Cloning and Prokaryotic Expression of Carotenoid Cleavage Dioxygenases from Mulberry (Morus notabilis)

Liu, Dan; Qiu, Changyu; Lü, Xiaomei; Zeng, Yanrong; Zhang, Chaohua; Li, Tao; Zhu, Guangshu; He, Jun; Lin, Qiang

doi:10.1155/2022/4811144

Cited by 1 publication

(1 citation statement)

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“…Most of the ChCCOs contained four histidine active sites, which might be closely related to their iron-binding abilities [28,29]. Subcellular localization analysis revealed that ChCCOs were mainly localized in cytoplasm and chloroplast, which was consistent with the CCOs from many other plant species [13,[30][31][32]. Synteny analysis revealed that ChCCD-like-a and ChCCD-like-b were tandem duplicated genes, suggesting that the tandem duplication of CCD-like subfamily members contributed to the amplification of the CCO gene family in C. humilis.…”

Section: Discussionsupporting

confidence: 68%

Characterization of Carotenoid Cleavage Oxygenase Genes in Cerasus humilis and Functional Analysis of ChCCD1

Cheng,

Yang,

Yin

et al. 2023

Plants

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Carotenoid cleavage oxygenases (CCOs) are key enzymes that function in degrading carotenoids into a variety of apocarotenoids and some other compounds. In this study, we performed genome-wide identification and characterization analysis of CCO genes in Cerasus humilis. Totally, nine CCO genes could be classified into six subfamilies, including carotenoid cleavage dioxygenase 1 (CCD1), CCD4, CCD7, CCD8, CCD-like and nine-cis-epoxycarotenoid dioxygenase (NCED), were identified. Results of gene expression analysis showed that ChCCOs exhibited diverse expression patterns in different organs and in fruits at different ripening stages. To investigate the roles of ChCCOs in carotenoids degradation, enzyme assays of the ChCCD1 and ChCCD4 were performed in Escerichia coli BL21(DE3) that can accumulate lycopene, β-carotene and zeaxanthin. The prokaryotic expressed ChCCD1 resulted in obvious degradation of lycopene, β-carotene and zeaxanthin, but ChCCD4 did not show similar functions. To further determine the cleaved volatile apocarotenoids of these two proteins, headspace gas chromatography/mass spectrometer analysis was performed. Results showed that ChCCD1 could cleave lycopene at 5, 6 and 5′, 6′ positions to produce 6-methy-5-hepten-2-one and could catalyze β-carotene at 9, 10 and 9′, 10′ positions to generate β-ionone. Our study will be helpful for clarifying the roles of CCO genes especially ChCCD1 in regulating carotenoid degradation and apocarotenoid production in C. humilis.

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