Role of Drosophila gene dunc-115 in nervous system

Axonal guidance signals are transduced through growth cone surface receptors to the interior leading to changes of actin dynamics and actin binding proteins, which are critical in determining the outcome of actin cytoskeleton reorganization. We report here the characterization of the Drosophila actin binding protein abLIM/Unc-115 homolog Dunc-115 and its role in the nervous system. Three Dunc-115 isoforms are identified as Dunc-115L, M and S, respectively. While Dunc-115L is a canonical homolog of Unc-115 with four LIM domains and one villin headpiece domain, Dunc-115M and S are novel isoforms without counterparts in other species. Our molecular modeling shows Dunc-115L is likely to bind to actin. Mutant analysis reveals that Dunc-115 is involved in axonal projection in both the visual and central nervous system.     

刺枝野丁香和穗花野丁香(茜草科)名称之合格发表

刺枝野丁香Leptodermis pilosa Diels var．acanthoclada Lo和穗花野丁香L．pilosa Diels vat．spicatiformis Lo发表时没指明模式,是不合格发表的名称。现通过指定模式,将它们的名称作合格发表。还对此2新变种及其近缘类群提供了分类检索表和地理分布图。     

关于木本石松植物鳞皮木属的正确名称

讨论了木本石松植物鳞皮木属Lepidophloios Stemberg的正确名称。基于Stemberg 1825年的原始描述和相关文献以及模式标本,Lepidophloios实际上是一个晚出的拼写变体,它的原始拼写为Lepidopfloyos。根据《国际植物命名法规》（维也纳法规规则60．1和61．1）,Lepidofloys Stemberg应该是鳞皮木属的正确名称。作者给出了鳞皮木属模式标本的图片和描述。     

六个石蒜居群的核型及四倍体石蒜的发现

染色体与核型的变化是植物系统发育和进化的一个重要方面。石蒜属Lycoris植物特别是石蒜L.radiata在染色体数目和核型上存在较大的变异。通过对不同居群的石蒜核型研究,可以为石蒜和石蒜属植物的核型演化及演化机制提供一些重要的基础资料。本文对分布于中国安徽省和浙江省的6个石蒜居群进行了细胞学研究。结果表明,6个石蒜居群的染色体数目和核型分别为：霍山居群2n=44=28st＋8t＋8T,2n=22=6st＋12t＋4T;黄山居群2n=22=22t,2n=22=18st＋4t,2n=21=12st＋7t＋2T;滁州居群2n=33=33t;马鞍山居群2n=33=18st＋15T,2n=25=1m＋20st＋2t＋2T;宣城居群2n=22=20st＋2T,2n=21=1m＋20st;杭州居群2n=22=12st＋4t＋6T,2n=21=18st＋3t。其中,部分居群的核型类型为首次报道;并首次发现了四倍体的石蒜居群。此外,对石蒜的核型进化和多倍体起源进行了初步探讨。     

植物病毒诱导的基因沉默效应的分子机制

主要从病毒诱导的基因沉默体系中植物与病毒的相互作用、VIGS涉及的信号分子和移动方式以及靶基因的沉默和病毒载体的复制关系介绍和分析植物病毒诱导的基因沉默效应的分子机制,并进一步分析此种体系在植物基因功能研究中应用的研究进展。     

beta-sitosterol decreases irradiation-induced thymocyte early damage by regulation of the intracellular redox balance and maintenance of mitochondrial membrane stability

Both radiation injury and oxidation toxicity occur when cells are exposed to ion irradiation (IR), ultimately leading to apoptosis. This study was designed to determine the effect of beta-sitosterol (BSS) on early cellular damage in irradiated thymocytes and a possible mechanism of effect on irradiation-mediated activation of the apoptotic pathways. Thymocytes were irradiated (6 Gy) with or without BSS. Cell apoptosis and apoptosis-related proteins were evaluated. BSS decreased irradiation-induced cell death and nuclear DNA strand breaks while attenuating intracellular reactive oxygen species (ROS) and increasing the activities of antioxidant enzymes, including superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx). BSS decreased the release of cytochrome c from mitochondria to the cytosol and the mitochondrio-nuclear translocation of apoptosis-inducing factor (AIF). Furthermore, BSS partially inhibited the radiation-induced increase of cleaved caspase 3 and cleaved PARP, and attenuated the activation of JNK and AP-1. In addition, evidence suggests that ROS generated by irradiation are involved in this course of cell damage. The results indicate that BSS confers a radioprotective effect on thymocytes by regulation of the intracellular redox balance which is carried out via the scavenging of ROS and maintenance of mitochondrial membrane stability.     

Essential dynamics sampling study of adenylate kinase: comparison to citrate synthase and implication for the hinge and shear mechanisms of domain motions

Essential dynamics sampling simulations of the domain conformations of unliganded Escherichia coli adenylate kinase have been performed to determine whether the ligand-induced closed-domain conformation is accessible to the open unliganded enzyme. Adenylate kinase is a three- domain protein with a central CORE domain and twoflanking domains, the LID and the NMPbind domains. The sampling simulations were applied to the CORE and NMPbind domain pair and the CORE and LID domain pair separately. One aim is to compare the results to those of a similar study on the enzyme citrate synthase to determine whether a similar domain-locking mechanism operates in adenylate kinase. Although for adenylate kinase the simulations suggest that the closed-domain conformation of the unliganded enzyme is at a slightly higher free energy than the open for both domain pairs, the results are radically different to those found for citrate synthase. In adenylate kinase the targeted domain conformations could always be achieved, whereas this was not the case in citrate synthase due to an apparent free-energy barrier between the open and closed conformations. Adenylate kinase has been classified as a protein that undergoes closure through a hinge mechanism, whereas citrate synthase has been assigned to the shear mechanism. This was quantified here in terms of the change in the number of interdomain contacting atoms upon closure which showed a considerable increase in adenylate kinase. For citrate synthase this number remained largely the same, suggesting that the domain faces slide over each other during closure. This suggests that shear and hinge mechanisms of domain closure may relate to the existence or absence of an appreciable barrier to closure for the unliganded protein, as the latter can hinge comparatively freely, whereas the former must follow a more constrained path. In general though it appears a bias toward keeping the unliganded enzyme in the open-domain conformation may be a common feature of domain enzymes.     

Hydrolase-catalyzed Michael addition of 1,3-dicarbonyl compounds to α,β-unsaturated compounds in organic solvent

A novel strategy to perform Michael additions between 1,3-dicarbonyl compounds and α,β-unsaturated compounds was developed by the catalysis of hydrolase. We found that 11 hydrolase could catalyze the enzymatic Michael addition reaction to form the carbon–carbon bond. In 2-methyl-2-butanol d-aminoacylase showed high Michael addition activity. The influence of substrate and Michael acceptor structure on Michael addition was evaluated systematically. Some control experiments demonstrated that the active site of d-aminoacylase was responsible for the enzymatic Michael addition reaction. This novel Michael addition activity of hydrolase is of practical significance in expanding the application of enzymes and in the evolution of new biocatalysts.