Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta

Abstract

The primary structure of an elastase from the Antarctic fish Notothenia neglecta (NE) was elucidated by molecular cloning and cDNA sequence analysis. The cDNA of interest was isolated from a cDNA library obtained from Notothenia's pyloric caeca. The amino acid sequence identity with mammalian elastases ranges between 53 and 64%, but interestingly reaches 79% with one isoform (CEB) of two recently isolated cod elastases. The most interesting changes distinguishing the model of NE, predicted from the three dimentional structure of the native porcine elastase (PE), concern the catalytic crevice located in the inter-domains region. These features might be involved in the adaptation to cold of the Antarctic elastase.