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Evolution of the Phycobiliproteins

Amino acid sequence alignments and phylogenetic analyses have been used to examine the relationships among 100 phycobiliprotein sequences. The alignments revealed a number of highly conserved amino acid residues that are involved in chromophore attachment and conformation, α-β interactions and phyco...

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Bibliographic Details
Published in:Journal of molecular biology 1995-04, Vol.248 (1), p.79-96
Main Authors: Apt, Kirk E., Collier, Jackie L., Grossman, Arthur R.
Format: Article
Language:English
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Summary:Amino acid sequence alignments and phylogenetic analyses have been used to examine the relationships among 100 phycobiliprotein sequences. The alignments revealed a number of highly conserved amino acid residues that are involved in chromophore attachment and conformation, α-β interactions and phycobilisome assembly. The phylogenetic analysis confirmed that the phycobiliprotein subfamilies, previously classified by their biochemical and spectroscopic properties, also formed coherent evolutionary groups. The α and β subunits formed two distinct evolutionary lines that originate from a common ancestor. The pattern of divergence among the α subfamilies was identical to that of the β subfamilies, strongly suggesting that the α and β subunits of each phycobiliprotein type have coevolved. The phylogenetic data support a monophyletic separation of the eukaryotic sequences from the extant cyanobacterial sequences. The eukaryotic phycoerythrins appeared more closely related to the marine Synechococcusphycoerythrins than to the other cyanobacterial phycoerythrins. The cryptophyte phycobiliproteins formed a monophyletic group within the rhodophyte lineage. In conjunction with other phylogenetic markers, the analysis of additional phycobiliprotein sequences may help to further resolve the relationships among phycobiliprotein-containing organisms.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1995.0203