The Cold Box stem-loop proximal to the 5'-end of the Escherichia coli cspA gene stabilizes its mRNA at low temperature.

The 5'-end region of cspA mRNA contains a Cold Box sequence conserved among several cold-shock mRNAs. This region forms a stable stem-loop structure followed by an AU-rich sequence. Here we show that the Cold Box region is essential for the normal scale of cspA mRNA induction after cold shock because a deletion of the stem-loop significantly destabilizes the mRNA and reduces the cold shock-induced cspA mRNA amount by approximately 50%. The AU-rich track, however, slightly destabilizes the mRNA. The integrity of the stem is essential for the stabilizing function, whereas that of the loop sequence is less important. Overexpression of a mutant cspA mRNA devoid of both the AUG initiation codon and the coding sequence results in a severe growth inhibition at low temperature along with a derepression of the chromosomal cspA expression. Furthermore, the overexpressed RNA is stably associated with the 30 S and 70 S ribosomes. Our results demonstrate that the AUG initiation codon and the coding region containing the downstream box are not required for cspA mRNA to bind ribosomes and that the 5'-untranslated region by itself has a remarkable affinity to ribosomes at low temperature.     

在双脉冲光刺激下瞳孔系统的采样控制特性

本文用实验揭示了瞳孔对光动态反应具有采样控制特性。实验中采用各种不同时间间隔的双脉冲光,以开环的方式(Maxwellian View)刺激瞳孔,当双脉冲之间间隔较长时,瞳孔反应相当于对双脉冲光的两次脉冲分别产生瞬态收缩;当双脉冲时间间隔短于0.6s 时,其反应就成了一次瞬态收缩,与单个光脉冲所引起的瞳孔反应一样。同—受试者的多次实验结果相同,不同受试者所得结果也基本一致。故瞳孔对脉冲刺激光引起反应后,必须至少约隔0.6s 才能对另一次脉冲光产生反应,这就说明了瞳孔动态反应具有离散的采样控制特性。实验还进一步证明,瞳孔系统的控制机制是双重模式的控制:不同的刺激条件下,瞳孔反应可呈现为瞬态反应(AC)或持续反应(DC),瞬态反应的 AC 通道为离散的采样控制,持续反应的 DC 通道为连续控制。     

辽宁犹伊螨属一新种：（蜱螨亚纲：犹伊螨科）

本文对独角仙体上的犹伊螨新种——大连犹伊螨Eviphis dalianensis sp.nov.进行了描述,该种与淮南犹伊螨Eviphis huainanensis Wen,1965近似。模式标本采自辽宁大连市,保存于辽宁省卫生防疫站虫媒消杀科。     

根田鼠静止代谢率特征的研究

通过实地测定分布于青海高原的根田鼠的RMR,发现其RMR水平明显高于与其体重相似的其它田鼠,而平均最小热传导值并不比后者低,说明可能是以保持高的RMR水平来适应高原寒冷气候的。同时发现,根田鼠以化学体温调节为主,以适应高原气温较大的波动。     

斑蜡蝉生殖系统的解剖与组织学

详细描述了斑蜡蝉两性生殖系统各部分的结构与组织学。精巢由6条互相分离的精巢管组成,而卵巢则含有14条典型的端滋式卵巢管。用组织化学方法测定了雄性附腺各段的分泌物的成分,它们分别构成精包、精液与精包鞘。订正了过去文献中关于雌性生殖系统某些部分的解释:过去误称为雌性附腺的其实是受精囊及其腺,而过去误称为受精囊的其实是接纳及消化精包的交配囊。受精囊腺的细胞具有一条曲折的细胞内分泌小管,贯穿内膜开口于腺腔。交配囊体及交配囊管上皮折突的内层为腺细胞,有孔道通过内膜与腔相通,它可以分泌一种(或多种)酶以消化精包。此外还从卵黄发生的速率与精包授精的关系,讨论了精包作为一种蛋白养料的来源,在雌虫营养与生殖上的重要性。     

玉米花粉单倍体植株染色体上异染色质的变异

我们用Giemsa BSG C-带技术检查了玉米花药培养获得的花粉单倍体植株根尖细胞染色体上异染色质的变异,观察结果表明,有的植株所显示的C-带数目是与供体植株的相一致,有的植株所显示的C-带数目则发生了显著变化,其中有的增加,有的减少。并讨论了异染色质发生变异的可能原因。还相应地观察到间期核中染色中心的变化是与中期染色体上C-带数目的变化相一致。     

IL-4 blocks the up-regulation of IL-2 receptors induced by IL-2 in normal human B cells

A negative influence of IL-4 on the IL-2-induced B cell proliferation and differentiation has recently been reported. In this study, we have further investigated a role of IL-4 on human tonsillar B cell proliferation and IL-2R expression. IL-4 enhanced Staphylococcus aureus Cowan 1 strain (SAC)-induced B cell proliferation, reaching the peak on day 3. However, from day 4, IL-4 inhibited IL-2-induced proliferation. In the cross-linking study, IL-4 enhanced the density of 125I-IL-2-binding protein at low affinity binding condition (2 nM of 125I-IL-2) in SAC-activated B cells. However, IL-4 blocked the enhancement in the density of 125I-IL-2-binding proteins induced by IL-2, from day 3, in both high (50 pM of 125I-IL-2) and low affinity binding conditions, suggesting that IL-4 is able to block IL-2-induced IL-2R up-regulation. This was confirmed by a binding study: B cells that cultured for 3 days with SAC plus IL-2 expressed an average of 180 +/- 20 high affinity receptors/cell with a Kd of 12 pM and 5800 +/- 500 low affinity receptors/cell with a Kd of 980 pM. By coculturing with IL-4, high affinity receptors were almost undetectable and the expression of low affinity receptors was reduced by more than 80%. IL-4-mediated inhibition of IL-2-induced IL-2R expression does not seem to be due to the direct interaction between IL-4 and cell surface receptors, inasmuch as preincubation of cells with IL-4 for 60 min at 37 degrees C did not alter the binding of 125I-IL-2 to cells previously cultured for 3 days with SAC plus IL-2. These data suggest that IL-4 has a capacity to block the up-regulation of the high as well as low affinity IL-2R-induced by IL-2 in normal human B cells, and could provide a possible explanation for the decreased responsiveness of B cells to IL-2 in the presence of IL-4.     

Calcium binding to the subunit c ofE. coli ATP-synthase and possible functional implications in energy coupling

The 8-kDa subunit c of theE. coli F₀ ATP-synthase proton channel was tested for Ca⁺⁺ binding activity using a⁴⁵Ca⁺⁺ ligand blot assay after transferring the protein from SDS-PAGE gels onto polyvinyl difluoride membranes. The purified subunit c binds⁴⁵Ca⁺⁺ strongly with Ca⁺⁺ binding properties very similar to those of the 8-kDa CF₀ subunit III of choloroplast thylakoid membranes. The N-terminal f-Met carbonyl group seems necessary for Ca⁺⁺ binding capacity, shown by loss of Ca⁺⁺ binding following removal of the formyl group by mild acid treatment. The dicyclohexylcarbodiimide-reactive Asp-61 is not involved in the Ca⁺⁺ binding, shown by Ca⁺⁺ binding being retained in twoE. coli mutants, Asp61Asn and Asp61Gly. The Ca⁺⁺ binding is pH dependent in both theE. coli and thylakoid 8-kDa proteins, being absent at pH 5.0 and rising to a maximum near pH 9.0. A treatment predicted to increase the Ca⁺⁺ binding affinity to its F₀ binding site (chlorpromazine photoaffinity attachment) caused an inhibition of ATP formation driven by a base-to-acid pH jump in whole cells. Inhibition was not observed when the Ca⁺⁺ chelator EGTA was present with the cells during the chlorpromazine photoaffinity treatment. An apparent Ca⁺⁺ binding constant on the site responsible for the UV plus chlorpromazine effect of near 80–100 nM was obtained using an EGTA-Ca⁺⁺ buffer system to control free Ca⁺⁺ concentration during the UV plus chlorpromazine treatment. The data are consistent with the notion that Ca⁺⁺ bound to the periplasimic side of theE. coli F₀ proton channel can block H⁺ entry into the channel. A similar effect occurs in thylakoid membranes, but the Ca⁺⁺ binding site is on the lumen side of the thylakoid, where Ca⁺⁺ binding can modulate acid-base jump ATP formation. The Ca⁺⁺ binding to the F₀ and CF₀ complexes is consistent with a pH-dependent gating mechanism for control of H⁺ ion flux across the opening of the H⁺ channel.This work was supported in part by grants from the Department of Energy and the U.S. Department of Agriculture.On leave from the Institute of Soil Science and Photosynthesis, Russian Academy of Science, Pushchino, Russia.