes phycoerythrin during nitrogen deprivation in order to help supply the biosynthetic demands for cellular growth (see Chapter 2).…”

mentioning

confidence: 99%

Physiological studies of phototrophy and heterotrophy in two algae with contrasting nutritional characteristics, Pyrenomonas salina (Cryptophyceae) and Poterioochromonas malhamensis (Chrysophyceae)

Lewitus¹

1990

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Characterization of cryptomonad phycoerythrin and phycocyanin

Cited by 74 publications

References 37 publications

Adaptation of Synechococcus in situ determined by variability in intracellular phycoerythrin-543 at a coastal station off the Southern California coast, USA

Adaptation of Synechococcus in situ determined by variability in intracellular phycoerythrin-543 at a coastal station off the Southern California coast, USA

Immunochemistry on Cryptomonad Biliproteins

Physiological studies of phototrophy and heterotrophy in two algae with contrasting nutritional characteristics, Pyrenomonas salina (Cryptophyceae) and Poterioochromonas malhamensis (Chrysophyceae)

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