https://www.ahs.ac.cn/images/0513-353X/images/top-banner1.jpg|#|苹果
https://www.ahs.ac.cn/images/0513-353X/images/top-banner2.jpg|#|甘蓝
https://www.ahs.ac.cn/images/0513-353X/images/top-banner3.jpg|#|菊花
https://www.ahs.ac.cn/images/0513-353X/images/top-banner4.jpg|#|灵芝
https://www.ahs.ac.cn/images/0513-353X/images/top-banner5.jpg|#|桃
https://www.ahs.ac.cn/images/0513-353X/images/top-banner6.jpg|#|黄瓜
https://www.ahs.ac.cn/images/0513-353X/images/top-banner7.jpg|#|蝴蝶兰
https://www.ahs.ac.cn/images/0513-353X/images/top-banner8.jpg|#|樱桃
https://www.ahs.ac.cn/images/0513-353X/images/top-banner9.jpg|#|观赏荷花
https://www.ahs.ac.cn/images/0513-353X/images/top-banner10.jpg|#|菊花
https://www.ahs.ac.cn/images/0513-353X/images/top-banner11.jpg|#|月季
https://www.ahs.ac.cn/images/0513-353X/images/top-banner12.jpg|#|菊花

ACTA HORTICULTURAE SINICA ›› 2016, Vol. 43 ›› Issue (10): 2039-2049.doi: 10.16420/j.issn.0513-353x.2016-0406

Previous Articles     Next Articles

Cloning and Expression Analysis of Catalase CAT1 Gene from Luffa cylindrical

WEN Qing-fang*,LIU Jian-ting,ZHU Hai-sheng,CHEN Min-dong,WANG-Bin,and ZHANG Qian-rong   

  1. (Crops Research Institute,Fujian Academy of Agricultural Sciences;Vegetable Research Center,Fujian Academy of Agricultural Sciences;Fujian Engineering Research Center for Vegetables,Fuzhou 350013,China)
  • Online:2016-10-25 Published:2016-10-25

Abstract:

A length of 1 755 bp cDNA was isolated from Luffa cylindrical by using RACE and RT-PCR techniques,which contained a 1 479 bp open reading frame(ORF)that encoded 492 amino acids,with a predicted molecular weight of 56.98 kD and a hypothetical isoelectric point of 7.126. It shared over 92% identity with the homologous proteins from Cucumis sativusArabidopsis thaliana and Raphanus sativus,proving that it was highly conservative. This gene was named LcCAT1 and the GenBank accession was KP222260. Wolf Psort protection indicated that LcCAT1 protein was located in the peroxisome,and Motif Scan analysis showed that LcCAT1 protein had the characteristic amino acid sequences of catalase proximal heme-ligand and heme active sites in the position of 344–352 and 54–70 sites,respectively,which  suggested that LcCAT1 protein was a typical hydrogen peroxide enzyme(tCAT).The Real time PCR revealed that LcCAT1 exhibited a tissue specific expression,and the expression level in Luffa cylindrical‘Fusi 3leaves was the highest,which was almost five times than that in flowers,fruits,roots and stems. The levels of LcCAT1 were different among six luffa varieties,and the expression in Luffa cylindrical was higher than that in Luffa acutangula Roxb. What is more,the level of LcCAT1 in‘Fusi 3was up-regulated during fresh-cut and post-harvest storage browning processes,which was consistent with the changes observed in peroxidase activity,suggesting that LcCAT1 gene may play a regulation role in luffa browning process.

Key words: Luffa cylindrical, browning, CAT1, gene cloning, real time PCR

CLC Number: