Abstract:
: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.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Tsuji FI,Ohmiya Y,Fagan TF,Toh H,Inouye Sdoi
10.1111/j.1751-1097.1995.tb08713.xsubject
Has Abstractpub_date
1995-10-01 00:00:00pages
657-61issue
4eissn
0031-8655issn
1751-1097journal_volume
62pub_type
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