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Xueying Tao(도설영),Wu Jing(오청),Kyoung-Sook Kim(김경숙),Ziniu Yu(유자우),Young-Choon Lee(이영춘) 한국생명과학회 2008 생명과학회지 Vol.18 No.5
해양으로부터 분리한 한천분해효소를 생산하는 미생물을 분리하여 동정한 결과 이 세균은 Pseudoalteromonas sp.로 판명되어 Pseudoalteromonas sp. JT-6로 명명하였다. 또한 이 균주로부터 한천분해효소 유전자를 클로닝하여 염기서열을 결정하였던 바, 이 유전자는 445개의 아미노산을 코드하는 1338 bp의 염기서열로 이루어져 있었다. 이 유전자는 Janthinobacterium sp. SY12와 99%의 높은 아미노산 서열 상동성을 나타내었고 N-말단으로부터 신호서열, 당분해효소 family 16에 속하는 β-agarase 촉매영역 및 탄수화물 결합영역으로 이루어진 도메인 구조를 나타내었다. 대장균에서 생산되어 정제된 재조합 한천분해효소는 40℃와 pH 9.0에서 최대 활성을 나타내었으며, 기질인 한천분해 형태로 볼 때 본 효소는 endo-type의 β-agarase임이 증명되었다. A gene (agaA6) encoding an extracellular agarase from a marine bacterium, Pseudoalteromonas sp. JT-6, was cloned, sequenced and expressed in Escherichia coli. It comprised an open reading frame of 1338 base pairs and encodes a protein of 445 amino acids with a predicted molecular weight of 50,150 daltons. The entire amino acid sequence of this agarase gene showed 99% identity with the agaA gene from Janthinobacterium sp. SY12. It consists of a signal peptide, a glycoside hydrolase family 16 β-agarase domain and a carbohydrate-binding domain. The recombinant agarase was overexpressed and purified to homogeneity. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant enzyme were around 40℃ and 9.0. The enzyme was an endo-type β-agarase and hydrolyzed agarose to several oligosaccharides.
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Function of Global Regulator CodY in Bacillus thuringiensis BMB171 by Comparative Proteomic Analysis
( Ming Xia Qi ),( Fei Mei ),( Hui Wang ),( Ming Sun ),( Ge Jiao Wang ),( Ziniu Yu ),( Yeon Ho Je ),( Ming Shun Li ) 한국미생물 · 생명공학회 2015 Journal of microbiology and biotechnology Vol.25 No.2
CodY is a highly conserved protein in low G+C gram-positive bacteria that regulates genes involved in sporulation and stationary-phase adaptation. Bacillus thuringiensis is a grampositive bacterium that forms spores and parasporal crystals during the stationary phase. To our knowledge, the regulatory mechanism of CodY in B. thuringiensis is unknown. To study the function of CodY protein in B. thuringiensis, BMB171codY- was constructed in a BMB171 strain. A shuttle vector containing the ORF of cry1Ac10 was transformed into BMB171 and BMB171codY-, named BMB171cry1Ac and BMB171codY-cry1Ac, respectively. Some morphological and physiological changes of codY mutant BMB171codY-cry1Ac were observed. A comparative proteomic analysis was conducted for both BMB171codY-cry1Ac and BMB171cry1Ac through two-dimensional gel electrophoresis and MALDI-TOF-MS/MS analysis. The results showed that the proteins regulated by CodY are involved in microbial metabolism, including branched-chain amino acid metabolism, carbohydrate metabolism, fatty acid metabolism, and energy metabolism. Furthermore, we found CodY to be involved in sporulation, biosynthesis of poly-β-hydroxybutyrate, growth, genetic competence, and translation. According to the analysis of differentially expressed proteins, and physiological characterization of the codY mutant, we performed bacterial one-hybrid and electrophoretic mobility shift assay experiments and confirmed the direct regulation of genes by CodY, specifically those involved in metabolism of branched-chain amino acids, ribosomal recycling factor FRR, and the late competence protein ComER. Our data establish the foundation for in-depth study of the regulation of CodY in B. thuringiensis, and also offer a potential biocatalyst for functions of CodY in other bacteria.
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