The HERC proteins: functional and evolutionary insights

HERC proteins are defined as containing both HECT and RCC1-like domains in their amino acid sequences. Six HERC genes have turned up in the human genome which encode two different sorts of polypeptides: while the small HERC proteins possess little more than the two aforementioned domains, the large ones are giant proteins with a plethora of potentially important regions. It is now almost 10 years since the discovery of the first family member and information is starting to accumulate pointing to a general role for these proteins as ubiquitin ligases involved in membrane-trafficking events. In this review, the available data on these six members are discussed, together with an account of their evolution.Received 16 March 2005; received after revision 13 April 2005; accepted 28 April 2005     

Small heat shock proteins: molecular structure and chaperone function

Small heat shock proteins (sHSPs) associate with nuclei, cytoskeleton and membranes, and as molecular chaperones they bind partially denatured proteins, thereby preventing irreversible protein aggregation during stress. sHSP monomers consist of a conserved α-crystallin domain of approximately 90 amino acid residues, bordered by variable amino- and carboxy-terminal extensions. The sHSPs undergo dynamic assembly into mono- and poly-disperse oligomers where the rate of disassembly affects chaperoning. The α-crystallin domain contains several β-strands organized into two β-sheets responsible for dimer formation, the basic building block of most sHSPS. The amino-terminal extension modulates oligomerization, subunit dynamics and substrate binding, whereas the flexible carboxy-terminal extension promotes solubility, chaperoning and oligomerization, the latter by inter-subunit linkage. Crystallization studies have revealed sHSP structure and function. Additionally, site-directed mutagenesis, biophysical investigations, functional studies and the discovery of relationships between mutated sHSPs and diseases have illuminated the role of sHSP within cells. Received 8 May 2005; received after revision 24 June 2005; accepted 19 July 2005     

有机溶剂沉淀法去除子宫内膜癌血清高丰度蛋白的比较研究

建立了一种简便有效、成本低廉的去除子宫内膜癌血清高丰度蛋白的方法．运用3种不同的有机溶剂（不同体积倍数）处理子宫内膜癌血清样品,SDS．PAGE电泳检测去除高丰度蛋白．结果表明：不同的有机溶剂沉淀法都能去除血清样品中绝大部分的高、中丰度蛋白,但低丰度蛋白质保留、减弱及丢失的现象不一．用1倍体积乙腈可有效去除子宫内膜癌血清样品中的绝大部分高丰度蛋白,同时保留较多的小分子量蛋白．     

富营养化湖泊中藻类蛋白特征及其资源化开发

藻类的大量繁殖是富营养化水体最显著的污染特征.介绍我国富营养化水体中藻类生长特性、营养价值,就藻类蛋白在食品、药品、光电材料、生物探针、环境监测、毒素等方面的资源化开发利用进行了综述,相关研究成果对富营养化水体中藻类蛋白的资源化开发利用具有重要的意义.     

植物抗菌肽研究进展

植物抗菌肽是一类对细菌,真菌等微生物有抑制或杀灭作用的小分子多肽,它能被细菌,真菌或物理的,化学的刺激所诱导,有些抗菌肽甚至在植物体内能组成性的表达,从化学结构来看,植物抗菌肽要包括硫堇,植物防卫素,脂转移蛋白和橡胶素类等,它们抗菌能力强,有较好的耐热性,抗菌机理独特,在农业,医药及食品等领域有着广泛的应用前景。作者总结了国内外植物抗菌肽研究进展,对其应用研究的基因工程等方面作了阐述,并对进一步研     

Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question

In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this network are two protein families, the AAA+ and the Hsp70 family. The major Hsp70 chaperone, DnaK, efficiently prevents protein aggregation and supports the refolding of damaged proteins. In a special case, DnaK, together with the assistance of the AAA+ protein ClpB, can also refold aggregated proteins. Other Hsp70 systems have more specialized functions in the cell, for instance HscA appears to be involved in the assembly of Fe/S proteins. In contrast to ClpB, many AAA+ proteins associate with a peptidase to form proteolytic machines which remove irreversibly damaged proteins from the cellular pool. The AAA+ component of these proteolytic machines drives protein degradation. They are required not only for recognition of the substrate but also for substrate unfolding and translocation into the proteolytic chamber. In many cases, specific adaptor proteins modify the substrate binding properties of AAA+ proteins. While chaperones and proteases do not appear to directly cooperate with each other, both systems appear to be necessary for proper functioning of the cell and can, at least in part, substitute for one another. RID="*" ID="*"Corresponding author.     

嗜水气单胞菌Ⅲ型分泌系统研究进展

主要对嗜水气单胞菌Ⅲ型分泌系统、效应蛋白及其致病机理等方面的研究进展进行了综述.细菌分泌系统的发现是近年来细菌致病机制研究的重要进展,许多革兰氏阴性细菌借助于细菌的分泌系统,分泌出毒性因子和效应蛋白,与寄主进行分子交流.     

Amphipols: polymeric surfactants for membrane biology research

Membrane proteins classically are handled in aqueous solutions as complexes with detergents. The dissociating character of detergents, combined with the need to maintain an excess of them, frequently results in more or less rapid inactivation of the protein under study. Over the past few years, we have endeavored to develop a novel family of surfactants, dubbed amphipols (APs). APs are amphiphilic polymers that bind to the transmembrane surface of the protein in a noncovalent but, in the absence of a competing surfactant, quasi-irreversible manner. Membrane proteins complexed by APs are in their native state, stable, and they remain water-soluble in the absence of detergent or free APs. An update is presented of the current knowledge about these compounds and their demonstrated or putative uses in membrane biology.     

Heterologous expression of G-protein-coupled receptors: comparison of expression systems from the standpoint of large-scale production and purification

G-protein-coupled receptors (GPCRs) are of prime importance for cell signal transduction mechanisms and are the target of many current and potential drugs. However, structural data on these membrane proteins is still scarce because of their low natural abundance and the low efficiency of most of the expression systems currently available. This review presents the most important expression systems currently employed for heterologous expression of GPCRs; Escherichia coli, yeast, insect cells and mammalian cells. After briefly recalling the specificity, advantages and limitations of each system, particular emphasis is put on the quantitative comparison of these expression systems in terms of overall expression yield, and on the influence of various factors (primary sequence, origin, cell type, N- and C-terminal tags) on the results.