Molecular evolution of the Ca(2+)-binding photoproteins of the Hydrozoa.

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 Photobiol

authors

Tsuji FI,Ohmiya Y,Fagan TF,Toh H,Inouye S

doi

10.1111/j.1751-1097.1995.tb08713.x

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

657-61

issue

4

eissn

0031-8655

issn

1751-1097

journal_volume

62

pub_type

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