Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins.

Abstract:

:A cDNA for a type II antifreeze protein was isolated from liver of smelt (Osmerus mordax). The predicted protein sequence is homologous to that from sea raven (Hemitripterus americanus) and both show homology to a family of calcium-dependent lectins. Smelt and sea raven belong to taxonomic orders believed to have diverged prior to Cenozoic glaciation. Thus, type II antifreeze proteins appear to have evolved independently in these fish species from pre-existing calcium-dependent lectins. Sequence alignment of the antifreezes and the lectins suggest that these proteins adopt a similar fold, that the sea raven antifreeze has lost its Ca2+ binding sites, and the smelt antifreeze has retained one site. Experiments show that smelt antifreeze protein activity is responsive to Ca2+ but that of sea raven antifreeze protein is not. These results suggest that the type II fish antifreeze proteins and calcium-dependent lectins share a common ancestry, related folding structures, and functional similarity.

authors

Ewart KV,Rubinsky B,Fletcher GL

doi

10.1016/s0006-291x(05)90005-3

subject

Has Abstract

pub_date

1992-05-29 00:00:00

pages

335-40

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)90005-3

journal_volume

185

pub_type

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