Phycobilisomes from the nonchromatic adapting cyanobacterium Spirulina platensis are composed of a central core containing allophycocyanin and rods with phycocyanin and linker polypeptides in a regular array. Room temperature absorption spectra of phycobilisomes from this organism indicated the presence of phycocyanin and allophycocyanin. However, low temperature absorption spectra showed the association of a phycobiliviolin type of chromophore within phycobilisomes. This chromophore had an absorption maximum at 590 nanometers when phycobilisomes were suspended in 0.75 molar K-phosphate buffer (pH 7.0). Purified phycocyanin from this cyanobacterium, was found to consist of three subparticles and the phycobiliviolin type of chromophore was associated with the lowest density subparticle. Circular dichroism spectra of phycocyanin subparticles also indicated the association of this chromophore with the lowest density subparticle. Absorption spectral analysis of a and ,B subunits of phycocyanin showed that phycobiliviolin type of chromophore was attached to the a subunit, but not the ,B subunit. Effect of light quality showed that green light enhanced the synthesis of this chromophore as analyzed from the room temperature absorption spectra of phycocyanin subparticles and subunits, while red or white light did not have any effect. Low temperature absorption spectra of phycobilisomes isolated from green, red, and white light conditions also indicated the enhancement of phycobiliviolin type of chromophore under green light.nm (14,22 (3,10,11,13).The present communication describes the effect of light quality on the synthesis and regulation of phycobiliproteins in the nonchromatic adapting cyanobacterium Spirulina platensis. We report here the presence of a PXB type of chromophore in this cyanobacterium and modulation in its level in response to the light quality.
MATERIALS AND METHODS
OrganismThe cyanobacterium Spirulina platensis was obtained from the Microbiology Division, Indian Agricultural Research Institute, New Delhi, India.
Culture ConditionsPhycobiliproteins are the major accessory light harvesting pigments present in cyanobacteria, red algae, and cryptomonads. These proteins are broadly classified into three groups based on the spectroscopic properties: PE,2 Xmax, 540-570 nm; PC, Xmax, 610-620 nm; and APC, Xmax,650-655 nm (12,14). A few cyanobacteria possess a fourth type of biliprotein, PEC, Xmax, 568 nm, 585 nm(s) in place of PE (7). Each of these phycobiliproteins are comprised of two subunits, a and p3, to which linear tetrapyrroles are covalently attached by a cysteine thioether bond (15). The absorption characteristics of these tetrapyrroles in acidic aqueous solutions group them into four types: PCB, Xmax, 660 nm; PXB, Xmax, 590 nm; phycoerythrobilin Xmax, 555 nm; and phycourobilin Amax, 495