大肠杆菌核糖体蛋白质L24和L27突变对λN和λQ基因表达的影响

核糖体是生物体翻译遗传密码的唯一场所。核糖体各组份的确切功能目前仍不清楚。本实验室的研究已证实：有些核糖体蛋白质突变能在翻译水平上影响核糖体翻译的特异性。本文使用转座子Tn10将核糖蛋白质L24（rpmA）突变从A19的衍生株转到T83菌株上,并研究这2个突变对λN和λQ基因及对N-lacZ和Q-lacZ融合基因表达的不同影响,为核糖体蛋白质能影响核糖体翻译的特异性提供了又一个实例。     

大豆耐盐机理及相关基因分子标记

大豆耐盐涉及多种生理代谢途径.耐盐大豆能够通过Cl-排除、控制Na 的吸收和转运、合成渗透调节物质、改变细胞膜膜脂组分及相关酶类的活性等多种形式来适应盐胁迫;野生大豆群体具有盐腺,从形态结构上适应盐逆境;大豆-根瘤菌共生体在盐胁迫下通过互作来提高整体的耐盐性.分子生物学技术应用于大豆耐盐研究,已获得了一些与耐盐相关基因连锁的分子标记.广泛搜集筛选大豆栽培种和野生种资源,利用分子生物学技术和基因工程提高大豆耐盐性,将成为未来大豆耐盐研究的主要内容.     

以色列野生二粒小麦(Triticum dicoccoides)耐盐性鉴定

采用水培法对从以色列引进的分属8个自然群体的93份野生二粒小麦进行了耐盐性初步鉴定.结果表明:①供试材料中仅有高耐盐材料3份,耐盐材料7份 ,耐盐性较好的材料仅占参试材料总数的10.7%;②8个自然群体的野生二粒小麦的耐盐性存在较大差异,其中3号群体耐盐性明显高于其他群体,说明来自Tabigha地区的野生二粒小麦具有丰富的耐盐基因源;③将经过鉴定的耐盐性较好的野生二粒小麦与普通小麦中的耐盐品种进行比较研究发现,以色列耐盐性较好的野生二粒小麦的耐盐性不如普通小麦中的茶淀红和SW10两个耐盐品种.     

大豆耐盐机理及相关基因分子标记

大豆耐盐涉及多种生理代谢途径。耐盐大豆能够通过Cl-排除、控制Na+的吸收和转运、合成渗透调节物质、改变细胞膜膜脂组分及相关酶类的活性等多种形式来适应盐胁迫;野生大豆群体具有盐腺,从形态结构上适应盐逆境;大豆-根瘤菌共生体在盐胁迫下通过互作来提高整体的耐盐性。分子生物学技术应用于大豆耐盐研究,已获得了一些与耐盐相关基因连锁的分子标记。广泛搜集筛选大豆栽培种和野生种资源,利用分子生物学技术和基因工程提高大豆耐盐性,将成为未来大豆耐盐研究的主要内容。     

G protein β<Subscript>1</Subscript>γ<Subscript>2</Subscript> subunits purification and their interaction with adenylyl cyclase

A preliminary study on the interaction of G protein (guanine triphosphate binding pro- tein) β1γ2 subunits and their coupled components in cell signal transduction was conducted in vitro. The insect cell lines, Sf9 (Spodoptera frugiperda) and H5 (Trichoplusia ni) were used to express the recombinant protein Gβ1γ2. The cell membrane containing Gβ1γ2 was isolated through affinity chromatography column with Ni-NTA agarose by FPLC method, and the highly purified protein was obtained. The adenylyl cyclase 2 (AC2) activity assay showed that the purified Gβ1γ2 could significantly stimulate AC2 activity. The interaction of β1γ2 subunits of G protein with the cytoplasmic tail of various mammalian adenylyl cyclases was monitored by BIAcore technology using NTA sensor chip, which relies on the phenomenon of surface plasmon resonance (SPR). The experiments showed the direct binding of Gβ1γ2 to the cytoplasmic tail C2 domain of AC2. The specific binding domain of AC2 with Gβ1γ2 was the same as AC2 activity domain which was stimulated by β1γ2.     

G protein β1γ2 subunits purification and their interaction with adenylyl cyclase

A preliminary study on the interaction of G protein (guanine triphosphate binding pro- tein) β1γ2 subunits and their coupled components in cell signal transduction was conducted in vitro. The insect cell lines, Sf9 (Spodoptera frugiperda) and H5 (Trichoplusia ni) were used to express the recombinant protein Gβ1γ2. The cell membrane containing Gβ1γ2 was isolated through affinity chromatography column with Ni-NTA agarose by FPLC method, and the highly purified protein was obtained. The adenylyl cyclase 2 (AC2) activity assay showed that the purified Gβ1γ2 could significantly stimulate AC2 activity. The interaction of β1γ2 subunits of G protein with the cytoplasmic tail of various mammalian adenylyl cyclases was monitored by BIAcore technology using NTA sensor chip, which relies on the phenomenon of surface plasmon resonance (SPR). The experiments showed the direct binding of Gβ1γ2 to the cytoplasmic tail C2 domain of AC2. The specific binding domain of AC2 with Gβ1γ2 was the same as AC2 activity domain which was stimulated by β1γ2.