Carotenoid Isomerase Is Key Determinant of Petal Color of Calendula officinalis*
Carotenoid Isomerase Is Key Determinant of Petal Color of Calendula officinalis*
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类胡萝卜素异构酶是金盏花花瓣颜色的关键决定因素*
DOI:
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发表时间:
2011
影响因子:
4.8
通讯作者:
A. Ohmiya
中科院分区:
文献类型:
--
作者:
S. Kishimoto;A. Ohmiya
Background: Reddish 5-cis-carotenoids accumulate in the orange but not yellow petals of calendula. Results: A CRTISO in orange petals of calendula lacks an isomerase activity. Conclusion: CRTISO activity is a key factor in determining calendula petal color. Significance: Cys-His-His at position 462 and Gly at position 450 of CoCRTISO are important for the isomerase activity. Orange petals of calendula (Calendula officinalis) accumulate red carotenoids with the cis-configuration at the C-5 or C-5′ position (5-cis-carotenoids). We speculated that the orange-flowered calendula is a carotenoid isomerase (crtiso) loss-of-function mutant that impairs the cis-to-trans conversion of 5-cis-carotenoids. We compared the sequences and enzyme activities of CRTISO from orange- and yellow-flowered calendulas. Four types of CRTISO were expressed in calendula petals. The deduced amino acid sequence of one of these genes (CoCRTISO1) was different between orange- and yellow-flowered calendulas, whereas the sequences of the other three CRTISOs were identical between these plants. Analysis of the enzymatic activities of the CoCRTISO homologs showed that CoCRTISO1-Y, which was expressed in yellow petals, converted carotenoids from the cis-to-trans-configuration, whereas both CoCRTISO1-ORa and 1-ORb, which were expressed in orange petals, showed no activity with any of the cis-carotenoids we tested. Moreover, the CoCRTISO1 genotypes of the F2 progeny obtained by crossing orange and yellow lines linked closely to petal color. These data indicate that CoCRTISO1 is a key regulator of the accumulation of 5-cis-carotenoids in calendula petals. Site-directed mutagenesis showed that the deletion of Cys-His-His at positions 462–464 in CoCRTISO1-ORa and a Gly-to-Glu amino acid substitution at position 450 in CoCRTISO1-ORb abolished enzyme activity completely, indicating that these amino acid residues are important for the enzymatic activity of CRTISO.
影响因子:
3.5
作者:
HO, SN;HUNT, HD;PEASE, LR
通讯作者:
PEASE, LR
影响因子:
6.9
作者:
Matthews, PD;Luo, RB;Wurtzel, ET
通讯作者:
Wurtzel, ET