海马内生长抑素与γ－氨基丁酸在大鼠穿梭箱主动回避反应中的作用

本实验以大鼠穿梭箱主动回避反应（ＡＡＲ）的习得和消退为学习记忆的指标,研究了海马内生长抑素（ＳＳ）和γ－氨基丁酸（ＧＡＢＡ）在学习记忆中的作用。结果如下：（１）经训练而建立了ＡＡＲ的大鼠,其海马内ＳＳ较对照组显著增高,而海马内ＧＡＢＡ含量却明显降低;（２）海马内注入ＳＳ的耗竭剂半胱胺（Ｃｙｓ,２０ｇ／Ｌ）使大鼠ＡＡＲ的习得受到明显损害,ＡＡＲ的消退显著加速,海马内ＳＳ明显降低,而ＧＡＢＡ含量却显著升高;（３）海马内注入ＧＡＢＡ（２００ｇ／Ｌ）使大鼠ＡＡＲ的消退显著加速的同时,其海马内ＳＳ含量亦显著降低。由此表明,海马内ＳＳ可能有促进学习记忆的作用,而海马内ＧＡＢＡ升高则有相反的效应;二者在海马调控学习记忆过程中具有重要作用。     

大兴安岭天然沼泽湿地生态系统碳储量

采用碳/氮分析仪测定法与标准木解析法,研究大兴安岭5种典型天然沼泽湿地(草丛沼泽、灌丛沼泽、毛赤杨沼泽、白桦沼泽和落叶松沼泽)的生态系统碳储量(植被和土壤)、净初级生产力、植被年净固碳量及其沿沼泽至森林方向过渡带水分环境梯度的分布格局,揭示其空间变异规律性,并定量评价寒温带5种典型天然沼泽湿地的碳储量与固碳能力及其长期碳汇作用。结果表明:①5种天然沼泽湿地的植被碳储量分布在(0.48±0.08)—(8.33±0.66)kgC/m2之间,沿过渡带环境梯度呈递增趋势;②土壤碳储量分布在(19.21±6.17)—(38.28±4.86)kgC/m2之间,沿过渡带环境梯度却呈递减趋势;③生态系统碳储量分布在(27.54±7.16)—(38.76±4.58)kgC/m2之间,沿过渡带环境梯度基本呈恒定分布规律性,且以湿地土壤碳储量占优势地位(69.8%—98.8%);④植被净初级生产力分布在(0.68±0.10)—(1.08±0.12)kg.m-.2a-1之间,毛赤杨沼泽最高,草丛沼泽、灌丛沼泽、白桦沼泽居中,落叶松沼泽最低,且总体上低于温带森林湿地而高于寒温带天然落叶松林;⑤植被年净固碳量分布在(0.32±0.09)—(0.51±0.06)kgC.m-.2a-1,毛赤杨沼泽最高(高于全球植被平均年净固碳量)、灌丛沼泽和白桦沼泽居中(达到或接近全球平均值)、草丛沼泽和落叶松沼泽最低(略低于全球平均值),故这5种沼泽湿地均属于碳汇功能相对较强的湿地植被类型。     

白细胞介素2亲和性配体的筛选

白细胞介素2(IL-2)及其受体拮抗剂的研究对免疫抑制药物的研制具有重要作用.抗白细胞介素2受体α链中和性单克隆抗体5G1(抗Tac型抗体)能够特异性地阻断IL-2与其受体的结合.因此,5G1可作为目标分子被用来在噬菌体展示肽库中筛选白细胞介素2的亲和性配体.经过4轮亲和性筛选以及5G1亲和活性的测定,6个具有明显5G1亲和活性的噬菌体克隆被发现.DNA序列分析结果显示出,所得到的肽序列具有明显的保守性,即SSFT(L/P)I.该序列与IL-2受体α链没有同源性.因此,SSFT(L/P)I可能模拟了IL-2受体α链上的一个不连续表位(mimotope),为白细胞介素2亲和性配体片段.     

肝脏发育相关信号通路

肝脏发育从肝芽的出现开始,到肝祖细胞的形成,接着肝祖细胞的增殖、分化和迁移,直至最后器官的形成,经历了复杂的细胞信号调控过程。本文综述了肝脏发育过程中常见的信号调控作用,包括成纤维生长因子(fibroblast growth factor,FGF)、骨形态发生蛋白(bone morphogenetic protein,BMP)、β-转化生长因子(transforming growth factor-β,TGF-β)、肝细胞生长因子(hepatocyte growth factor,HGF)和Wnt等信号通路,并重点讨论了在胚胎阶段调控肝脏发育的信号途径以及肝细胞和胆管细胞发育成熟过程中的信号因子作用,最后对肝脏再生相关的信号调控进行了简要介绍。     

火干扰对小兴安岭毛赤杨沼泽温室气体排放动态影响及其影响因素

利用静态箱-气相色谱法,对小兴安岭轻度火烧毛赤杨沼泽CH4、CO2、N2O生长季排放通量进行研究.结果表明:火烧使毛赤杨沼泽生长季CH4排放通量提高485.2％,CO2和N2O排放通量分别下降45.5％、24.8％.火烧未改变CH4季节性排放规律,但改变了CO2、N2O季节性变化规律.火烧样地CH4排放通量与土壤15cm温度间存在显著正相关性关系而与水位相关性不显著,火烧样地CO2排放与土壤0-30 cm温度呈显著或极显著正相关,与水位极显著负相关.对照样地CO2排放通量与土壤0-15 cm温度呈显著或极显著正相关,与水位极显著负相关,火烧使毛赤杨沼泽CH4排放源的强度增强,CO2、N2O的排放消弱,全球温室潜势下降约为43.34％.     

The use of SARS-CoV-2-related coronaviruses from bats and pangolins to polarize mutations in SARS-Cov-2

正Dear Editor,The coronavirus disease 2019 (COVID-19) caused by the SARS-CoV-2 coronavirus has become a global pandemic.The SARS-CoV-2 genome has a similarity of 96.2%to that of RaTG13, a bat SARS-CoV-2-related coronavirus detected in Rhinolophus affinis (Paraskevis et al., 2020; Zhou et al.,2020). The SARS-CoV-2 genome also has 85.5%-92.4%     

ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity,and D1 contributes to the heat-induced activity

The 97-kDa valosin-containing protein (p97-VCP) plays a role in a wide variety of cellular activities, many of which are regulated by the ubiquitin-proteasome (Ub-Pr)-mediated degradation pathway. We previously demonstrated that VCP binds to multi-ubiquitin chains and may act as a molecular chaperone that targets the ubiquitinated substrates to the proteasome for degradation. In this report, we show that although the ubiquitin chain-binding activity, carried out by the N-terminal 200 residues (N domain), is necessary for the degradation of proteasome substrates, it is not sufficient. Using in vitro degradation assays, we demonstrated that the entire VCP molecule, consisting of the N domain and two ATPase domains D1 and D2, is required for mediating the Ub-Pr degradation. The ATPase activity of VCP requires Mg(2+), and is stimulated by high temperature. Under optimal conditions, VCP hydrolyzes ATP with a K(m) of approximately 0.33 mm and a V(max) of approximately 0.52 nmol P(i) min(-1) microg(-1). At a physiological temperature, mutation in D2 significantly inhibits the ATPase activity, while that in D1 has little effect. Interestingly, mutations in D1, but not D2, abolish the heat-stimulated ATPase activity. Thus, we provide the first demonstration that the ATPase activity of VCP is required for mediating the Ub-Pr degradation, that D2 accounts for the major ATPase activity, and that D1 contributes to the heat-induced activity.     

Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7

CNAP1 (hCAP-D2/Eg7) is an essential component of the human condensin complex required for mitotic chromosome condensation. This conserved complex contains a structural maintenance of chromosomes (SMC) family protein heterodimer and three non-SMC subunits. The mechanism underlying condensin targeting to mitotic chromosomes and the role played by the individual condensin components, particularly the non-SMC subunits, are not well understood. We report here characterization of the non-SMC condensin component CNAP1. CNAP1 contains two separate domains required for its stable incorporation into the complex. We found that the carboxyl terminus of CNAP1 possesses a mitotic chromosome-targeting domain that does not require the other condensin components. The same region also contains a functional bipartite nuclear localization signal. A mutant CNAP1 missing this domain, although still incorporated into condensin, was unable to associate with mitotic chromosomes. Successful chromosome targeting of deletion mutants correlated with their ability to directly bind to histones H1 and H3 in vitro. The H3 interaction appears to be mediated through the H3 histone tail, and a subfragment containing the targeting domain was found to interact with histone H3 in vivo. Thus, the CNAP1 C-terminal region defines a novel histone-binding domain that is responsible for targeting CNAP1, and possibly condensin, to mitotic chromosomes.     

A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis

In eukaryotes, enzymes of different subcellular compartments participate in the assembly of membrane lipids. As a consequence, interorganelle lipid transfer is extensive in growing cells. A prominent example is the transfer of membrane lipid precursors between the endoplasmic reticulum (ER) and the photosynthetic thylakoid membranes in plants. Mono- and digalactolipids are typical photosynthetic membrane lipids. In Arabidopsis, they are derived from one of two pathways, either synthesized de novo in the plastid, or precursors are imported from the ER, giving rise to distinct molecular species. Employing a high-throughput robotic screening procedure generating arrays of spot chromatograms, mutants of Arabidopsis were isolated, which accumulated unusual trigalactolipids. In one allelic mutant subclass, trigalactosyldiacylglycerol1, the primary defect caused a disruption in the biosynthesis of ER-derived thylakoid lipids. Secondarily, a processive galactosyltransferase was activated, leading to the accumulation of oligogalactolipids. Mutations in a permease-like protein of the outer chloroplastic envelope are responsible for the primary biochemical defect. It is proposed that this protein is part of a lipid transfer complex.