Abstract
Much controversy exists as to the level at which light exerts control over the biosynthesis of the photosynthetic apparatus in higher plants and other organisms. The eukaryotic red algaCyanidium caldarium, like higher plants, undergoes light induction of chlorophyll synthesis. In addition to chlorophyll α the alga also synthesises the linear tetrapyrrole phycocyanobilin, which is combined with α or β apobiliproteins to form phycocyanin, the major light-harvesting pigment in this organism. We have previously shown that the tetrapyrrole precursor 5-aminolaevulinic acid (ALA) can substitute for light in inducing the biosynthesis of the phycocyanobilin moiety of this protein. We have also described the appearance of a protein of similar isoelectric point and molecular weight to phycocyanin in ALA-fed cells (Turner et al., 1992, Plant Physiol Biochem 30: 309–314). We now report on the protein's immunological and sequence identity with phycocyanin α and β subunits, and provide further evidence that bilin-apoprotein ligation is light dependent.
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Turner, L., Houghton, J.D. & Brown, S.B. Purification and identification of apophycocyanin α and β subunits from soluble protein extracts of the red algaCyanidium caldarium. Light exposure is not a prerequisite for biosynthesis of the protein moiety of this photosynthetic accessory pigment. Planta 201, 78–83 (1997). https://doi.org/10.1007/BF01258683
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DOI: https://doi.org/10.1007/BF01258683