EVIDENCE FOR A TRANSIENT ASSOCIATION OF NEW PROTEINS WITH THE SPIRULINA-MAXIMA PHYCOBILISOME IN RELATION TO LIGHT-INTENSITY

Environmental parameters are known to affect phycobilisomes. Variations of their structure and relative composition in phycobiliproteins have been observed. We studied the effect of irradiance variations on the phycobilisome structure in the cyanobacterium Spirulina maxima and discovered the appearance of new polypeptides associated with the phycobilisomes under an increased light intensity. In high light, the six rods of phycocyanin associated with the central core of allophycocyanin contained only one to two phycocyanin hexamers instead of the two to three they contained in low light. The concomitant disappearance of a 33-kD linker polypeptide was observed. Moreover, in high light three polypeptides of 29, 30, and 47 kD, clearly unrelated to linkers, were found to be associated with the phycobilisome fraction: protein labeling showed that a specific association of these polypeptides was induced by high light. One polypeptide, at least, would play the role of a chaperone protein. Not only the synthesis of these proteins, which appeared slightly increased in high light, but also their association with phycobilisome structure are light intensity dependent.