Abstract

Phycobilisomes (PBS), the major light harvesting antenna of the cyanobacterium Synechococcus contain phycocyanin (PC) and allophycocyanin (APC) as major pigment-protein complexes. PBS also absorb ultraviolet-B (280-320 nm) radiation. Exposure of Synechococcus PBS to low dose of UV-B (approximately 0.28 mw.cm-2) for 90 min induced change in absorption, emission and excitation characteristics of PBS and these changes got enhanced after 3 h of exposure. Room temperature excitation and emission spectra clearly indicated uncoupling of energy transfer from PC to APC on exposure to UV-B. Also, the 77K emission spectra suggested that F682 emission originating from APC decreased by 42% after 3 h of exposure. Circular dichroism (CD) spectra of UV-B exposed PBS indicated changes (14% decrease) in the alpha-helical content after 90 min treatment. SDS-PAGE analysis indicated degradation of a 75 kDa polypeptide (which appear to be a linker polypeptide) on UV-B treatment. The degradation of this polypeptide seems to induce changes in pigment-protein interaction and decoupling of energy transfer within the PBS. Our results for the first time clearly indicate that the PBS of Synechococcus are targets for UV-B damage.

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