Expression of a cysteine proteinase inhibitor (oryzacystatin-I) in transgenic tobacco plants

1993 ◽  
Vol 21 (4) ◽  
pp. 655-663 ◽  
Author(s):  
Sameer A. Masoud ◽  
Lowell B. Johnson ◽  
Frank F. White ◽  
Gerald R. Reeck
Keyword(s):  
Transgenic Tobacco ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor ◽  
Transgenic Tobacco Plants ◽  
Tobacco Plants

scholarly journals Signal Peptide of Potato PinII Enhances the Expression of Cry1Ac in Transgenic Tobacco

2004 ◽  
Vol 36 (8) ◽  
pp. 553-558 ◽  
Author(s):  
Yun-Jun Liu ◽  
Yuan Yuan ◽  
Jun Zheng ◽  
Ya-Zhong Tao ◽  
Zhi-Gang Dong ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Signal Peptide ◽  
Proteinase Inhibitor ◽  
Peptide Sequence ◽  
Fluorescent Detection ◽  
Transgenic Tobacco Plants ◽  
Tobacco Plants ◽  
Signal Peptide Sequence ◽  
Proteinase Inhibitor Ii ◽  
Cry1ac Protein

Abstract The modified Cry1Ac was expressed in transgenic tobacco plants. To allow secretion of the Cry1Ac protein into the intercellular space, the signal peptide sequence of potato proteinase inhibitor II (pinII) was N-terminally fused to the Cry1Ac encoding region. Expression of Cry1Ac in transgenic tobacco plants was assayed with ELISA. The results showed that pinII signal peptide sequence enhanced the expression of Cry1Ac protein and led to the secretion of the Cry1Ac protein in transgenic tobacco plants. GFP gene was also fused to the signal peptide sequence and transformed to tobacco. The results of fluorescent detection showed that GFP had localized in the apoplast of transgenic plants.

scholarly journals Wound-induced expression of a potato proteinase inhibitor II gene in transgenic tobacco plants

1987 ◽  
Vol 6 (2) ◽  
pp. 303-306 ◽  
Author(s):  
Jose J. Sanchez-Serrano ◽  
Michael Keil ◽  
Aileen O'Connor ◽  
Jeff Schell ◽  
Lothar Willmitzer
Keyword(s):  
Transgenic Tobacco ◽  
Proteinase Inhibitor ◽  
Transgenic Tobacco Plants ◽  
Tobacco Plants ◽  
Induced Expression ◽  
Proteinase Inhibitor Ii ◽  
Potato Proteinase Inhibitor Ii

The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants

10.1038/70781 ◽  
1999 ◽  
Vol 17 (12) ◽  
pp. 1223-1226 ◽  
Author(s):  
Rafael Gutierrez-Campos ◽  
Juan Antonio Torres-Acosta ◽  
Luis Jorge Saucedo-Arias ◽  
Miguel Angel Gomez-Lim
Keyword(s):  
Transgenic Tobacco ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Transgenic Tobacco Plants ◽  
Tobacco Plants ◽  
Cysteine Proteinase Inhibitors

Production of an active recombinant thrombomodulin derivative in transgenic tobacco plants and suspension cells

2005 ◽  
Vol 14 (3) ◽  
pp. 251-259 ◽  
Author(s):  
Helga Schinkel ◽  
Andreas Schiermeyer ◽  
Raphael Soeur ◽  
Rainer Fischer ◽  
Stefan Schillberg
Keyword(s):  
Transgenic Tobacco ◽  
Transgenic Tobacco Plants ◽  
Suspension Cells ◽  
Tobacco Plants ◽  
Recombinant Thrombomodulin

scholarly journals Overexpression of the pitaya phosphoethanolamine N-methyltransferase gene (HpPEAMT) enhanced simulated drought stress in tobacco

2021 ◽  
Author(s):  
Ai-Hua Wang ◽  
Lan Yang ◽  
Xin-Zhuan Yao ◽  
Xiao-Peng Wen
Keyword(s):  
Drought Stress ◽  
Stress Response ◽  
Transgenic Plants ◽  
Drought Tolerance ◽  
Transgenic Tobacco ◽  
Sequence Similarity ◽  
Amino Acid Sequence Similarity ◽  
Transgenic Tobacco Plants ◽  
Wild Type ◽  
Tobacco Plants

AbstractPhosphoethanolamine N-methyltransferase (PEAMTase) catalyzes the methylation of phosphoethanolamine to produce phosphocholine and plays an important role in the abiotic stress response. Although the PEAMT genes has been isolated from many species other than pitaya, its role in the drought stress response has not yet been fully elucidated. In the present study, we isolated a 1485 bp cDNA fragment of HpPEAMT from pitaya (Hylocereus polyrhizus). Phylogenetic analysis showed that, during its evolution, HpPEAMT has shown a high degree of amino acid sequence similarity with the orthologous genes in Chenopodiaceae species. To further investigate the function of HpPEAMT, we generated transgenic tobacco plants overexpressing HpPEAMT, and the transgenic plants accumulated significantly more glycine betaine (GB) than did the wild type (WT). Drought tolerance trials indicated that, compared with those of the wild-type (WT) plants, the roots of the transgenic plants showed higher drought tolerance ability and exhibited improved drought tolerance. Further analysis revealed that overexpression of HpPEAM in Nicotiana tabacum resulted in upregulation of transcript levels of GB biosynthesis-related genes (NiBADH, NiCMO and NiSDC) in the leaves. Furthermore, compared with the wild-type plants, the transgenic tobacco plants displayed a significantly lower malondialdehyde (MDA) accumulation and higher activities of the superoxide dismutase (SOD) and peroxidase (POD) antioxidant enzymes under drought stress. Taken together, our results suggested that HpPEAMT enhanced the drought tolerance of transgenic tobacco.

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