蛋白质组学研究相关技术及进展

蛋白质组学以蛋白质组为研究对象,应用相关研究技术,从整体水平上来认识蛋白的存在及活动方式。随着人类基因组计划的完成,蛋白质组学的研究也得到了快速发展,与蛋白质组学研究相关的一些技术也日益得到完善和提高。简要综述了近年来蛋白质组学研究中最为重要的样品制备、蛋白质分离、蛋白质鉴定等技术及研究进展。     

蛋白质组学在木薯育种中的应用

蛋白质组学通过研究整体蛋白质活动来揭示生命运动规律,是解析功能基因组表达的必要手段。目前蛋白质组学为木薯选育种研究提供了重要手段和新思路。介绍了蛋白质组学研究平台并对其在选育高光效高淀粉积累、高蛋白质、高类胡萝卜素及抗逆木薯种质方面的应用进行了综述。     

末端蛋白质组学研究进展

蛋白质是一类重要的生物大分子,参与生物体的各种生命活动。蛋白质组学研究主要致力于从整体水平上对一个生物体包含的所有蛋白质进行定性和定量分析。蛋白质的末端参与众多的生物学过程,与蛋白质的转运、定位、凋亡和降解等有密切联系。因此,详细研究末端蛋白质组学将有助于揭示相关的生物学机制,是蛋白质组学研究的重点之一。本文就蛋白质末端的修饰、功能、研究方法及应用前景进行简要综述。     

我国蛋白质组学研究现状及展望

蛋白质组学是系统研究分子机器、亚细胞器、细胞、组织、器官乃至整体等生物体系内蛋白质全组成及其活动规律的科学,已成为21世纪生命科学的焦点之一。本文简要介绍了蛋白质组学研究背景,我国蛋白质组学研究现状、存在问题和前景展望。     

种子蛋白质与蛋白质组的研究

综述了种子蛋白质与蛋白质组的研究,主要介绍了种子发育与形成、种子休眠与萌发、种子保存与活力以及种子与环境相互作用的蛋白质与蛋白质组的研究.同时阐述了当今蛋白质组学在种子研究中的应用以及所取得的成果,并展望了种子蛋白质组学的发展方向,种子生物学的研究将从基因水平走向整体水平,因此环境因子与种子蛋白质的相互作用是研究的重点.运用蛋白质组学将能揭示蛋白质的功能并明晰种子的生命机制.     

蛋白质组学在感染性疾病研究中的应用

蛋白质组学在人类疾病研究中的应用 ,主要是通过比较分析正常组织细胞与异常组织细胞、同一疾病在不同的发展时期细胞内整体蛋白质的表达差异 ,对差异表达的蛋白质进行鉴定、定量、表征 ,寻找与疾病相关的新的标志物 ,为人类疾病研究提供新的手段和依据 ,蛋白质组学在感染性疾病研究中的应用就是其中的一个方面。1 .蛋白质组学在感染性疾病研究中的应用蛋白质组学在人类感染性疾病研究中的应用主要是对引起感染性疾病的致病源的整体蛋白质进行研究 ,同时结合血清学 ,对其进行分析 ,鉴定出与疾病相关的新的标志物 ,为感染性疾病的诊断、治疗…     

蛋白质组学及其在肿瘤研究中的应用

简要介绍了蛋白质组学的概念、研究方法及其在肿瘤研究中的应用.蛋白质组学研究直接定位于蛋白质水平，从整体、动态、定量的角度去研究基因的功能，是后基因组计划的一个重要组成部分.恶性肿瘤是一种多基因参与的复杂疾病，从蛋白质整体水平上研究恶性肿瘤将有助于进一步揭示恶性肿瘤的发病机制，发现恶性肿瘤特异性的标志物及其药物治疗的靶标.     

蛋白质组学及其在肿瘤研究中的应用

简要介绍了蛋白质组学的概念、研究方法及其在肿瘤研究中的应用.蛋白质组学研究直接定位于蛋白质水平,从整体、动态、定量的角度去研究基因的功能,是后基因组计划的一个重要组成部分.恶性肿瘤是一种多基因参与的复杂疾病,从蛋白质整体水平上研究恶性肿瘤将有助于进一步揭示恶性肿瘤的发病机制,发现恶肿瘤特异性的标志物及其药物治疗的靶标.     

蛋白质组学分析技术在微生物研究中的应用

随着后基因组时代的到来,蛋白质组学分析为研究微生物的生命活动和细胞功能提供了一个广阔的视角。综述了大规模分析微生物蛋白质组的策略和方法,包括自上而下的蛋白质组学分析、自下而上的蛋白质组学分析、蛋白质组定量分析技术、蛋白质修饰研究方法和蛋白质芯片技术。最后,对沙门氏菌蛋白质组学的研究进展进行了简要介绍。     

卵泡液蛋白质组学研究进展

蛋白质组的概念最初在1994年提出.蛋白质组学是以细胞内全部蛋白质的存在及其活动为研究对象,它极大地促进了我们对后基因组时代基因功能的理解.卵泡液作为卵母细胞生长和分化的培养基,直接或间接影响卵母细胞的生育力和发育潜能,其中的一些蛋白质可以作为卵母细胞成熟的标记.应用蛋白质组学方法可以筛选与卵母细胞成熟及一些与生殖疾病有关的标记蛋白.本文就卵泡液的蛋白质组学研究进展作简要综述.     

Patch engineering: a general approach for creating proteins that have new binding activities

Patch engineering is a technique for creating folded proteins that have new binding activities. Different protein scaffolds are used to present a patch of discontinuous residues on a folded-protein surface. By varying simultaneously the residues in these patches and displaying these mutant proteins on phage, one can select proteins that have new binding activities. Patch engineering is applicable to any protein fold. Novel proteins derived by this approach might replace antibodies in certain applications or provide lead molecules for the design of non-peptide analogues.     

Ubiquitin and ubiquitin-like proteins as multifunctional signals

Protein ubiquitylation is a recognized signal for protein degradation. However, it is increasingly realized that ubiquitin conjugation to proteins can be used for many other purposes. Furthermore, there are many ubiquitin-like proteins that control the activities of proteins. The central structural element of these post-translational modifications is the ubiquitin superfold. A common ancestor based on this superfold has evolved to give various proteins that are involved in diverse activities in the cell.     

Heat shock protein-90 and the catalytic activities of the 20 S proteasome (multicatalytic proteinase complex)

The effect of heat shock protein 90 (Hsp-90) and several other proteins on the catalytic activities of the 20 S proteasome (MPC) was examined. The chymotrypsin-like (ChT-L) and peptidylglutamyl-peptide hydrolyzing (PGPH) activities of the pituitary MPC were inhibited by Hsp-90 with IC50 values of 8 and 28 nM, respectively. Bovine serum albumin and two other proteins tested inhibited the same activities with much higher IC50 values. The trypsin-like and branched-chain amino-acid-preferring activities were not affected by any of the proteins. None of the activities of the bovine spleen MPC, an enzyme form in which the X, Y, and Z subunits are virtually completely replaced by the LMP2, LMP7, and LMP10 subunits, was affected by either Hsp-90 or the other proteins tested. Hsp-90 inhibited the degradation of the oxidized B-chain of insulin by the pituitary MPC but not by its spleen counterpart. The PA28 activator (11 S regulator; REG) of the proteasome abolished the inhibitory effect of Hsp-90 and other proteins on the ChT-L and PGPH activities of the pituitary MPC. It is suggested that Hsp-90 induces conformational changes that affect the ChT-L and PGPH activities expressed by the X and Y subunits, respectively, but does not affect the activities expressed by LMP subunits.     

秸秆质外体蛋白对纤维素酶活力的影响

研究了玉米秸秆在储存过程中质外体蛋白含量的变化情况,及其对Penicilllumexpansum纤维素酶活力的影响。结果表明随着储存时间的延长,可抽提的玉米秸秆质外体蛋白的数量逐渐减少,与P.expansum纤维素酶的协同作用也随之减弱。储存玉米秸秆质外体蛋白没有内源性纤维素酶活力,而新鲜玉米秸秆有内源性EG活性,但它的稳定性较差,储存半年后基本降解或失活。储存秸秆质外体蛋白对FPA酶活力、棉花酶活力、β-葡萄糖苷酶活力有明显的增效作用,最大增效分别达到95.32%、102.06%和96.6%。而对CMCase却表现出抑制作用,最大抑制率为49.52%,质外体蛋白-EG-βG表现出明显的协同关系,而它对CBH酶活力没有影响。消除内源性EG的影响后,新鲜玉米秸质外体蛋白对FPA活力、棉花酶活力、β-葡萄糖苷酶活力的促进率,以及CMCase的抑制率均高于储存秸秆的质外体蛋白。可见质外体蛋白是天然纤维素酶解研究不可忽视的影响因素。     

Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins

Effects of aluminum, magnesium, and fluoride (AMF) on members of both the trimeric G protein and smaller (20-25 kDa) monomeric GTP-binding protein families were examined. The dissociation of GDP from G proteins was blocked by AMF but was unchanged with the addition of AMF to any of six of the monomeric GTP-binding proteins. Biochemical activities and properties of one of the smaller GTP-binding proteins, ADP-ribosylation factor, were also found to be unaffected by AMF. It is concluded that the ability of AMF to activate the trimeric G proteins is not shared by the smaller GTP-binding proteins and thus should prove to be a useful discriminator between cellular activities regulated by these two families of regulatory proteins.     

Bioactive components of ovine and caprine cheese whey

Cheese whey, also known as sweet whey, is a by-product of cheese-making that contains many valuable constituents. Among them, whey proteins stand out for their high nutritional value in terms of biological value and composition in essential amino acids. In recent years, the increasing demand for caprine and ovine cheeses has produced important amounts of whey from these species, boosting research on the biological activities of its constituent proteins. Different bioactivities have been associated to these proteins, among them antihypertensive, antimicrobial, opioid, antioxidant and immunomodulant activity being the most studied. Although biological activities are present in the intact proteins, in many cases whey proteins act as precursors of bioactive peptides that are released from the hydrolysis of these proteins with different enzymes. This review presents an overview of the different biological activities described for caprine and ovine cheese whey proteins as well as for other whey components such as lactose, oligosaccharides or minerals.     

Ribosome-Inactivating Proteins: A Family of Plant Proteins That Do More Than Inactivate Ribosomes

Many plants contain proteins that are commonly designated as ribosome-inactivating proteins (RIPs). Based on the structure of the genes and the mature proteins a novel system is proposed to unambiguously classify all RIPs in type-1, type-2, and type-3 RIPs. In addition, the concept of one- and two-chain type-1 RIPs is introduced. After an overview of the occurrence, molecular structure, and amino acid sequences of RIPs, the formation of the mature proteins from the primary translation products of the corresponding mRNAs is elaborated in detail in a section dealing with the biosynthesis, posttranslational modifications, topogenesis, and subcellular location of the different types of RIPs. Details about the three-dimensional structure of type-1 RIPs and the A and B chains of type-2 RIPs are discussed in a separate section. Based on the data given in the previous sections, the phylogenic and molecular evolution of RIPs is critically assessed and a novel model is proposed for the molecular evolution of RIPs. Subsequently, the enzymatic activities of RIPs are critically discussed whereby special attention is given to some presumed novel activities, and a brief overview is given of the biological activities of the different types of RIPs on cells and whole organisms. By combining the data on the enzymatic activities and biological activities of RIPs, and the current knowledge of different plant physiological aspects of these proteins, the role of RIPs in plants is revisited. Thereby the attention is focussed on the role of RIPs in plant defense with the emphasis on protection against plant-eating organisms and viruses. Finally, there is a short discussion on the discovery of a novel class of enzymes called RALyases that use ribosomes damaged by RIPs as a substrate and may act cooperatively with RIPs. There is discussion regarding why the identification of this novel enzyme gives valuable clues to the origin and original function of RIPs and may be helpful to unravel the physiological role of modem RIPs.     

Arf GAPs as regulators of the actin cytoskeleton.

The Arf (ADP-ribosylation factor) GAPs (GTPase-activating proteins) are a family of proteins with a common catalytic domain that induces hydrolysis of GTP bound to Arf GTP-binding proteins. At least three groups of multidomain Arf GAPs affect the actin cytoskeleton and cellular activities, such as migration and movement, that depend on the cytoskeleton. One role of the Arf GAPs is to regulate membrane remodelling that accompanies actin polymerization. Regulation of membrane remodelling is mediated in part by the regulation of Arf proteins. However, Arf GAPs also regulate actin independently of effects on membranes or Arf. These functions include acting as upstream regulators of Rho family proteins and providing a scaffold for Rho effectors and exchange factors. With multiple functional elements, the Arf GAPs could integrate signals and biochemical activities that result in co-ordinated changes in actin and membranes necessary for a wide range of cellular functions.     

Arf GAPs as regulators of the actin cytoskeleton

The Arf (ADP-ribosylation factor) GAPs (GTPase-activating proteins) are a family of proteins with a common catalytic domain that induces hydrolysis of GTP bound to Arf GTP-binding proteins. At least three groups of multidomain Arf GAPs affect the actin cytoskeleton and cellular activities, such as migration and movement, that depend on the cytoskeleton. One role of the Arf GAPs is to regulate membrane remodelling that accompanies actin polymerization. Regulation of membrane remodelling is mediated in part by the regulation of Arf proteins. However, Arf GAPs also regulate actin independently of effects on membranes or Arf. These functions include acting as upstream regulators of Rho family proteins and providing a scaffold for Rho effectors and exchange factors. With multiple functional elements, the Arf GAPs could integrate signals and biochemical activities that result in co-ordinated changes in actin and membranes necessary for a wide range of cellular functions.