4篇
您的检索式：作者名="Baoqing Dun"
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| 1 | Development of highly glyphosate-tolerant tobacco by coexpression of glyphosate acetyltransferase gat and EPSPS G2-aroA genes显示文摘The widely used herbicide glyphosate targets 5-enolpyruvylshikimate-3-phosphate synthase(EPSPS).Glyphosate acetyltransferase(GAT)effectively detoxifies glyphosate by N-acetylation.With the aim of identifying a new strategy for development of glyphosate-tolerant crops,the plant expression vector pG2-GAT harboring gat and G2-aroA(encoding EPSPS)has been transformed into tobacco(Nicotiana tabacum)to develop novel plants with higher tolerance to glyphosate.Results from Southern and Western blotting analyses indicated that the target genes were integrated into tobacco chromosomes and expressed effectively at the protein level.Glyphosate tolerance was compared among transgenic tobacco plants containing gat,G2-aroA,or both genes.Plants containing both gat and G2-aroA genes were the most glyphosate-tolerant.This study has shown that a combination of different strategies may result in higher tolerance in transgenic crops,providing a new approach for development of glyphosate-tolerant crops. | Baoqing Dun Xujing Wang Wei Lu Ming Chen Wei Zhang Shuzhen Ping Zhixing Wang Baoming Zhang Min Lin | 2014 | The Crop Journal2014，2，Z1： | 4 |
| 2 | Identification of a New Gene Encoding EPSPS with High Glyphosate Resistance from the Metagenomic Library显示文摘 | Dan Jin Wei Lu Shuzhen Ping Wei Zhang Jian Chen Baoqing Dun Ruiqiang Ma Zhonglin Zhao Jiying Sha Liang Li Zhirong Yang Ming Chen Min Lin | | 0，2007，： | 1 |
| 3 | Fusion Expression of Glucoamylase and Xylanase in Pichia pastoris显示文摘Employing RT-PCR amplification method, the mature peptide coding sequence of glucoamylase (amyA) gene was amplified from total RNA of Talaromyces emersonii and the xylanase (xynA) gene from genomic DNA of Paenibacillus sp. H10-3. The result showed that the mature peptide sequence of amyA is 1857bp long and encodes 618 amino acids; and the mature peptide sequence of xynA is 636bp long and encodes 211 amino acids. Then these two genes were spliced by overlap extension PCR (SOE-PCR), yielding fusion gene amyA-l-xynA. The fusion gene amyA-l-xynA was then cloned into a Pichia pastoris expression vector pPIC9 to produce the recombinant expression plasmid pPIC9-amyA-l-xynA. The recombinant plasmid pPIC9-amyA-l-xynA was linearized and transformed into Pichia pastoris GS115 via electric shock, yielding engineering strain ALX2. The maximum yields of glucoamylase and xylanase in ALX2 fermentation supernatant were determined as 10.7 and 51.8U/ml, respectively. | Zhi WANG Baoqing DUN Jingang GU Xuan ZHAO Gu TIAN Ming LU Guiying LI | 2012 | Agricultural Biotechnology2012，1，5： | 0 |
| 4 | Reconstruction of enzymatic activity from split genes encoding glyphosate-tolerant EPSPS protein of Psedomonas fluorescens G2 strain by intein mediated protein complementation显示文摘A mutagenesis library was constructed using GPS-LS system to insert a random 5 aa into the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) encoded by aroA gene. Active EPSPS pro- teins were identified by the ability to rescue growth of aroA-deleted mutant ER2799 on M9 minimal media. 12 unique sites, which can tolerate a 5-aa insertion, were identified. In all of the 12 sites, only F295/T296 site was found to split the G2-EPSPS properly by co-transformation of plasmids into E. coli ER2799. The G2-EPSPS gene was then divided into N-termi- nal and C-terminal from F295/T296 site which were fused to the N-terminal and C-terminal of Ssp.DnaE intein, respectively, creating two plasmids pMEPS- N295IN and pKEPSc296Ic. Co-transformation of plasmids, pMEPSN295IN and pKEPSc296Ic, rescu- ed growth of ER2799 in M9 minimal media, indicating that the intein splicing domains were bringing the EPSPS fragments together to generate activity. Re- consituted activity of splitted G2-EPSPS enzyme was 4.48 U/mg. | DUN Baoqing LU Wei ZHANG Wei PING Shuzhen WANG Xujing CHEN Ming XU Yuquan JIN Dan WANG Jin ZHAO Zhonglin LIANG Aimin HOU Songna XU Ming-Qun LIN Min | 2006 | Chinese Science Bulletin2006，51，13： | 0 |
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