Sulfurtransferases as essential players during dissimilatory sulfur oxidation

硫转移酶是异化硫氧化过程中的重要参与者

• 批准号: 184061176
• 负责人: Privatdozentin Dr. Christiane Dahl
• 金额: --
• 依托单位: Institut für Mikrobiologie und Biotechnologie (IfMB)
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2010
• 资助国家: 德国
• 起止时间: 2009-12-31 至 2018-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/184061176?language=en
• 关键词: Sulfurtransferases; essential; players; during; dissimilatory

Persulfide groups are chemically versatile and participate in a wide array of biochemical pathways. Whilst it is well documented that persulfurated proteins supply a number of important and elaborate biosynthetic pathways with sulfane sulfur, this project aims at exploring the exact contribution of sulfurtransferase-catalyzed reactions to oxidative sulfur metabolism. We already collected basic information on the extensive sulfur-trafficking system occurring in the cytoplasm of sulfur oxidizing bacteria pursuing the Dsr (dissimilatory sulfite reductase) pathway of sulfur oxidation. In addition, we gathered biochemical and bioinformatic evidence pointing at the so-called heterodisulfide-reductase (Hdr) -like system as a wide-spread alternative sulfite-generating system in sulfur-oxidizing prokaryotes. Sulfur-trafficking was established to also be of pivotal importance in organisms pursuing this pathway and thus emerges as a central and common element during dissimilatory sulfur oxidation. The present project will address two major questions: (1.) What is the exact series of events during protein-bound sulfur oxidation via the Dsr pathway? (2.) Does the Hdr-like system indeed work a sulfite-generating system and how exactly are sulfur transfer reactions involved? To solve these questions, biochemical characterization of proteins (reconstitution of enzyme systems in vitro, identification of substrates and products), protein interaction studies, and gene expression profiling will be combined with gene inactivation and complementation studies (growth experiments with wild type, defined mutant and complemented mutants strains) as well as with molecular genetic techniques. The genetically accessible purple sulfur bacterium Allochromatium vinosum will serve as the model organism for the studies on sulfur transfer reactions and oxidation of protein-bound sulfur via the Dsr system, while Thioalkalivibrio and Thiorhdospira species as well as the genetically accessible Alphaproteobacterium Hyphomicrobium denitrificans will be used for elucidating sulfur transfer reactions and oxidation of protein-bound sulfur associated with the Hdr-like system. Ultimately, our results are expected to completely unravel the networks of sulfur transfer reactions occurring in sulfur oxidizing prokaryotes, to add new reactions and proteins to persulfide group biochemistry and to clarify a new pathway of sulfur oxidation.

过硫化物基团在化学上是通用的，并且参与广泛的生物化学途径。虽然它是有据可查的，全硫化蛋白质提供了一些重要的和复杂的生物合成途径与硫烷硫，该项目的目的是探索硫转移酶催化的反应氧化硫代谢的确切贡献。我们已经收集了关于硫氧化细菌细胞质中发生的广泛硫运输系统的基本信息，这些硫氧化细菌追求硫氧化的Dsr（异化亚硫酸盐还原酶）途径。此外，我们收集了生物化学和生物信息学证据，指出所谓的杂二硫化物还原酶（HDR）样系统作为硫氧化原核生物中广泛存在的替代亚硫酸盐生成系统。硫运输也被确定为在追求这一途径的生物体中具有关键重要性，因此在异化硫氧化过程中作为一个中心和共同的元素出现。本项目将解决两个主要问题：（1）。通过Dsr途径蛋白质结合硫氧化过程中的确切事件系列是什么？（2.）类Hdr系统是否真的是一个亚硫酸盐生成系统？硫转移反应到底是如何参与的？为了解决这些问题，蛋白质的生物化学表征（体外酶系统的重建，底物和产物的鉴定），蛋白质相互作用研究和基因表达谱将与基因失活和互补研究（野生型，确定的突变体和补充突变体菌株的生长实验）以及分子遗传学技术相结合。遗传上可获得的紫色硫细菌Allochromatium vinosum将作为研究硫转移反应和通过Dsr系统氧化蛋白质结合硫的模式生物，而硫碱弧菌和硫螺旋菌属物种以及遗传上可获得的Alphaproteobacterium Hyphomicrobium plasticans将用于阐明硫转移反应和与Hdr-样系统相关的蛋白质结合硫的氧化。最终，我们的研究结果有望完全解开硫氧化原核生物中发生的硫转移反应网络，为过硫化物基团生物化学添加新的反应和蛋白质，并阐明硫氧化的新途径。

项目成果

The functional diversity of the prokaryotic sulfur carrier protein TusA.

原核硫载体蛋白TusA的功能多样性

• DOI: 10.1016/bs.ampbs.2019.07.004
• 发表时间: 2019
• 期刊: Advances in microbial physiology
• 作者: Tanabe;Leimkühler
• 通讯作者: Leimkühler

A protein trisulfide couples dissimilatory sulfate reduction to energy conservation

• DOI: 10.1126/science.aad3558
• 发表时间: 2015-12
• 期刊: Science
• 影响因子: 56.9
• 作者: A. A. Santos-A.;S. Venceslau;Fabian Grein;W. Leavitt;C. Dahl;D. Johnston;I. Pereira

DsrL Mediates Electron Transfer between NADH and rDsrAB in Allochromatium vinosum.

• DOI: 10.1111/1462-2920.14899
• 发表时间: 2019-12
• 期刊: Environmental microbiology
• 影响因子: 5.1
• 作者: Maria Löffler;Julia Feldhues;S. Venceslau;Lydia Kammler;Fabian Grein;I. Pereira;C. Dahl