Molecular evolution and environmental acclimation of the fish skeletal muscle tropomyosin

M. C. Huang, Y. Ochiai

Research output: Chapter in Book/Report/Conference proceedingChapter


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.

Original languageEnglish
Title of host publicationTeleosts
Subtitle of host publicationEvolutionary Development, Diversity and Behavioral Ecology
PublisherNova Science Publishers, Inc.
Number of pages30
ISBN (Electronic)9781629487557
ISBN (Print)9781629487540
Publication statusPublished - 2014 Jan 1
Externally publishedYes


  • Evolution
  • Fish
  • Muscle
  • Stability
  • Structure
  • Tropomyosin

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)


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