Rubisco的研究进展

Ｒｕｂｉｓｃｏ的研究进展李凤玲（山东省莱阳农学院基础部２６５２００）吴光耀（北京大学生命科学院１００８７１）核酮糖－１,５－二磷酸羧化酶／加氧酶（Ｒｉｂｕｌｏｓｅ１,５－ｂｉｓｐｈｏｐｈａｔｅｃａｒｂｏｘｙｌａｓｅ－ｏｘｙｇｅｎａｓｅ,缩写为Ｒｕｂｉ...     

Rubisco活化酶的研究进展

Ｒｕｂｉｓｃｏ活化酶是最近发现的一种该编码的叶绿体蛋白,它在叶绿体内具有激活光合碳同化限速酶Ｒｕｂｉｓｃｏ的功能,该酶能在生理水平ＲｕＢＰ,ＣＯ２浓度（１０μｍｏｌ／Ｌ）下使Ｒｕｂｉｓｃｏ达到最大的活化程度,Ｒｕｂｉｓｃｏ活化酶的研究揭示了长期以来未能解决的Ｒｕｂｉｓｃｏ在体内活化的机理,Ｒｕｂｉｓｃｏ活化酶能解除磷酸糖对Ｒｕｂｉｓｃｏ活性的抑制作用,它的活化活性需要有ＡＴＰ的存在,同时它有ＡＴＰ     

Rubisco活化酶的研究进展

Rubisco活化酶是近年中发现的一种可以调节Rubisco活性的酶,它能使Rubisco在植株体内条件下达到最大活化程度。Rubisco活化酶不仅具有活化Rubisco的活性,而且具有ATP水解酶活性。在ATP水解过程中,Rubisco活化酶促使各种磷酸糖抑制物从Rubisco上解离下来,恢复Rubisco活性。Rubisco活化酶的发现与研究使许多Rubisco体内活化中的疑难问题得到了阐明。本文还介绍了Rubisco活化酶的分子特性、酶作用机制以及环境因素对它活性影响等方面的最新研究进展。     

Rubisco活化酶的研究进展

Rubisco活化酶是近年中发现的一种可以调节Rubisco活性的酶 ,它能使Rubisco在植株体内条件下达到最大活化程度。Rubisco活化酶不仅具有活化Rubisco的活性 ,而且具有ATP水解酶活性。在ATP水解过程中 ,Rubisco活化酶促使各种磷酸糖抑制物从Rubisco上解离下来 ,恢复Rubisco活性。Rubisco活化酶的发现与研究使许多Rubisco体内活化中的疑难问题得到了阐明。本文还介绍了Rubisco活化酶的分子特性、酶作用机制以及环境因素对它活性影响等方面的最新研究进展。     

水稻转绿型白化突变系W25转绿过程中Rubisco、Rubisco活化酶活性与光合速率的变化

水稻 (OryzasativaL .)转绿型白化突变系W2 5在转绿过程中叶绿素、可溶性蛋白质和Rubisco含量的动态变化过程表明 ,白化突变体内叶绿素、可溶性蛋白质和Rubisco含量极低 ,随着转绿过程各组分含量迅速提高 ,转绿至第 30天时超过野生种 2 177s;Rubisco初始活力与Rubisco活化酶含量呈极显著正相关。Rubisco活化酶基因表达的研究结果表明 ,突变体的Rubisco活化酶表达高于野生种 2 177s。在转绿过程中 ,Rubisco活化酶含量的提高要先于Rubisco和光合速率     

植物Rubisco活化酶的研究进展

植物Rubisco活化酶广泛存在于光合生物中,是AAA＋家族成员,具有ATP酶活性,并具有对温度反应的活化Rubisco和分子伴侣的双重功能。该文重点介绍了近年来对Rubisco活化酶的分子特性、作用机制、温度等因子的影响及基因工程研究的最新进展。     

大肠杆菌分子伴侣GroF系统及其胁助的Rubisco蛋白装配

分子伴吕协助蛋白质在体内正确组装,对分子伴侣结构和作用机制的研究不仅在生物大分子结构和功能研究中具有重要的理论意义,而且还具有广泛应用价值。大肠杆菌分子伴侣ＧｒｏＥ系统是迄今为止研究得最为透彻的分子伴侣。本文侧重总结了ＧｒｏＥ系统的作用机制及在该系统的帮助下光合细菌核酮糖１,５－二磷酸羧化／加氧酶（Ｒｕｂｉｓｃｏ）的装配情况。     

Rubisco活化酶及其对Rubisco的调节作用

介绍了Robisco活化酶的发现和分子生物学特性，以及活化酶对光合作用中的关键酶──Ru－bisco的调节机制，这种调节主要是通过减轻磷酸糖的抑制作用实现的。     

大肠杆菌分子伴侣GroE系统及其协助的Rubisco蛋白装配

分子伴侣协助蛋白质在体内正确组装,对分子伴侣结构和作用机制的研究不仅在生物大分子结构和功能研究中具有重要的理论意义,而且还具有广泛的应用价值。大肠杆菌分子伴侣GroE系统是迄今为止研究得最为透彻的分子伴侣。本文侧重总结了GroE系统的作用机制以及在该系统的帮助下光合细菌核酮糖1,5二磷酸羧化/加氧酶(Rubisco蛋白)的装配情况。     

Heat sensitivity of Rubisco,Rubisco activase and Rubisco binding protein in higher plants

During the past few years the investigations concerning Rubisco and the changes of its activity and properties at elevated temperature were reconsidered with special reference to the important role of Rubisco activase and Rubisco binding protein. The major changes in Rubisco, Rubisco activase and Rubisco binding protein reported recently are presented in this review. New information on these proteins, including their changes under heat stress conditions, is discussed together with open questions.     

Rubisco活化酶的分子生物学

Rubisco活化酶是广泛存在于光合生物中、调节Rubisco活性的酶,Rubisco活化酶同时具有活化Rubisco和催化ATP水解的作用.它依赖ATP水解,促使RuBP或其它磷酸糖类从Rubisco上解离下来,以恢复Rubisco的活性.该文介绍Rubisco活化酶的分子特性、作用机制、光合作用调节及基因工程的最新研究进展.     

植物叶片中Rubisco含量的免疫沉淀法测定

Rubisco为光合生物中的关键性酶,对光合作用起重要的调节作用,Rubisco又是植物中重要的氮源贮藏物质。因而Ｒu-bisco的定量测定十分重要,以扬麦为实验材料,提取,纯化Ｒubisco,再以纯化的Ｒubisco为抗原制备Ｒubisco抗体,利用所得抗体采用免疫沉淀技术测定不同植物中的Ｒubisco含量,为Ｒubisco的准确定量测定提供了较简便,快速的方法。     

植物Rubisco活性中心的模拟分析

通过对与不同配基结合的植物Rubisco复合物结构的重叠比较分析 ,发现Rubisco的活性差异是由其中一段Loop6环序列所造成的 ;金属离子与活性中心的结合会造成活性中心巨大的构象变化 .进一步用SwissPDBViewer软件模拟不同配基的植物Rubisco活性中心与此Loop环的氢键相互作用 .结果表明 ,有 3个Lys残基Lys2 0 1、Lys334、Lys175与Rubisco是否处于活性状态密切相关 ,这些残基的结构变化对分子设计可能有重要的参考价值     

Antisense inhibition of Rubisco activase increases Rubisco content and alters the proportion of Rubisco activase in stroma and thylakoids in chloroplasts of rice leaves

BACKGROUND AND AIMS: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase (RCA) is a nuclear-encoded chloroplast protein that modifies the conformation of Rubisco, releases inhibitors from active sites, and increases enzymatic activity. It appears to have other functions, e.g. in gibberellin signalling and as a molecular chaperone, which are related to its distribution within the chloroplast. The aim of this research was to resolve uncertainty about the localization of RCA, and to determine whether the distributions of Rubisco and RCA were altered when RCA content was reduced. The monocotyledon, Oryza sativa was used as a model species. METHODS: Gas exchange and Rubisco were measured, and the sub-cellular locations of Rubisco and RCA were determined using immunogold-labelling electron microscopy, in wild-type and antisense rca rice plants. KEY RESULTS: In antisense rca plants, net photosynthetic rate and the initial Rubisco activity decreased much less than RCA content. Immunocytolocalization showed that Rubisco in wild-type and antisense plants was localized in the stroma of chloroplasts. However, the amount of Rubisco in the antisense rca plants was greater than in the wild-type plants. RCA was detected in both the chloroplast stroma and in the thylakoid membranes of wild-type plants. The percentage of RCA labelling in the thylakoid membrane was shown to be substantially decreased, while the fraction in the stroma was increased, by the antisense rca treatment. CONCLUSIONS: From the changes in RCA distribution and alterations in Rubisco activity, RCA in the stroma of the chloroplast probably contributes to the activation of Rubisco, and RCA in thylakoids compensates for the reduction of RCA in the stroma, allowing steady-state photosynthesis to be maintained when RCA is depleted. RCA may also have a second role in protecting membranes against environmental stresses as a chaperone.     

Regulation of Rubisco activity in vivo

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is not able to achieve and maintain adequate CO₂ and Mg²⁺ activation under physiological conditions. Higher plants and green algae contain Rubisco activase, a soluble protein which not only facilitates Rubisco activation in situ but also regulates enzyme activity in response to irradiance and other factors. Regulation of Rubisco activity by modulation of activation state coordinates the rate of CO₂ fixation with the rate of substrate regeneration. This regulation may be required to ensure that the levels of photosynthetic metabolites in the chloroplast are optimal for photosynthesis under a variety of environrmental conditions. Some plant species also appear to regulate Rubisco activity by synthesizing 2-carboxyarabinitol 1-phosphate, an inhibitor of Rubisco in the dark. This inhibitor may function primarily as a regulator of metabolite binding in the dark rather than as a modulator of Rubisco activity in the light.     

大麦和玉米叶片叶绿体中Rubisco及其活化酶的免疫金标记定位

运用免疫金标记电镜技术研究了禾本科C3植物大麦(Hordeum vulgare L.)和C4植物玉米(Zea mays L.)叶片中Rubisoo及其活化酶(RCA)的细胞定位,结果表明:两种植物叶片解剖结构及叶绿体超微结构差别明显.在大麦叶细胞中,只有一种叶肉细胞叶绿体,Rubisoo和RCA主要分布于叶绿体的间质中.在玉米叶细胞中,存在着维管束鞘细胞和叶肉细胞两种类型叶绿体,Rubisco主要分布于鞘细胞叶绿体的基质中,但在叶肉细胞叶绿体中亦有少量特异性标记;RCA在鞘细胞叶绿体和叶肉细胞叶绿体的基质中都有分布.两种植物叶绿体结构及光合作用关键酶定位的不同,体现了C3植物和C4植物在光合器结构与功能上的差异.     

H2O2对水稻Rubisco稳定性的影响

H2 O2 浓度低于 2 0mmol·L-1时 ,Rubisco分子稳定 ;高于 2 0mmol·L-1则Rubisco的大亚基之间发生交联 ,全酶发生聚沉。H2 O2 处理后 ,Rubisco表面巯基数目减少 ,对两种蛋白水解酶尤其是胰蛋白酶的敏感性增强 ,大亚基水解明显增加。H2 O2 处理只会增加Rubisco大亚基的水解程度 ,不会造成新的水解位点