A novel pathogenesis-related protein (SsPR10) from Solanum surattense with ribonucleolytic and antimicrobial activity is stress- and pathogen-inducible

A cDNA clone (designated as SsPR10, GenBank Accession Number AY660753 ) encoding a PR10 protein from yellow-fruit nightshade (Solanum surattense) was isolated and characterized. SsPR10 encoded a 160-amino-acid polypeptide with a predicted molecular mass of 17.58 kDa and pI of 5.29. Sequence alignments showed that SsPR10 had high identity (68.1%) with CaPR10, but had only about 31.7% identity with JIOsPR10 at the amino acid level. Genomic DNA gel blot analysis indicated that SsPR10 belonged to a multigene family. The constitutively expressed SsPR10 was detected to be the highest in roots of the sterile seedlings cultured in jars, while SsPR10 expression was the highest in old yellow leaves from the seedlings incubated with sap containing TMV. SsPR10 always expressed at slightly higher level in senescent leaves than in tender ones under both conditions. Further expression analysis revealed that the signaling components of defense/stress pathways (MeJA, SA, ABA, GA3, H2O2 and Cu2+) up-regulated significantly the SsPR10 mRNA levels over the control. However, darkness failed to induce SsPR10 expression and its expression was also inhibited by cold treatment. The SsPR10 was successfully expressed in Eschericha coli and the expressed protein was purified to near homogeneity. The dialytically renatured SsPR10 protein without phosphorylation exhibited ribonucleolytic activity against S. surattense leaf total RNA preparations and could inhibit hyphal growth of Pyricularia oryzae. Our findings suggest that the novel stress- and pathogen-inducible SsPR10 with ribonucleolytic and antimicrobial activity participates not only in the defense/stress response pathways but also in plants' growth, development and senescence.     

mAtNOS1 induces apoptosis of human mammary adenocarcinoma cells

mAtNOS1 is a novel gene recently reported in mammalian genome with functions that are not fully understood. The present study shows that in human mammary adenocarcinoma MCF-7 cells, mAtNOS1 expression increases mitochondrial nitric oxide and calcium. Our study further shows that overexpression of mAtNOS1 induces apoptosis in MCF-7 cells by increasing mitochondrial protein tyrosine nitration and cytochrome c release. The present study suggests a novel function for mAtNOS1 in regulating mitochondrial nitric oxide and calcium and inducing apoptosis of MCF-7 cells.     

Molecular Cloning and Characterization of a Mannose-binding Lectin Gene from Dendrobium officinale

Using RNA extracted from Dendrobium officinale young leaves and primers designed according to the conservative regions of Orchidaceae lectins, the full-length cDNA of Dendrobium officinale agglutinin (DOA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of doa was 768 bp and contained a 498 bp open reading frame (ORF) encoding a lectin precursor of 165 amino acids. Through comparative analysis of doa gene and its deduced amino acid sequence with those of other Orchidaceae species, it was found that doa encoded a precursor lectin with signal peptide. DOA was a mannose-binding lectin with three mannose-binding sites. Semi-quantitative RT-PCR analysis revealed that doa mRNA expression was detected in all tested tissues including root, stem and leaf, however, the expression was higher in stem, lower in leaf. As the doa mRNA was detected in all the tested plant tissues, the doa was considered to be a constitutively expressed gene.     

生物热分析研究 1.四种天然氨基酸热分解机理

本文采用热分析方法（ＴＧ,ＤＴＡ）和红外光谱等手段,对四种天然氨基酸（盐酸赖氨基酸,色氨酸,天门冬氨酸,苯丙氨酸）的热稳定性和热分解机理进行了研究,发现这四种天然氨基酸热分解的共同特点是首先失去羧基,形成胺的中间产物,然后是中间产物分解,且脱羧温度与β位碳原子上所连的基团密切相关,从电荷密度等因素出发对此进行了分析和讨论。     

北带马尾松毛虫灾害发生级别的气候因子预报模型研究

以河南省四县马毛尾松毛虫灾害20多年的观测数据及相应27项气象资料为研究材料,采用双重筛选逐步回归的方法,通过计算机处理,建立了15个我国北带马尾松毛虫灾害的预报模型．经回测历史符合率为60％～90％．本研究的创新在于以方差为权重客观地将三个预报指标加权平均为一个综合指标,并据此划分出灾害的3个等级,使其更具科学性．     

中华山蝠翼的形态学发育模式

为了揭示中华山蝠翼的形态学发育模式,2012-2014年, 通过对50只中华山蝠幼蝠进行人工饲养实验观察及测量,辅以野外标志重捕,研究中华山蝠翼的生长。结果显示：中华山蝠翼外形各量度值先呈直线增长,后增长速度逐渐减慢。各指标增长速度减慢的日龄各不相同,臂膜长在25日龄生长速度逐渐减慢;翼展、翼面积、臂膜面积在30日龄增长速度减慢;掌膜长及掌膜面积则在40日龄增长速度减慢。臂膜长发育最快,试飞前 (28日龄) 已达到成体臂膜长的80.9%。翼载在幼蝠生后14日龄内呈直线增长,然后开始直线下降,到试飞期 (35日龄左右),翼载值降到最低,是成体翼载的80.0%,此后呈极缓慢增长趋势。中华山蝠翼的生长主要集中在试飞前。试飞后,则通过减缓体重的增长速度甚至减轻体重,保持翼面积尤其是掌膜面积的增长速度,从而降低翼载,以便更快地适应飞行生活。Logistic, Von Bertalanffy和Gompertz 3种非线性曲线中,Gompertz模型对翼展拟合度最佳,Gompertz和Von Bertalanffy模型对翼面积拟合度优于Logistic曲线。     

Molecular cloning of BPL1, a pectate lyase-like gene in Brassica napus

Pectate lyase (EC 4.2.2.2) is an enzyme involved in the maceration and soft rotting of plant tissue via degradation of cell wall in organisms. Plants as well as bacteria and fungi are capable of producing pectate lyases. Here we report the cloning of a novel full-length cDNA of pectate lyase gene, designated BPL1, from Brassica napus by rapid amplification of cDNA ends. BPL1 cDNA is 1787 bp containing a 1503 bp ORF encoding a 500 amino acid protein precursor. The protein precursor has a potential signal peptide with 22 amino acids. Alignment of sequences shows that there are some extremely conserved amino acids among pectate lyase-like proteins from different plant species, and novel C-terminal domains are found in Arabidopsis and Brassica. Phylogenetic analysis of 50 pectate lyase-like proteins from various species demonstrates the obvious distinction among pectate lyase-like proteins from plants, bacteria and fungi, which are subsequently clustered into three groups. The cloning of BPL1 enables us to explore its diverse roles in higher plants and potential application in crop improvement.     

cDNA cloning and characterization of a mannose-binding lectin fromZingiber officinaleRoscoe (ginger) rhizomes

Using RNA extracted fromZingiber officinale rhizomes and primers designed according to the conservative regions of monocot mannose-binding lectins, the full-length cDNA ofZ. officinale agglutinin (ZOA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA ofzoa was 746 bp and contained a 510 bp open reading frame (ORF) encoding a lectin precursor of 169 amino acids with a signal peptide. ZOA was a mannose-binding lectin with three typical mannose-binding sites (QDNY). Semi-quantitative RT-PCR analysis revealed thatzoa expressed in all the tested tissues ofZ. officinale including leaf, root and rhizome, suggesting it to be a constitutively expressing form. ZOA protein was successfully expressed inEscherichia coli with the molecular weight expected. To our knowledge, this is the first mannose-binding lectin cDNA cloned from the family Zingiberaceae. Our results demonstrate that monocot mannose-binding lectins also occur within the family Zingiberaceae