Abstract
| Original language | English |
|---|---|
| Article number | e106465 |
| Number of pages | 14 |
| Journal | PLoS ONE |
| Volume | 9 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 2014 |
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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. / Pilbrow, J R; Sabherwal, Manya; Garama, Daniel James; Carne, Alan.
In: PLoS ONE, Vol. 9, No. 9, e106465, 2014.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - A novel fatty acid-binding protein-like carotenoid-binding protein from the gonad of the New Zealand sea urchin Evechinus chloroticus
AU - Pilbrow, J R
AU - Sabherwal, Manya
AU - Garama, Daniel James
AU - Carne, Alan
PY - 2014
Y1 - 2014
N2 - 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 9 -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 beta-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.
AB - 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 9 -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 beta-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.
UR - http://www.plosone.org/article/fetchObject.action?uri=info:doi/10.1371/journal.pone.0106465&representation=PDF
U2 - 10.1371/journal.pone.0106465
DO - 10.1371/journal.pone.0106465
M3 - Article
VL - 9
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 9
M1 - e106465
ER -