Light- and MgCl2-dependent characteristics of four chlorophyll-protein complexes isolated from the marine dinoflagellate, Glenodinium sp (original) (raw)
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Proceedings of the Royal Society of London, 1990
Affinity-purified antibodies prepared against the peridinin-chlorophyll aprotein (POP) complex from the dinoflagellate pygmaea were employed to study the immunological similarity of PCP among 28 dinoflagellate species, representing eight genera in four families. The anti-HpPCP antibodies cross-reacted with the subunits of PCP apoproteins from all dinoflagellates tested, but did not cross-react with pigment proteins from the chrysophyte Cricosphaera establishing its specificity for dinoflagellate pigment-protein complexes. Among the dinoflagellates, the PCP apoprotein occurs either as a monomer of about 35 kDa or as an apparent homodimer of about 15 kDa. In some instances, both subunit polypeptides are present simultaneously. The occurrence of different quaternary structures of the PCP apoprotein in different algae can serve as a taxonomic tool, when used in conjunction with other characters. Abbreviations used in the text: PCP, peridinin-chlorophyll a-protein; anti-HpPCP, antibodies against PCP from Heterocapsa ; SDS-page, sodium dodecyl sulphate polyacrylamide gel electrophoresis.
Biochimica et biophysica acta, 2014
The chlorophyll a-chlorophyll c2-peridinin-protein (apcPC), a major light harvesting component in peridinin-containing dinoflagellates, is an integral membrane protein complex. We isolated functional acpPC from the dinoflagellate Symbiodinium. Both SDS-PAGE and electrospray ionization mass spectrometry (ESI-MS) analysis quantified the denatured subunit polypeptide molecular weight (MW) as 18kDa. Size-exclusion chromatography (SEC) and blue native gel electrophoresis (BN-PAGE) were employed to estimate the size of native acpPC complex to be 64-66kDa. We also performed native ESI-MS, which can volatilize and ionize active biological samples in their native states. Our result demonstrated that the native acpPC complex carried 14 to 16 positive charges, and the MW of acpPC with all the associated pigments was found to be 66.5kDa. Based on these data and the pigment stoichiometry, we propose that the functional light harvesting state of acpPC is a trimer. Our bioinformatic analysis indic...
Characterization of the peridinin–chlorophyll a-protein complex in the dinoflagellate Symbiodinium
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2012
The water-soluble peridinin-chlorophyll a-proteins (PCPs) are one of the major light harvesting complexes in photosynthetic dinoflagellates. PCP contains the carotenoid peridinin as its primary pigment. In this study, we identified and characterized the PCP protein and the PCP gene organization in Symbiodinium sp. CS-156. The protein molecular mass is 32.7 kDa, revealing that the PCP is of the monomeric form. The intronless PCP genes are organized in tandem arrays. The PCP gene cassette is composed of 1095-bp coding regions and spacers in between. Despite the heterogeneity of PCP gene tandem repeats, we identified a single form of PCP, the sequence of which exactly matches the deduced sequence of PCP gene clone 7 (JQ395030) by LC-MS/MS analysis of tryptic digested PCP, revealing the mature PCP apoprotein is 312 amino acids in length. Pigment analysis showed a peridinin-to-Chl a ratio of 4. The peridinin-to-Chl a Q y energy transfer efficiency is 95% in this complex.
Biochimica Et Biophysica Acta - Bioenergetics, 1979
Three chlorophyll-protein complexes have been resolved from blue-green algae using an improved procedure for membrane solubilization and electrophoretic fractionation. One complex has a red absorbance maximum of 676 nm and a molecular weight equivalency of 255 000 + 15 000. A second complex has an absorbance maximum of 676 nm, a molecular weight equivalency of 118000+ 8000, and resembles the previously described P-700-chlorophyll a-protein (CPI) of higher plants and algae. The third chlorophyll-protein has a red absorbance maximum of 671 nm and a molecular weight equivalency of 58 000 + 5000. Blue-green algal membrane fractions enriched in Photosystem I and heterocyst cells do not contain this third chlorophyll-protein, whereas Photosystem II-enriched membrane fractions and vegetative cells do. A component of the same spectral characteristics and molecular weight equivalency was also observed in chlorophyll b-deficient mutants of barley and maize. It is hypothesized that this third complex is involved in some manner with Photosystem II.
Journal of Experimental Marine Biology and Ecology, 2016
The effects of two irradiance levels on growth, cell volume, pigment content and photosynthetic efficiency were analysed in cultures of the peridinin-containing dinoflagellates Akashiwo sanguinea, Prorocentrum micans and Scrippsiella trochoidea. Strains were isolated from coastal waters in southern Brazil, and cells were grown at low (LL, 87-90 μmol photons m −2 s −1) and high (HL, 450-490 μmol photons m −2 s −1) light intensities. The composition of photosynthetic pigments was analysed by high-performance-liquid-chromatography (HPLC) in samples collected at days 2, 7 and 14 of growth, and the photosynthetic efficiency (F v /F m) was determined by pulse-amplitude-modulated fluorometry. On day 14, cells were stained with Nile Red and observed under the fluorescence microscope for lipid content determination. Similar growth rates were observed for A. sanguinea (μ = 0,26-0,33 d −1) and P. micans (μ = 0,25-0,31 d −1) under HL and LL, whereas S. trochoidea presented significantly higher values under HL (0,29 ± 0.02; p b 0,001) than LL (μ = 0,23 ± 0.01 d −1). Increase in the cell volume was observed for P. micans along the growth curve in both irradiances while for A. sanguinea at LL only. The three species presented low concentration of photoprotective pigments under both HL and LL, whereas S. trochoidea and P. micans showed higher photosynthetic efficiency (average: F v /F m N 0.5) compared to A. sanguinea (F v / F m~0 .2). Microscope observation revealed that intracellular lipid concentration increased at HL in the three species, in all growth stages. In short, the three dinoflagellates are adapted to HL intensity and increased lipids might serve as a protective mechanism for the cells.
Plant and Cell Physiology, 1992
Light-harvesting chlorophyll-protein was purified from thylakoid membranes of the marine unicellular alga Nannochloropsis sp. (Eustigmatophyceae), which contains neither chlorophyll b nor chlorophyll c. Solubilization of thylakoid membranes with octyl-/?-D-glucopyranoside or with digitonin followed by separation on sucrose density gradient yielded a chlorophyll-protein complex composed of an apoprotein of 26 kDa and an average of 9 chlorophyll a and 4 violaxanthin molecules per apoprotein. Excitation spectra of chlorophyll a fluorescence for the algal thylakoid membranes indicated energy transfer from the xanthophylls; however, any attempt to solubilize the membranes greatly decreased energy transfer which was further reduced as the purification proceeded. The 26 kDa polypeptide of the isolated light-harvesting complex did not cross-react with polyclonal antibodies raised against analogous proteins from higher plants and chlorophyll a/c alga. The N-terminus amino acid sequence of the apoprotein shows significant structural similarity to the N-termini of the mature light harvesting fucoxanthin, chlorophyll a/c proteins from the diatom Phaeodactylum tricornutum, but not with the N-termini of light-harvesting proteins from chlorophyll a/b containing organisms.
Chlorophyll and peptide compositions in the two photosystems of marine green algae
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1976
The molar ratios of chlorophyll a to b in the thalli of marine green algae were between 1.5 and 2.2, being appreciably lower than the ratio between 2.8 and 3.4 found for the leaves of higher plants and the cells of fresh-water green algae. The ratio of chlorophylls to P-700 in these marine algae was also lower than that in higher plants. The a/b ratios in the pigment proteins of Photosystems 1 and 2 separated by polyacrylamide-gel electrophoresis from sodium dodecyl sulfate-solubilized chloroplasts of four species of marine green algae, Bryopsis maxima, Cheatomorpha spiralis, Enteromorpha compressa and Ulva conglobata, were approximately 5 and l, which are considerably smaller than the ratios, 7 and 2, respectively, found for the pigment proteins of the two photosystems of higher plants separated by the same technique.
Journal of Phycology, 1998
The absorbance and fluorescence emission spectra for three species of Dinophysis, D. caudata Saville-Kent, D. fortii Pavillard, and D. acuminata Claparède et Lachmann, were obtained through an in vivo microanalytical technique using a new type of transparent filter. The pigment signatures of these Dinophysis species were compared to those of Synechococcus Nägeli, a cryptophyte, and two wild rhodophytes, as well as those of another dinoflagellate, a diatom, and a chlorophyte. Phycobilins are not considered a native protein group for dinoflagellates, yet the absorption and fluorescence properties of the three Dinophysis species were demonstrated to closely resemble phycobilins and chlorophylls of Rhodomonas Karsten (Cryptophyceae). Analyses of Dinophysis species using epifluorescence microscopy found no additional nucleus or nuclear remnant as would be contributed by an endosymbiont.