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Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia sinensis).
J Agric Food Chem. 2016 Mar 02; 64(8):1770-6.JA

Abstract

Hydroperoxide lyase (HPL, E.C. 4.1.2.) is the major enzyme in the biosynthesis of natural volatile aldehydes and alcohols in plants, however, little was known about HPL in tea plants (Camellia sinensis). A unique cDNA fragment was isolated by suppressive subtractive hybridization (SSH) from a tea plant subjected to herbivory by tea geometrid Ectropis obliqua. This full length cDNA acquired by RACE was 1476 bp and encoded 491 amino acids. DNA and protein BLAST searches showed high homology to HPL sequences from other plants. The His-tag expression vector pET-32a(+)/CsHPL was constructed and transferred into Escherichia coli Rosetta (DE3). The expression product of recombinant CsHPL in E. coli was about 60 kDa. The enzyme activity of CsHPL was 0.20 μmol·min(-1)·mg(-1). Quantitative RT-PCR analysis indicated CsHPL was strongly up-regulated in tea plants after Ectropis obliqua attack, suggesting that it may be an important candidate for defense against insects in tea plants.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Deng WW
State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University , 130 Changjiang West Road, Hefei, Anhui 230036, China.
Wu YL
State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University , 130 Changjiang West Road, Hefei, Anhui 230036, China.
Li YY
State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University , 130 Changjiang West Road, Hefei, Anhui 230036, China.
Tan Z
State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University , 130 Changjiang West Road, Hefei, Anhui 230036, China.
Wei CL
State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University , 130 Changjiang West Road, Hefei, Anhui 230036, China.

MeSH

Aldehyde-LyasesAmino Acid SequenceAnimalsCamellia sinensisCloning, MolecularCytochrome P-450 Enzyme SystemGene Expression Regulation, PlantMolecular Sequence DataMothsPlant LeavesPlant ProteinsSequence Alignment

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

26886573

Citation

Deng, Wei-Wei, et al. "Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia Sinensis)." Journal of Agricultural and Food Chemistry, vol. 64, no. 8, 2016, pp. 1770-6.
Deng WW, Wu YL, Li YY, et al. Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia sinensis). J Agric Food Chem. 2016;64(8):1770-6.
Deng, W. W., Wu, Y. L., Li, Y. Y., Tan, Z., & Wei, C. L. (2016). Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia sinensis). Journal of Agricultural and Food Chemistry, 64(8), 1770-6. https://doi.org/10.1021/acs.jafc.5b05748
Deng WW, et al. Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia Sinensis). J Agric Food Chem. 2016 Mar 2;64(8):1770-6. PubMed PMID: 26886573.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular Cloning and Characterization of Hydroperoxide Lyase Gene in the Leaves of Tea Plant (Camellia sinensis). AU - Deng,Wei-Wei, AU - Wu,Yi-Lin, AU - Li,Ye-Yun, AU - Tan,Zhen, AU - Wei,Chao-Ling, Y1 - 2016/02/17/ PY - 2016/2/18/entrez PY - 2016/2/18/pubmed PY - 2016/10/14/medline KW - Camellia sinensis KW - Ectropis obliqua KW - hydroperoxide lyase KW - induced defense response KW - suppressive subtractive hybridization (SSH) SP - 1770 EP - 6 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 64 IS - 8 N2 - Hydroperoxide lyase (HPL, E.C. 4.1.2.) is the major enzyme in the biosynthesis of natural volatile aldehydes and alcohols in plants, however, little was known about HPL in tea plants (Camellia sinensis). A unique cDNA fragment was isolated by suppressive subtractive hybridization (SSH) from a tea plant subjected to herbivory by tea geometrid Ectropis obliqua. This full length cDNA acquired by RACE was 1476 bp and encoded 491 amino acids. DNA and protein BLAST searches showed high homology to HPL sequences from other plants. The His-tag expression vector pET-32a(+)/CsHPL was constructed and transferred into Escherichia coli Rosetta (DE3). The expression product of recombinant CsHPL in E. coli was about 60 kDa. The enzyme activity of CsHPL was 0.20 μmol·min(-1)·mg(-1). Quantitative RT-PCR analysis indicated CsHPL was strongly up-regulated in tea plants after Ectropis obliqua attack, suggesting that it may be an important candidate for defense against insects in tea plants. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/26886573/Molecular_Cloning_and_Characterization_of_Hydroperoxide_Lyase_Gene_in_the_Leaves_of_Tea_Plant__Camellia_sinensis__ DB - PRIME DP - Unbound Medicine ER -