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Molecular analysis of a homogentisate phytyltransferase gene from Lactuca sativa L.

Tocochromanols, usually known as vitamin E, play a crucial role in human and animal nutrition. The enzyme homogentisate phytyltransferase (HPT) performs the first committed step of the vitamin E biosynthetic pathway. The full-length cDNA encoding HPT was isolated from Lactuca sativa L. by rapid ampl... Full description

Journal Title: Molecular Biology Reports 2011, Vol.38(3), pp.1813-1819
Main Author: Ren, Weiwei
Other Authors: Zhao, Lingxia , Zhang, Lida , Wang, Yuliang , Cui, Lijie , Tang, Yueli , Sun, Xiaofen , Tang, Kexuan
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0301-4851 ; E-ISSN: 1573-4978 ; DOI: 10.1007/s11033-010-0297-6
Link: http://dx.doi.org/10.1007/s11033-010-0297-6
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recordid: springer_jour10.1007/s11033-010-0297-6
title: Molecular analysis of a homogentisate phytyltransferase gene from Lactuca sativa L.
format: Article
creator:
  • Ren, Weiwei
  • Zhao, Lingxia
  • Zhang, Lida
  • Wang, Yuliang
  • Cui, Lijie
  • Tang, Yueli
  • Sun, Xiaofen
  • Tang, Kexuan
subjects:
  • Homogentisate phytyltransferase
  • Lactuca sativa
  • Real-time fluorescent quantitative PCR
  • The vitamin E biosynthetic pathway
ispartof: Molecular Biology Reports, 2011, Vol.38(3), pp.1813-1819
description: Tocochromanols, usually known as vitamin E, play a crucial role in human and animal nutrition. The enzyme homogentisate phytyltransferase (HPT) performs the first committed step of the vitamin E biosynthetic pathway. The full-length cDNA encoding HPT was isolated from Lactuca sativa L. by rapid amplification of cDNA ends (RACE). The cDNA, designated as LsHPT , was 1,670 bp long containing an open reading frame (ORF) of 1,185 bp which encoded a protein of 395 amino acids. Sequence analysis indicated that the deduced protein, named as LsHPT, shared high identity with other dicotyledonous HPTs. Real-time fluorescent quantitative PCR (qPCR) analysis revealed that LsHPT was preferentially expressed in mature leaves compared with other tissues. When lettuce plants were subjected to drought and high-light stress treatments, LsHPT expression was markedly increased. Expression of LsHPT in Arabidopsis showed that LsHPT could enhance the α-tocopherol biosynthesis in Arabidopsis . Transient expression of LsHPT via agroinfiltration resulted in 9-fold increase in LsHPT mRNA level and nearly 18-fold enhancement in α-tocopherol content compared with the negative controls.
language: eng
source:
identifier: ISSN: 0301-4851 ; E-ISSN: 1573-4978 ; DOI: 10.1007/s11033-010-0297-6
fulltext: fulltext
issn:
  • 1573-4978
  • 15734978
  • 0301-4851
  • 03014851
url: Link


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titleMolecular analysis of a homogentisate phytyltransferase gene from Lactuca sativa L.
creatorRen, Weiwei ; Zhao, Lingxia ; Zhang, Lida ; Wang, Yuliang ; Cui, Lijie ; Tang, Yueli ; Sun, Xiaofen ; Tang, Kexuan
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subjectHomogentisate phytyltransferase ; Lactuca sativa ; Real-time fluorescent quantitative PCR ; The vitamin E biosynthetic pathway
descriptionTocochromanols, usually known as vitamin E, play a crucial role in human and animal nutrition. The enzyme homogentisate phytyltransferase (HPT) performs the first committed step of the vitamin E biosynthetic pathway. The full-length cDNA encoding HPT was isolated from Lactuca sativa L. by rapid amplification of cDNA ends (RACE). The cDNA, designated as LsHPT , was 1,670 bp long containing an open reading frame (ORF) of 1,185 bp which encoded a protein of 395 amino acids. Sequence analysis indicated that the deduced protein, named as LsHPT, shared high identity with other dicotyledonous HPTs. Real-time fluorescent quantitative PCR (qPCR) analysis revealed that LsHPT was preferentially expressed in mature leaves compared with other tissues. When lettuce plants were subjected to drought and high-light stress treatments, LsHPT expression was markedly increased. Expression of LsHPT in Arabidopsis showed that LsHPT could enhance the α-tocopherol biosynthesis in Arabidopsis . Transient expression of LsHPT via agroinfiltration resulted in 9-fold increase in LsHPT mRNA level and nearly 18-fold enhancement in α-tocopherol content compared with the negative controls.
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titleMolecular analysis of a homogentisate phytyltransferase gene from Lactuca sativa L.
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abstractTocochromanols, usually known as vitamin E, play a crucial role in human and animal nutrition. The enzyme homogentisate phytyltransferase (HPT) performs the first committed step of the vitamin E biosynthetic pathway. The full-length cDNA encoding HPT was isolated from Lactuca sativa L. by rapid amplification of cDNA ends (RACE). The cDNA, designated as LsHPT , was 1,670 bp long containing an open reading frame (ORF) of 1,185 bp which encoded a protein of 395 amino acids. Sequence analysis indicated that the deduced protein, named as LsHPT, shared high identity with other dicotyledonous HPTs. Real-time fluorescent quantitative PCR (qPCR) analysis revealed that LsHPT was preferentially expressed in mature leaves compared with other tissues. When lettuce plants were subjected to drought and high-light stress treatments, LsHPT expression was markedly increased. Expression of LsHPT in Arabidopsis showed that LsHPT could enhance the α-tocopherol biosynthesis in Arabidopsis . Transient expression of LsHPT via agroinfiltration resulted in 9-fold increase in LsHPT mRNA level and nearly 18-fold enhancement in α-tocopherol content compared with the negative controls.
copDordrecht
pubSpringer Netherlands
doi10.1007/s11033-010-0297-6
pages1813-1819
date2011-03