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1
Arabidopsis MiR396 Mediates the Development of Leaves and Flowers in Transgenic Tobacco

Fengxi Yang,Gang Liang,Dongmei Liu,Diqiu Yu 한국식물학회 2009 Journal of Plant Biology Vol.52 No.5
MicroRNAs (miRNAs) are single-stranded, noncoding small RNAs that usually function as posttranscriptional negative regulators by base pairing to target genes. They are pivotal to plant development. MiR396 is conserved among plant species and is predicted to target GRF (growth-regulating factor) genes in Arabidopsis. Here, overexpression of ath-miR396 in tobacco reduced the levels of three NtGRF-like genes containing an miR396 match site. Furthermore, its elevated expression resulted in a small, narrow leaf phenotype similar to that found with the Arabidopsis grf1grf2grf3 triple mutant. We also demonstrated that 35S:MIR396a transgenic plants were defective in the four whorls of floral organs. These results provide a link between the miR396- mediated regulatory pathway of NtGRF-like gene expression and the developmental processes for leaves and flowers in tobacco.
2
DEER FEEDING FOR VELVET PRODUCTION

Quankai Wang,Fengxi Liang,Tiefeng Wen 건국대학교 동물자원연구센터 1993 국제 심포지움 Vol.- No.4
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숫사슴은 녹용을 직접 생산한다. 숫사슴을 사양하는 목적은 종록으로서의 번식활동뿐만 아니라 녹용이라는 생산물을 생산하는 것이다. 이 때문에 종록으로서의 번식력과 녹용의 생산력을 충분히 발휘할 수 있도록 적절한 영양관리를 하여 과비나 수척하지 않도록 하여야 한다. 즉, 적당한 운동을 하여 정액의 품질을 높이고, 번식년한을 연장하는등 숫사슴의 잠재력을 최대한 발휘시키는 합리적인 이용에 노력하여야 한다. 본 논문은 주로 숫사슴의 사료, 계절별 영향섭취, 1일금여사료 배합량, 녹용생장기의 사양관리, 번식기의 사양관리, 월동기의 사양관리, 자록숫컷의 사양관리, 육성기의 사양관리, 광량조절에 의한 사양등의 내용을 소개한다. Chinese mainly raise Sika ( Cervus nippon ) and Wapiti ( Cervus elaphus ). Deer are raised in yard, which is a majar model of deer raising in China. The purpose of raising stags is to steadily improve their health level, to gain high quality velvet antlers and to cultivate good sexual desire, high semen quality and breeding value stags. Stags can directly affect velvet yield, offspring quality and deer group development. Therefore, it is very important to steadily improve deer feeding and management level.
3
Identification and Characterization of a Novel Terrabacter ginsenosidimutans sp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

An, Dong-Shan,Cui, Chang-Hao,Lee, Hyung-Gwan,Wang, Liang,Kim, Sun Chang,Lee, Sung-Taik,Jin, Fengxie,Yu, Hongshan,Chin, Young-Won,Lee, Hyeong-Kyu,Im, Wan-Taek,Kim, Song-Gun American Society for Microbiology 2010 Applied and environmental microbiology Vol.76 No.17
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ABSTRACTA new β-glucosidase from a novel strain of Terrabacter ginsenosidimutans (Gsoil 3082T) obtained from the soil of a ginseng farm was characterized, and the gene, bgpA (1,947 bp), was cloned in Escherichia coli. The enzyme catalyzed the conversion of ginsenoside Rb1 {3-O-[β-d-glucopyranosyl-(1-2)-β-d-glucopyranosyl]-20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol} to the more pharmacologically active rare ginsenosides gypenoside XVII {3-O-β-d-glucopyranosyl-20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol}, gypenoside LXXV {20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol}, and C-K [20-O-(β-d-glucopyranosyl)-20(S)-protopanaxadiol]. A BLAST search of the bgpA sequence revealed significant homology to family 3 glycoside hydrolases. Expressed in E. coli, β-glucosidase had apparent Km values of 4.2 ± 0.8 and 0.14 ± 0.05 mM and Vmax values of 100.6 ± 17.1 and 329 ± 31 μmol·min−1·mg of protein−1 against p-nitrophenyl-β-d-glucopyranoside and Rb1, respectively. The enzyme catalyzed the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position at pH 7.0 and 37°C. These cleavages occurred in a defined order, with the outer glucose of C-3 cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. These results indicated that BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K. Herein is the first report of the cloning and characterization of a novel ginsenoside-transforming β-glucosidase of the glycoside hydrolase family 3.

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