Abstract
Genes encoding the α and β subunits of class II phycoerythrin from Synechococcus sp. strain WH8103 were cloned and sequenced. The deduced amino acid sequences were compared to class II phycoerythrin from Synechococcus sp. strain WH8020 and found to share 92% identity, yet the proteins differ in the bilin isomer (phycoerythrobilin versus phycourobilin) bound to two of the six chromophore attachment sites. Amino acid residues which might contact the bilin at each of the two variable sites were inferred by sequence alignment with phycocyanins. Putative bilin-contacting residues differing between the two phycocrythrins were identified which may determine bilin specificity.
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de Lorimier, R., Chen, CC.J. & Glazer, A.N. Sequence comparison of two highly homologous phycoerythrins differing in bilin composition. Plant Mol Biol 20, 353–356 (1992). https://doi.org/10.1007/BF00014507
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DOI: https://doi.org/10.1007/BF00014507