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MOLECULAR EVOLUTION OF THE Ca 2+ ‐BINDING PHOTOPROTEINS OF THE HYDROZOA
Author(s) -
Tsuji Frederick I.,
Ohmiya Yoshihiro,
Fagan Thomas F.,
Toh Hiroyuki,
Inouye Satoshi
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb08713.x
Subject(s) - aequorin , photoprotein , ef hand , histidine , binding site , cysteine , chemistry , calcium binding protein , peptide sequence , amino acid , biochemistry , tyrosine , biology , stereochemistry , calcium , bioluminescence , enzyme , organic chemistry , intracellular , gene
— Alignment of the primary structures of the hydrozoan photoproteins, aequorin, mitrocomin, clytin and obelin showed very strong amino acid sequence identities. The Ca 2+ ‐binding sites of the proteins were found to be highly conserved. The Ca 2+ ‐binding sites were also homologous to the Ca 2+ ‐binding sites of other Ca 2+ ‐binding proteins. However, aequorin, mitrocomin, clytin and obelin differed from other Ca 2+ ‐binding proteins in that they contained a relatively large number of cysteine, tryptophan, histidine, proline and tyrosine residues, suggesting that these residues may have evolved as part of the light‐emitting mechanism. Construction of a phylogenetic tree showed that aequorin, mitrocomin, clytin and obelin form a closely related group of proteins.