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Alu Tandem Sequences Inhibit GFP Gene Expression by Triggering Chromatin Wrapping
Xiu Fang Wang,Xiao Yan Wang,Jing Liu,Jing Jing Feng,Wen Li Mu,Xiao Juan Shi,Qin Qing Yang,Xiao Cui Duan,Ying Xie,Zhan Jun Lu 한국유전학회 2009 Genes & Genomics Vol.31 No.3
Alu elements belonging to the short interspersed nuclear elements (SINE) of repetitive elements are present in more than one million copies which altogether represent 10% of the whole human genome. In this study, the roles of Alu tandem sequences in the process of GFP gene (GFP) expression and packing into chromatin of its DNA were studied. To detect the effect of Alu repeats on gene expression, different copies of Alus were inserted GFP downstream respectively in pEGFP-C1 vector. We found that Alu sequences decreased the amount of GFP transcription, the percentage of GFP positive cells and the accessibility to DNase I in length-dependent manner. Inserting Alu caused the production of higher-molecular-mass RNA, indicating Alu sequence did not induce premature transcriptional termination. Tight packing chromatins keep silent and resist to DNase I digestion, which is a general phenomenon. We suggested that head and tail tandem Alu sequences suppressed GFP expression in length dependent manner by triggering chromatin packing.
Zhan-qing Zhang,Yan-bing Wang,,Wei Lu,,Dan-ping Liu,,Bi-sheng Shi,,Xiao-nan Zhang,,Dan Huang,,Xiu-fen Li,,Xin-lan Zhou,,Rong-rong Ding, 대한진단검사의학회 2019 Annals of Laboratory Medicine Vol.39 No.1
Background: We examined changes in hepatitis B core-related antigen (HBcrAg) during the four sequential phases of chronic hepatitis B virus (HBV) infection: hepatitis B e antigen (HBeAg)-positive chronic infection (EPCI) and hepatitis (EPCH), followed by HBeAg-negative chronic infection (ENCI) and hepatitis (ENCH). We compared the performance of serum HBcrAg, hepatitis B surface antigen (HBsAg), and HBV DNA in predicting EPCH and ENCH.
Hong-tao Chang,Xiu-yuan He,Yu-Feng Liu,Lu Chen,Quan-hai Guo,Qiu-ying Yu,Jun Zhao,Xin-wei Wang,Xia Yang,Chuan-qing Wang 대한수의학회 2014 Journal of Veterinary Science Vol.15 No.3
A recombinant replication-defective adenovirus expressingthe major epitopes of porcine circovirus-2 (PCV-2) capsidprotein (rAd/Cap/518) was previously constructed and shownto induce mucosal immunity in mice following intranasaldelivery. In the present study, immune responses induced byintranasal immunization with a combination of rAd/Cap/518and cytosine-phosphate-guanosine oligodeoxynucleotides(CpG ODN) were evaluated in mice. The levels ofPCV-2-specific IgG in serum and IgA in saliva, lung, andintestinal fluids were significantly higher in the groupimmunized with rAd/Cap/518 and CpG ODN than animalsimmunized with rAd/Cap/518 alone. The frequencies ofIL-2-secreting CD4+ T cells and IFN-γ-producing CD8+ T cellswere significantly higher in the combined immunizationgroup than mice immunized with rAd/Cap/518 alone. Thefrequencies of CD3+, CD3+CD4+CD8−, and CD3+CD4−CD8+T cells in the combined immunization group were similar tothat treated with CpG ODN alone, but significantly higherthan mice that did not receive CpG ODN. PCV-2 load afterchallenge in the combined immunization group wassignificantly lower than that in the phosphate-buffered salineplacebo group and approximately 7-fold lower in the grouptreated with CpG ODN alone. These results indicate thatrAd/Cap/518 combined with CpG ODN can enhance systemicand local mucosal immunity in mice, and represent apromising synergetic mucosal vaccine against PCV-2.
( Hong Chen Zheng ),( Ming Zhe Sun ),( Ling Cai Meng ),( Hai Sheng Pei ),( Xiu Qing Zhang ),( Zheng Yan ),( Wen Hui Zeng ),( Jing Sheng Zhang ),( Jin Rong Hu ),( Fu Ping Lu ),( Jun She Sun ) 한국미생물 · 생명공학회 2014 Journal of microbiology and biotechnology Vol.24 No.4
High levels of extracellular xylanase activity (211.79 IU/mg) produced by Paenibacillus sp. NF1 were detected when it was submerged-cultured. After three consecutive purification steps using Octyl-Sepharose, Sephadex G75, and Q-Sepharose columns, a thermostable xylanase (XynNF) was purified to homogeneity and showed a molecular mass of 37 kDa according to SDS-PAGE. The specific activity of the purified XynNF was up to 3,081.05 IU/mg with a 14.55-fold purification. The activity of XynNF was stimulated by Ca2+, Ba2+, DTT, and β-mercaptoethanol, but was inhibited by Fe3+, Zn2+, Fe2+, Cu2+, SDS, and EDTA. The purified XynNF displayed a greater affinity for oat spelt xylan with the maximal enzymatic activity at 60°C and pH 6.0. XynNF, which was shown to be cellulose-free, with high stability at high temperature (70°C-80°C) and low pH range (pH 4.0-7.0), is potentially valuable for various industrial applications. The enzyme hydrolyzed oat spelt xylan to yield mainly xylooligosaccharides (95.8%) of 2-4 degree of polymerization (DP2-4). Moreover, the majority of the xylooligosacharides (DP2- 4) products was xylobiose (61.5%). The thermostable xylanase (XynNF) thus seems potentially usefull in the production of xylooligosaccharides.