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1.
Indian J Biochem Biophys ; 2000 Dec; 37(6): 486-90
Article in English | IMSEAR | ID: sea-28653

ABSTRACT

Phycobilisomes (Pbsomes) are the supra macromolecular pigment protein complexes of cyanobacteria. Synechococcus Pbsomes are comprised of phycocyanins (PC) and allophycocyanins (APC). Pbsomes are major light harvesting antennae and also absorb ultraviolet-B (UV-B) radiation (280-320 nm). Synechococcus Pbsomes, upon exposure to low dose of UV-B (0.28 mW cm-2) for different time intervals showed profound alteration in their steady state absorption, fluorescence excitation and emission characteristics (Sah et. al. Biochem. Mol. Biol.Int., Vol. 44, No. 2, 245-247). In the present study, we investigated the effect of low dose of UV-B on isolated Pbsome of Synechococcus. Our results demonstrate the following alterations. Absorbance at 623 nm initially showed a sharp decrease with increasing exposure time to UV-B radiation. The changes in the visible to near ultraviolet absorption and excitation ratio indicated a change in chromophore conformation, upon prolonged exposure of Pbsomes to UV-B radiation. This modification of chromophore conformation appeared to be associated with the loss of energy transfer from PC to APC. Circular dichroism spectra in the amide region showed a significant loss of the alpha helical content of Pbsomes when exposed for longer duration to UV-B. CD spectra in the visible region revealed a marked decrease in the rotational strength at 620 nm. Close monitoring of CD signals emanating in the 500 to 700 nm range further revealed that the decrease in the rotational strength was closely associated with an initial red shift in the positive CD band of Pbsomes when exposed to UV-B for short duration. However, the peak became constant over prolonged exposure to UV-B radiation and accompanied a prominent blue shoulder in the positive CD band which suggests the modification and uncoupling of the various phycocyanobilin (PCB) chromophores of the Synechococcus Pbsomes.


Subject(s)
Bacterial Proteins/chemistry , Cyanobacteria/chemistry , Dose-Response Relationship, Radiation , Light-Harvesting Protein Complexes , Phycobilisomes , Plant Proteins/chemistry , Protein Conformation , Ultraviolet Rays
2.
Indian J Biochem Biophys ; 2000 Dec; 37(6): 470-6
Article in English | IMSEAR | ID: sea-27340

ABSTRACT

Acyl-lipid desaturation introduces double bonds (unsaturated bonds) at specifically defined positions of fatty acids that are esterified to the glycerol backbone of membrane glycerolipids. Desaturation pattern of the glycerolipids of Cylindrospermopsis raciborskii (C. raciborskii), a filamentous cyanobacterial strain, was determined in cells grown at 35 degrees C and 25 degrees C. The lowering of the growth temperature from 35 degrees C to 25 degrees C resulted in a considerable accumulation of polyunsaturated octadecanoic fatty acids in all lipid classes. Lipid unsaturation of C. raciborskii was also compared to Synechocystis PCC6803. In C. raciborskii cells, a shift in growth temperature induced a much more pronounced alteration in the desaturation pattern of all lipid classes than in Synechocystis PCC6803. The tolerance to low-temperature photoinhibition of the C. raciborskii cells grown at 25 degrees C and 35 degrees C was also compared to the tolerance of Synechocystis cells grown at the same temperatures. Lower growth temperature increased the tolerance of C. raciborskii cells but not that of Synechocystis cells. These results strengthen the importance of polyunsaturated glycerolipids in the tolerance to environmental stresses and may give a physiological explanation for the determinative role of C. raciborskii strain in algal blooming in the Lake Balaton (Hungary).


Subject(s)
Adaptation, Physiological , Cold Temperature , Cyanobacteria/metabolism , Fatty Acids, Unsaturated/biosynthesis , Light
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