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Wallaby transthyretin

C M Brack1, W Duan, A J Hulbert

  • 1Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Australia.

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
|March 1, 1995
PubMed
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Researchers sequenced transthyretin cDNA from the Tammar wallaby. Evolutionary analysis of this marsupial transthyretin reveals insights into vertebrate evolution, aligning with fossil records.

Area of Science:

  • Comparative genomics
  • Molecular evolution
  • Mammalian biochemistry

Background:

  • Transthyretin (TTR) is a crucial protein involved in thyroid hormone and retinol transport.
  • Understanding TTR evolution across diverse species provides insights into protein structure-function relationships and vertebrate phylogeny.
  • Marsupials, like the Tammar wallaby (Macropus eugenii), represent a unique lineage for evolutionary comparisons.

Purpose of the Study:

  • To clone and sequence the transthyretin cDNA from the Tammar wallaby.
  • To compare the deduced amino acid and nucleotide sequences with those of other vertebrate species.
  • To investigate the evolutionary relationships of transthyretin using molecular phylogenetic analyses.

Main Methods:

  • Construction of a cDNA library from Tammar wallaby liver RNA.

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  • Cloning and sequencing of the full-length transthyretin cDNA.
  • Sequence alignment and phylogenetic analysis (parsimony) of nucleotide and amino acid sequences.

    • Main Results:

    • The Tammar wallaby transthyretin cDNA was successfully sequenced.
    • High similarity (86%) was observed in the thyroxine binding site compared to human transthyretin.
    • Greatest sequence differences were noted in the N-terminal region, corresponding to the disordered N-terminus of human transthyretin.
    • Phylogenetic trees derived from both amino acid and nucleotide sequences were consistent with established fossil records.

    Conclusions:

    • The study provides molecular data on marsupial transthyretin, contributing to the understanding of TTR evolution.
    • Sequence comparisons highlight conserved functional regions (thyroxine binding) and variable regions (N-terminus) across vertebrates.
    • Molecular phylogenetic analyses support the evolutionary history of transthyretins as reflected in the fossil record.