The genes encoding skeletal muscle tropomyosin, with a unique coiled-coiled linear structure along the full-length molecule, were cloned from a wide range of fish species, and the deduced amino acid sequences, especially the amino acid substitutions between fish species from tropical to cold waters were discussed, based not only on the phylogenetic analyses but also on the species-specificity of thermodynamic properties as measured by calorimetric studies and thermal helical decaying profiles of the purified tropomyosins. The results obtained showed clear differences in thermal stability among the fish species examined, though the identity of amino acid sequences was higher than 92%. It suggests that only a few amino acid substitutions affect the overall stability of the tropomyosin molecules. Several residues especially located on the molecular surface were considered to be responsible for such stability difference. However, it was difficult to pinpoint the responsible residues. Thus it is likely that communications between the residues far from each other on the molecule exist. On the other hand, the molecular mass of these tropomyosins measured by mass spectrometry were generally higher than those calculated based on the deduced amino acid sequences, suggesting the presence of post-translational modifications which could also affect their thermal stability difference.
|Title of host publication||Teleosts|
|Subtitle of host publication||Evolutionary Development, Diversity and Behavioral Ecology|
|Publisher||Nova Science Publishers, Inc.|
|Number of pages||30|
|Publication status||Published - 2014 Jan 1|
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)