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- 저자 : Yingshan Dong (검색결과 2 건)
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Identification and Functional Characterization of R3 MYB Transcription Factor Genes in Soybean
Shucai Wang,Jinsong Pang,Hongwei Xun,Zhibing Zhang,Yunxiao Zhou,Xueyan Qian,Yingshan Dong,Xianzhong Feng,Bao Liu 한국식물학회 2018 Journal of Plant Biology Vol.61 No.2
In Arabidopsis, trichome formation is regulatedby a MYB-bHLH-WD40 (MBW) transcriptional activatorcomplex, which can activate the expression of GLABRA2(GL2) and R3 MYB genes. GL2 is required for trichomeformation, whereas R3 MYBs inhibit trichome formation byblocking the formation of the MBW complex, thus inhibitingthe expression of GL2. By using the amino acid sequence of theArabidopsis R3 MYB transcription factor TRICHOMELESS1(TCL1) to BLAST the soybean (Glycine max) protein database,we found that there are a total of six R3 MYB genes insoybean, namely Glycine max TRICHOMELESS1 through 6(GmTCL1-GmTCL6). By generating transgenic plants, wefound that trichome formation in soybean plants overexpressingeach of the GmTCLs remained largely unchanged, and theexpression of putative GL1 and GL2 genes in the transgenicplants was unaffected. However, all the GmTCLs interactedwith GLABRA3 (GL3) in transfected Arabidopsis protoplasts,expression each of the GmTCLs in Arabidopsis inhibitedtrichome formation, and the expression levels of GL1 andGL2 were greatly reduced in the Arabidopsis transgenicplants. Moreover, phenotypic complementary analysis showedthat GmTCL1 is functionally equivalent to TCL1. Takentogether, these results suggest that GmTCLs are functionalR3 MYBs, however, they do not regulate trichome formationin soybean.
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Ying Shan,Ying Dong,Dong Jiang 한국응용생명화학회 2015 Applied Biological Chemistry (Appl Biol Chem) Vol.58 No.6
Antibiotic peptides are a battery of broadspectrum antibacterial cationic polypeptides widely distributed in the plant and animal kingdoms. Among them, the human defensins are the first line of defense against pathogens and Mytilin, which is isolated from mussel serum, plays a key role in the mussel defense system. The antibacterial activity of these two peptides is generally ascribed to their overall positive charge, which enables them to disrupt bacterial membrane integrity and function. The aim of this study was to develop an effective method for the biosynthesis of a fusion peptide containing human a-defensin 5 (HD5) and Mytilin-1 in Escherichia coli to improve the antimicrobial activity. The individual HD5 and Mytilin-1 peptides were also synthesized for comparison with the fusion peptide. All the peptides, expressed as soluble fusions with the peptide thioredoxin, were isolated using a three-step purification strategy involving nickel- Sepharose chromatography, enterokinase cleavage, and cationic exchange chromatography. The identity of the peptides was confirmed by SDS-PAGE. Antimicrobial activity assays demonstrated that all the recombinant peptides had strong bactericidal properties and that the HD5 and Mytilin-1 fusion protein displayed higher activity against E. coli and Staphylococcus aureus. The results of this study provide a platform for the development of novel cationic peptides for biological studies.
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