4.7 Article

Ferredoxin-dependent bilin reductases in eukaryotic algae: Ubiquity and diversity

Journal

JOURNAL OF PLANT PHYSIOLOGY
Volume 217, Issue -, Pages 57-67

Publisher

ELSEVIER GMBH
DOI: 10.1016/j.jplph.2017.05.022

Keywords

Algal evolution; Biliverdin; Bioinformatics; Cyanobacteriochromes; Oxygenic photosynthesis; Phycocyanobilin; Phycoerythrobilin; Phylogenetics; Phytochromobilin; Secondary endosymbiosis; Tetrapyrrole metabolism

Categories

Funding

  1. NIH [R01 GM068552]

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Linear tetrapyrroles (bilins) are produced from heme by heme oxygenase, usually forming biliverdin IX alpha (BV). Fungi and bacteria use BV as chromophore for phytochrome photoreceptors. Oxygenic photosynthetic organisms use BV as a substrate for ferredoxin-dependent bilin reductases (FDBRs), enzymes that produce diverse reduced bilins used as light-harvesting pigments in phycobiliproteins and as photoactive photoreceptor chromophores. Bilin biosynthesis is essential for phototrophic growth in Chlamydomonas reinhardtii despite the absence of phytochromes or phycobiliproteins in this organism, raising the possibility that bilins are more generally required for phototrophic growth by algae. We here leverage the recent expansion in available algal transcriptomes, cyanobacterial genomes, and environmental metagenomes to analyze the distribution and diversification of FDBRs. With the possible exception of euglenids, FDBRs are present in all photosynthetic eukaryotic lineages. Phylogenetic analysis demonstrates that algal FDBRs belong to the three previously recognized FDBR lineages. Our studies provide new insights into FDBR evolution and diversification.

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