利用定点突变分析白念珠菌依赖铁基因FRP1启动子元件

通过对白念珠菌高铁还原酶基因FRP1启动子进行突变分析, 确认启动子中特殊调控元件。我们通过分析FRP1起始密码子上游1000 bp序列发现在-160 和-650处有2个推测的Rim101p结合位点, 对其分别进行定点突变, 然后构建启动子与报告基因LacZ融合质粒, 转化整合到白念珠菌rim101-/-株和野生株中, 检测不同缺铁条件下b-半乳糖苷酶活性。结果发现碱性条件, Rim101p能够正向调控FRP1的表达; 启动子-160处突变对启动子功能影响较弱, 而-650突变使启动子活性大大降低, 此结果和双突变的结果相同, 表明Rim101p主要通过与启动子-650处结合位点相互作用来调控FRP1的表达。     

小果博落回中2种杀虫活性成分的分离及鉴定

以粘虫(Mythimna separata)3龄幼虫为试虫,采用生物活性示踪法从小果博落回(Macleaya microcarpa)乙醇提取物中分离纯化出2种活性成分,经MS1、H-NMR1、3C-NMR分析鉴定为二氢血根碱和二氢白屈菜红碱。采用小叶碟添加法测试了2种化合物对粘虫3龄幼虫的拒食及毒杀活性。结果表明,2种化合物对粘虫3龄幼虫均具有较高的拒食活性,48 h的拒食AFC50分别为0.168和0.231 mg.mL-1,同时,二氢血根碱对粘虫3龄幼虫具有一定的毒杀活性,96 h的LC50为0.085 mg.mL-1。分析认为二氢血根碱可能是小果博落回的主要杀虫活性成分之一。     

披碱草与新麦草属间杂种的细胞遗传学研究

将澳大利亚披碱草(Elymus scabervar.scaber,2n=6x=42,StYW)和华山新麦草(Psathyrostachys huas-hanica,2n=2x=14,Ns)进行属间杂交,成功获得杂种F1。分析亲本及其杂种F1的形态特征、繁育特性及花粉母细胞减数分裂染色体配对行为发现:杂种F1形态特征介于父母本之间,分蘖数等农艺性状超过双亲;花粉完全不育,结实率为0。亲本减数分裂染色体配对正常,但杂种F1花粉母细胞在减数分裂中期I染色体几乎没有配对,其构型为:27.31Ⅰ 0.01Ⅱ(环) 0.32Ⅱ(棒) 0.01Ⅲ,C值仅为0.01。以上结果表明:澳大利亚披碱草的StYW染色体组与华山新麦草的Ns染色体组间无同源性,它们之间的亲缘关系甚远。     

Hypoxia-inducible factor-1 and nuclear factor-kappaB inhibitory meroterpene analogues of bakuchiol, a constituent of the seeds of Psoralea corylifolia

Two new meroterpenoids, 12,13-dihydro-12,13-dihydroxybakuchiol (2) and (12'S)-bisbakuchiol C (3), were isolated from the seeds of Psoralea corylifolia L. (Fabaceae). The structures of 2 and 3 were elucidated by spectroscopic and chemical methods. Six meroterpenoids isolated from P. corylifolia and three semi-synthetic analogues were evaluated for HIF-1 and NF-kappaB inhibition, and O-methyl and O-ethylbakuchiols (6 and 7) inhibited HIF-1 and NF-kappaB activation without significantly decreasing the viability of the AGS and HeLa cells, respectively.     

The structure-based design, synthesis and biological evaluation of DNA-binding bisintercalating bisanthrapyrazole anticancer compounds

Anticancer drugs that bind to DNA and inhibit DNA-processing enzymes represent an important class of anticancer drugs. In order to find stronger DNA binding and more potent cytotoxic compounds, a series of ester-coupled bisanthrapyrazole derivatives of 7-chloro-2-[2-[(2-hydroxyethyl)methylamino]ethyl]anthra[1,9-cd]pyrazol-6(2H)-one (AP9) were designed and evaluated by molecular docking techniques. Because the anthrapyrazoles are unable to be reductively activated like doxorubicin and other anthracyclines, they should not be cardiotoxic like the anthracyclines. Based on the docking scores of a series of bisanthrapyrazoles with different numbers of methylene linkers (n) that were docked into an X-ray structure of double-stranded DNA, five bisanthrapyrazoles (n=1-5) were selected for synthesis and physical and biological evaluation. The synthesized compounds were evaluated for DNA binding and bisintercalation by measuring the DNA melting temperature increase, for growth inhibitory effects on the human erythroleukemic K562 cell line, and for DNA topoisomerase IIalpha-mediated cleavage of DNA and inhibition of DNA topoisomerase IIalpha decatenation activities. The results suggest that the bisanthrapyrazoles with n=2-5 formed bisintercalation complexes with DNA. In conclusion, a novel group of bisintercalating anthrapyrazole compounds have been designed, synthesized and biologically evaluated as possible anticancer agents.     

植物丝氨酸/精氨酸丰富(SR)蛋白的结构和功能及其在植物发育中的作用

丝氨酸／精氨酸丰富（SR）蛋白家族是真核生物中的一类剪接因子,在前体mRNA的组成性和选择性剪接中起作用。本文就近十几年来SR蛋白结构和功能及其在植物发育中的作用的研究进展作以介绍。     

UBE1DC1, an ubiquitin-activating enzyme, activates two different ubiquitin-like proteins

Ubiquitin and ubiquitin-like proteins are known to be covalently conjugated to a variety of cellular substrates via a three-step enzymatic pathway. These modifications lead to the degradation of substrates or change its functional status. The ubiquitin-activating enzyme (E1) plays a key role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. Ubiquitin-activating enzyme E1-domain containing 1 (UBE1DC1) had been proved to activate an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. In this report, UBE1DC1 is proved to activate another ubiquitin-like protein, SUMO2, besides Ufm1, both in vitro and in vivo by immunological analysis. It indicated that UBE1DC1 could activate two different ubiquitin-like proteins, SUMO2 and Ufm1, which have no significant similarity with each other. Subcellular localization in AD293 cells revealed that UBE1DC1 was especially distributed in the cytoplasm; whereas UBE1DC1 was mainly distributed in the nucleus when was cotransfected with SUMO2. It presumed that UBE1DC1 greatly activated SUMO2 in the nucleus or transferred activated-SUMO2 to nucleus after it conjugated SUMO2 in the cytoplasm.