{"title":"古菌蛋白的生物技术应用","authors":"F. Pecorari, V. Arcus, J. Wiegel","doi":"10.1155/2015/809758","DOIUrl":null,"url":null,"abstract":"Many industrial/biotechnological processes take place under extreme conditions of temperature, pH, salinity, or pressure which are not suitable for activities of proteins from model eukaryotic or common neutrophilic, mesophilic, and prokaryotic microorganisms. In contrast, Archaea offer a large panel of extremophile organisms that express proteins that are able to remain properly folded and functional under the harshest biophysical conditions. \n \nThe study of this group of organisms has uncovered archaeal enzymes and proteins with unusual properties compared to their traditional homologues. In addition, with their ease of production and better-behaved samples for X-ray crystallography, for example, archaeal proteins are often more convenient for structural biology studies than their eukaryotic equivalents. The knowledge thus gained can open routes to commercial biotechnological applications. These last years, with the emergence of next generation sequencing techniques to decode whole genomes and metagenomes and the pressure to develop “greener” industrial processes, the rate of new archaeal proteins reported has significantly increased, thereby widening again their potential of applications. In this special issue of Archaea, we present selected papers dealing with the uses of archaeal proteins as tools for various fields of biotechnologies and research. \n \nDNA and RNA ligases are essential enzymes in living cells and have applications in molecular biology. A review by M. Tanabe et al. discusses the uses of DNA ligases and recent progress in deciphering their catalytic mechanisms via structural studies, and they describe how protein engineering can improve ligation efficiency of an archaeal DNA ligase over a broad temperature range. In another paper on ligases, C. R. Chambers and W. M. Patrick present the current state of knowledge on archaeal nucleic acid ligases including RNA ligases, highlighting their remarkable properties relevant to biotechnologists, and they discuss the modifications of the activities of archaeal RNA ligases by directed mutagenesis to develop more efficient molecular biology protocols. \n \nJ. A. Littlechild reviews research regarding the discovery and potential applications of a range of thermophilic archaeal proteins, illustrating the power of archaeal enzymes for various industrial biocatalysis. Then, an article by V. M. Gumerov et al. describes the characterization of a novel thermostable and multifunctional β-glycosidase from Acidilobus saccharovorans that displays a high tolerance to glucose, a desired property for such enzymes used to process lignocellulose biomass. C.-H. Wu et al. present a review summarizing the strategies used in engineering and characterizing three different forms of soluble hydrogenase I from the hyperthermophile Pyrococcus furiosus, an enzyme which has been used in vitro for hydrogen production. \n \nArchaea are not only interesting for catalysis applications. J. C. Charlesworth and B. P. Burns give a comprehensive overview of archaeal low-molecular weight compounds including peptides with antimicrobial properties which can be exploited for biotechnological purposes. Finally, in their review, J. M. Miller and E. J. Enemark exemplify with MCM helicases how crystallography of archaeal homologues can be helpful to decipher structure/function relationships of their eukaryotic versions which are more difficult to crystallize. \n \nWe hope this special issue will provide the reader with an up-to-date overview of some of the diverse applications of archaeal proteins and, perhaps, prompt further research in this largely untapped field with rich prospects for the future of many biotechnological applications. \n \n \nFrederic Pecorari \n \nVickery L. Arcus \n \nJuergen Wiegel","PeriodicalId":49105,"journal":{"name":"Archaea-An International Microbiological Journal","volume":"2015 1","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2015-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2015/809758","citationCount":"2","resultStr":"{\"title\":\"Biotechnological Uses of Archaeal Proteins\",\"authors\":\"F. Pecorari, V. 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Wu et al. present a review summarizing the strategies used in engineering and characterizing three different forms of soluble hydrogenase I from the hyperthermophile Pyrococcus furiosus, an enzyme which has been used in vitro for hydrogen production. \\n \\nArchaea are not only interesting for catalysis applications. J. C. Charlesworth and B. P. Burns give a comprehensive overview of archaeal low-molecular weight compounds including peptides with antimicrobial properties which can be exploited for biotechnological purposes. Finally, in their review, J. M. Miller and E. J. 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引用次数: 2
摘要
许多工业/生物技术过程发生在极端的温度、pH值、盐度或压力条件下,这些条件不适合模型真核生物或普通嗜中性、嗜中温和原核微生物的蛋白质活性。相比之下,古生菌提供了大量的极端微生物,它们表达的蛋白质能够在最恶劣的生物物理条件下保持适当的折叠和功能。对这组生物的研究发现,与传统的同源物相比,古细菌的酶和蛋白质具有不同寻常的特性。此外,例如,由于它们易于生产和更好的x射线晶体学样品,古细菌蛋白质通常比它们的真核生物等价物更便于进行结构生物学研究。由此获得的知识可以为商业生物技术应用开辟道路。近年来,随着解码全基因组和宏基因组的下一代测序技术的出现,以及发展“绿色”工业过程的压力,报道的新古细菌蛋白质的比率显着增加,从而再次扩大了它们的应用潜力。在本期《古生菌》特刊中,我们介绍了一些论文,这些论文涉及古生菌蛋白作为生物技术和研究各个领域的工具。DNA和RNA连接酶是活细胞中必不可少的酶,在分子生物学中有着广泛的应用。m.t anabe等人的一篇综述讨论了DNA连接酶的用途以及通过结构研究破译其催化机制的最新进展,并描述了蛋白质工程如何在广泛的温度范围内提高古细菌DNA连接酶的连接效率。在另一篇关于连接酶的论文中,C. R. Chambers和W. M. Patrick介绍了包括RNA连接酶在内的古菌核酸连接酶的现状,强调了它们与生物技术相关的显著特性,并讨论了通过定向诱变来修饰古菌RNA连接酶的活性,以开发更有效的分子生物学方案。J. a . Littlechild回顾了关于一系列嗜热古菌蛋白的发现和潜在应用的研究,说明了古菌酶在各种工业生物催化中的作用。然后,V. M. Gumerov等人的一篇文章描述了一种新型的耐热多功能β-糖苷酶的特性,这种酶来自于saccharovorans,对葡萄糖具有高耐受性,这是用于处理木质纤维素生物质的酶所期望的特性。学术界。Wu等人发表了一篇综述,概述了工程中使用的策略,并描述了三种不同形式的可溶性氢化酶I,这种酶来自超嗜热的炽热焦球菌,这种酶已被用于体外产氢。古细菌不仅对催化应用感兴趣。J. C. Charlesworth和B. P. Burns全面概述了古细菌低分子量化合物,包括具有抗菌特性的肽,可用于生物技术目的。最后,在他们的综述中,j.m. Miller和e.j. Enemark用MCM解旋酶举例说明,古细菌同源物的晶体学如何有助于破译其真核版本的结构/功能关系,而真核版本更难结晶。我们希望这期特刊将为读者提供一些古生菌蛋白的不同应用的最新概述,并可能促进这一尚未开发的领域的进一步研究,并为未来的许多生物技术应用提供丰富的前景。Frederic Pecorari Vickery L. Arcus Juergen Wiegel
Many industrial/biotechnological processes take place under extreme conditions of temperature, pH, salinity, or pressure which are not suitable for activities of proteins from model eukaryotic or common neutrophilic, mesophilic, and prokaryotic microorganisms. In contrast, Archaea offer a large panel of extremophile organisms that express proteins that are able to remain properly folded and functional under the harshest biophysical conditions.
The study of this group of organisms has uncovered archaeal enzymes and proteins with unusual properties compared to their traditional homologues. In addition, with their ease of production and better-behaved samples for X-ray crystallography, for example, archaeal proteins are often more convenient for structural biology studies than their eukaryotic equivalents. The knowledge thus gained can open routes to commercial biotechnological applications. These last years, with the emergence of next generation sequencing techniques to decode whole genomes and metagenomes and the pressure to develop “greener” industrial processes, the rate of new archaeal proteins reported has significantly increased, thereby widening again their potential of applications. In this special issue of Archaea, we present selected papers dealing with the uses of archaeal proteins as tools for various fields of biotechnologies and research.
DNA and RNA ligases are essential enzymes in living cells and have applications in molecular biology. A review by M. Tanabe et al. discusses the uses of DNA ligases and recent progress in deciphering their catalytic mechanisms via structural studies, and they describe how protein engineering can improve ligation efficiency of an archaeal DNA ligase over a broad temperature range. In another paper on ligases, C. R. Chambers and W. M. Patrick present the current state of knowledge on archaeal nucleic acid ligases including RNA ligases, highlighting their remarkable properties relevant to biotechnologists, and they discuss the modifications of the activities of archaeal RNA ligases by directed mutagenesis to develop more efficient molecular biology protocols.
J. A. Littlechild reviews research regarding the discovery and potential applications of a range of thermophilic archaeal proteins, illustrating the power of archaeal enzymes for various industrial biocatalysis. Then, an article by V. M. Gumerov et al. describes the characterization of a novel thermostable and multifunctional β-glycosidase from Acidilobus saccharovorans that displays a high tolerance to glucose, a desired property for such enzymes used to process lignocellulose biomass. C.-H. Wu et al. present a review summarizing the strategies used in engineering and characterizing three different forms of soluble hydrogenase I from the hyperthermophile Pyrococcus furiosus, an enzyme which has been used in vitro for hydrogen production.
Archaea are not only interesting for catalysis applications. J. C. Charlesworth and B. P. Burns give a comprehensive overview of archaeal low-molecular weight compounds including peptides with antimicrobial properties which can be exploited for biotechnological purposes. Finally, in their review, J. M. Miller and E. J. Enemark exemplify with MCM helicases how crystallography of archaeal homologues can be helpful to decipher structure/function relationships of their eukaryotic versions which are more difficult to crystallize.
We hope this special issue will provide the reader with an up-to-date overview of some of the diverse applications of archaeal proteins and, perhaps, prompt further research in this largely untapped field with rich prospects for the future of many biotechnological applications.
Frederic Pecorari
Vickery L. Arcus
Juergen Wiegel
期刊介绍:
Archaea is a peer-reviewed, Open Access journal that publishes original research articles as well as review articles dealing with all aspects of archaea, including environmental adaptation, enzymology, genetics and genomics, metabolism, molecular biology, molecular ecology, phylogeny, and ultrastructure. Bioinformatics studies and biotechnological implications of archaea will be considered. Published since 2002, Archaea provides a unique venue for exchanging information about these extraordinary prokaryotes.