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Molecular cloning, expression pattern of β-carotene 15,15-dioxygenase gene and association analysis with total carotenoid content in pearl oyster Pinctada fucata martensii.

Authors :
Lei, Chao
Li, Junhui
Zheng, Zhe
Du, Xiaodong
Deng, Yuewen
Source :
Comparative Biochemistry & Physiology - Part B: Biochemistry & Molecular Biology. Mar2019, Vol. 229, p34-41. 8p.
Publication Year :
2019

Abstract

Abstract β -carotene-15,15-dioxygenase is an enzyme involved in carotenoid metabolism to catalyze oxidative cleavage of β -carotene at its central double bond to two molecules of retinal in intestinal cells of vertebrate. In this study, we cloned and characterized β -carotene-15,15-dioxygenase in pearl oyster Pinctada fucata martensii (PmβCDOX). The full length of PmβCDOX gene was 1802 bp, including 1554 bp of the open reading frame (ORF) that encoded 517 amino acids, a 5′UTR of 134 bp and a 3′ UTR of 114 bp. PmβCDOX was expressed at various tissues with highest level in hepatopancreas. Eighteen and fifteen single nucleotide polymorphisms (SNPs) were separately obtained in the exon and promoter of PmβCDOX. Eight SNPs (six SNPs in the exon and two SNPs in the promoter region) were significantly associated to total carotenoid content (TCC) (P <.05). The eight SNPs of significantly associated TCC were divided three haploblocks. Haplotypes CCTT had larger TCC than other haplotypes. The present results suggest that PmβCDOX is involved in carotenoid metabolism in pearl oyster. Our study will be helpful for development gene marker in selective breeding programs for TCC trait of the species. Highlights • We cloned the full-length and promoter of βCDOX in Pinctada fucata martensii. • Eighteen and fifteen single nucleotide polymorphisms (SNPs) were separately obtained in the exon and promoter of PmβCDOX. • Haplotypes CCTT had larger TCC (total carotenoid content) than other haplotypes. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10964959
Volume :
229
Database :
Academic Search Index
Journal :
Comparative Biochemistry & Physiology - Part B: Biochemistry & Molecular Biology
Publication Type :
Academic Journal
Accession number :
134253840
Full Text :
https://doi.org/10.1016/j.cbpb.2018.11.006