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A novel fatty acid-binding protein-like carotenoid- Binding protein from the gonad of the New Zealand sea urchin Evechinus chloroticus

Journal Article


Abstract


  • A previously uncharacterized protein with a carotenoid-binding function has been isolated and characterized from the gonad of the New Zealand sea urchin Evechinus chloroticus. The main carotenoid bound to the protein was determined by reversed phase-high performance liquid chromatography to be 99-cis-echinenone and hence this 15 kDa protein has been called an echinenone-binding protein (EBP). Purification of the EBP in quantity from the natural source proved to be challenging. However, analysis of EBP by mass spectrometry combined with information from the Strongylocentrotus purpuratus genome sequence and the recently published E. chloroticus transcriptome database, enabled recombinant expression of wild type EBP and also of a cysteine61 to serine mutant that had improved solubility characteristics. Circular dichroism data and ab initio structure prediction suggests that the EBP adopts a 10-stranded b-barrel fold consistent with that of fatty acid-binding proteins. Therefore, EBP may represent the first report of a fatty acid-binding protein in complex with a carotenoid.

UOW Authors


  •   Brewster, Jodi
  •   Sabherwal, Manya (external author)
  •   Garama, Daniel (external author)
  •   Carne, Alan (external author)

Publication Date


  • 2014

Citation


  • Pilbrow, J., Sabherwal, M., Garama, D. & Carne, A. (2014). A novel fatty acid-binding protein-like carotenoid- Binding protein from the gonad of the New Zealand sea urchin Evechinus chloroticus. PLoS One, 9 (9), e106465-1-e106465-14.

Scopus Eid


  • 2-s2.0-84906996462

Start Page


  • e106465-1

End Page


  • e106465-14

Volume


  • 9

Issue


  • 9

Place Of Publication


  • United States

Abstract


  • A previously uncharacterized protein with a carotenoid-binding function has been isolated and characterized from the gonad of the New Zealand sea urchin Evechinus chloroticus. The main carotenoid bound to the protein was determined by reversed phase-high performance liquid chromatography to be 99-cis-echinenone and hence this 15 kDa protein has been called an echinenone-binding protein (EBP). Purification of the EBP in quantity from the natural source proved to be challenging. However, analysis of EBP by mass spectrometry combined with information from the Strongylocentrotus purpuratus genome sequence and the recently published E. chloroticus transcriptome database, enabled recombinant expression of wild type EBP and also of a cysteine61 to serine mutant that had improved solubility characteristics. Circular dichroism data and ab initio structure prediction suggests that the EBP adopts a 10-stranded b-barrel fold consistent with that of fatty acid-binding proteins. Therefore, EBP may represent the first report of a fatty acid-binding protein in complex with a carotenoid.

UOW Authors


  •   Brewster, Jodi
  •   Sabherwal, Manya (external author)
  •   Garama, Daniel (external author)
  •   Carne, Alan (external author)

Publication Date


  • 2014

Citation


  • Pilbrow, J., Sabherwal, M., Garama, D. & Carne, A. (2014). A novel fatty acid-binding protein-like carotenoid- Binding protein from the gonad of the New Zealand sea urchin Evechinus chloroticus. PLoS One, 9 (9), e106465-1-e106465-14.

Scopus Eid


  • 2-s2.0-84906996462

Start Page


  • e106465-1

End Page


  • e106465-14

Volume


  • 9

Issue


  • 9

Place Of Publication


  • United States