两系杂交小麦恢复系MR168抗条锈病基因遗传分析及分子标记定位

小麦条锈病是影响杂交小麦普及推广的重要因素。文章利用基因推导法和SSR分子标记技术,研究了温光型两系杂交小麦恢复系MR168的抗条锈性遗传规律及其控制基因染色体位置。结果表明,MR168对CY29、CY31、CY32、CY33等条锈菌生理小种表现高抗至免疫;对SY95-71/MR168杂交组合的正反交F1、BC1、F2和F3群体分单株接种鉴定显示,MR168对CY32号小种的抗性受1对显性核基因控制,该抗病基因来源于春小麦品种辽春10号。利用集群分离分析法(Bulked segregant analysis,BSA)和简单重复序列(Simple sequence repeat,SSR)分子标记分析抗病亲本MR168、感病亲本SY95-71及183个F2代单株,发现了与MR168抗条锈病基因连锁的5个微卫星标记Xgwm273、Xgwm18、Xbarc187、Xwmc269、Xwmc406,并将该基因初步定位在1BS着丝粒附近,暂命名为YrMR168;构建了包含YrMR168的SSR标记遗传图谱,距离YrMR168最近的两个微卫星位点是Xgwm18和Xbarc187,遗传距离分别为1.9 cM和2.4 cM,这两个微卫星标记可用于杂交小麦抗条锈病分子标记辅助育种。     

水曲柳大孢子发生及雌配子体发育的研究

水曲柳（ＦｒａｘｉｎｕｓｍａｎｄｓｈｕｉｃａＲｕｐｒ．）子房为二心皮;二室,中轴胎座,每室内具二个倒生胚珠,薄珠心,单珠被。单个孢原细胞分化于珠心顶端表皮之下,直接发育成为大孢子母细胞,大孢子四分体为直线形,通常为合点端第一大孢子具功能,胆囊发育为蓼型。     

3种阴生地被植物对SO_2胁迫的生理响应及净化能力

该研究以3种阴生地被植物麦冬、虎耳草和紫萼玉簪为研究材料,采用人工模拟熏气方法,测定不同浓度(5.71,11.43,17.14,22.86mg·m~(-3))SO_2胁迫下参试植物的外观受害症状,以及膜质过氧化、保护酶活性、渗透调节物质等生理指标,以叶片吸硫量比较3种植物的净化能力,并采用模糊数学隶属函数与主成分分析法对其抗SO_2能力进行综合评价。结果显示:(1)随着SO_2熏气浓度的升高,3种植物的叶片都有不同程度的受害症状,叶片叶绿素含量、汁液pH值和相对含水量下降,丙二醛含量、叶片相对电导率、可溶性糖、游离脯氨酸含量上升,且其SOD和CAT活性显著增强。(2)隶属函数法和主成分分析法综合评定结果显示,3种地被植物对SO_2抗性能力表现为:麦冬紫萼玉簪虎耳草,与叶片受伤害症状和叶液pH值下降的顺序相反,说明这2个指标可作为简单可行的评价SO_2抗性的重要鉴定指标。(3)3种植物均有一定的SO_2净化能力,其强弱顺序为虎耳草麦冬紫萼玉簪。研究表明,3种阴生地被植物都能够在SO_2胁迫下提高其保护酶活性和渗透调节物质含量,增强其抗硫胁迫和SO_2吸收能力,并以麦冬对SO_2抗性最强,虎耳草对SO_2的吸收能力最强;该试验中最低参试SO_2浓度远远高于城市大气中的实际SO_2浓度,在试验环境下3种阴生植物再都未呈现伤害症状,说明吸收硫能力强的虎耳草和麦冬可以在SO_2污染严重的林下区域大面积应用推广。     

Natural patterns of activity and long-term synaptic plasticity

Long-term potentiation (LTP) of synaptic transmission is traditionally elicited by massively synchronous, high-frequency inputs, which rarely occur naturally. Recent in vitro experiments have revealed that both LTP and long-term depression (LTD) can arise by appropriately pairing weak synaptic inputs with action potentials in the postsynaptic cell. This discovery has generated new insights into the conditions under which synaptic modification may occur in pyramidal neurons in vivo. First, it has been shown that the temporal order of the synaptic input and the postsynaptic spike within a narrow temporal window determines whether LTP or LTD is elicited, according to a temporally asymmetric Hebbian learning rule. Second, backpropagating action potentials are able to serve as a global signal for synaptic plasticity in a neuron compared with local associative interactions between synaptic inputs on dendrites. Third, a specific temporal pattern of activity--postsynaptic bursting--accompanies synaptic potentiation in adults.     

Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1)

S6K1 is a member of the AGC subfamily of serine-threonine protein kinases, whereby catalytic activation requires dual phosphorylation of critical residues in the conserved T-loop (T229) and hydrophobic motif (HM; T389) peptide regions of its catalytic kinase domain (residues 1-398). In addition to its kinase domain, S6K1 contains a C-terminal autoinhibitory domain (AID; residues 399-502), which prevents T-loop and HM phosphorylation; and autoinhibition is relieved on multi-site Ser-Thr phosphorylation of the AID (S411, S418, T421, and S424). Interestingly, 66 of the 104 C-terminal AID amino acid residues were computer predicted to exist in structurally disordered peptide regions, begetting interest as to how such dynamics could be coupled to autoregulation. To begin addressing this issue, we developed and optimized protocols for efficient AID expression and purification. Consistent with computer predictions, aberrant mobilities in both SDS-PAGE and size-exclusion chromatography, as well as low chemical shift dispersion in (1)H-(15)N HSQC NMR spectra, indicated purified recombinant AID to be largely unfolded. Yet, trans-addition of purified AID effectively inhibited PDK1-catalyzed T-loop phosphorylation of a catalytic kinase domain construct of S6K1. Using an identical purification protocol, similar protein yields of a tetraphospho-mimic mutant AID(D(2)ED) construct were obtained; and this construct displayed only weak inhibition of PDK1-catalyzed T229 phosphorylation. Purification of the structurally 'disordered' and functional C-terminal AID and AID(D(2)ED) constructs will facilitate studies aimed to understand the role of conformational plasticity and protein phosphorylation in modulating autoregulatory domain-domain interactions.