Pablo A Cea, F. González-Ordenes, V. Castro-Fernández, V. Guixé
{"title":"甲藻目adp依赖性糖激酶嗜盐性的评价","authors":"Pablo A Cea, F. González-Ordenes, V. Castro-Fernández, V. Guixé","doi":"10.3390/MOL2NET-04-06138","DOIUrl":null,"url":null,"abstract":"Halophilic organisms have evolved to live in environments of high salinity, therefore theirmolecular machinery has adapted to carry out its functions in presence of molar concentrations ofsalt. Most of the work aimed to understand the structural adaptations of these proteins has beendone using proteins from the archeon class Halobacteria. Proteins from these organisms arecharacterized by a low abundance of basic residues and a high amount of acidic residues, whichaccumulate on the protein surface, coupled with a reduction of bulky hydrophobic residues in itscore [1]. Nevertheless, halophilic organisms have been reported in a wide variety of taxa, includingother archaea orders, which their adaptation mechanisms have not been explored. To evaluate theubiquity of the protein structural adaptations found in Halobacteria, we built homology modelsof ADP-dependent kinases from halophilic and non-halophilic organisms of the archaeal orderMethanosarcinales and compared them to models from Halobacterial and Eucariotic proteins.Our results show that proteins from halophilic organisms of the Methanosarcinales order do notshow the classical bias in amino acid composition observed in Halobacteria, like the reduction ofthe hydrophobic core and negative surface charge. However, experimental characterization of theADP-dependent phosphofructokinase of the halophilic organism Methanohalobium evestigatum(from Methanosarcinales order) confirmed that the protein is indeed halotolerant, and thischaracter can be further exacerbated in presence of osmolytes commonly found on halophilicarchaea, like betaine [2]. These results suggest that the adaptations required to maintain thestructure and function of a protein in extreme salt concentrations can vary widely betweendifferent organisms. These adaptations do not rely exclusively on the amino acidic composition,being instead a product of the coevolutionary process between the protein and its intracellularenvironment. Fondecyt 1150460 \nReferences \n[1] Graziano, G., a Merlino, A. (2014). Molecular bases of protein halotolerance. Biochimica et Biophysica Acta(BBA) - Proteins and Proteomics, 1844(4), 850–858[2] Sowers, K. R., a Gunsalus, R. P. (1995). Halotolerance in Methanosarcina spp.: Role of N (sup (epsilon))-Acetyl-(beta)-Lysine,(alpha)-Glutamate, Glycine Betaine, and K (sup+) as Compatible Solutes for OsmoticAdaptation. Applied and environmental microbiology, 61(12), 4382-4388.","PeriodicalId":20475,"journal":{"name":"Proceedings of MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition","volume":"10 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Assessing the halophilic character of ADP-dependent sugar kinases from the archeon order Methanosarcinales\",\"authors\":\"Pablo A Cea, F. González-Ordenes, V. Castro-Fernández, V. Guixé\",\"doi\":\"10.3390/MOL2NET-04-06138\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Halophilic organisms have evolved to live in environments of high salinity, therefore theirmolecular machinery has adapted to carry out its functions in presence of molar concentrations ofsalt. Most of the work aimed to understand the structural adaptations of these proteins has beendone using proteins from the archeon class Halobacteria. Proteins from these organisms arecharacterized by a low abundance of basic residues and a high amount of acidic residues, whichaccumulate on the protein surface, coupled with a reduction of bulky hydrophobic residues in itscore [1]. Nevertheless, halophilic organisms have been reported in a wide variety of taxa, includingother archaea orders, which their adaptation mechanisms have not been explored. To evaluate theubiquity of the protein structural adaptations found in Halobacteria, we built homology modelsof ADP-dependent kinases from halophilic and non-halophilic organisms of the archaeal orderMethanosarcinales and compared them to models from Halobacterial and Eucariotic proteins.Our results show that proteins from halophilic organisms of the Methanosarcinales order do notshow the classical bias in amino acid composition observed in Halobacteria, like the reduction ofthe hydrophobic core and negative surface charge. However, experimental characterization of theADP-dependent phosphofructokinase of the halophilic organism Methanohalobium evestigatum(from Methanosarcinales order) confirmed that the protein is indeed halotolerant, and thischaracter can be further exacerbated in presence of osmolytes commonly found on halophilicarchaea, like betaine [2]. These results suggest that the adaptations required to maintain thestructure and function of a protein in extreme salt concentrations can vary widely betweendifferent organisms. These adaptations do not rely exclusively on the amino acidic composition,being instead a product of the coevolutionary process between the protein and its intracellularenvironment. Fondecyt 1150460 \\nReferences \\n[1] Graziano, G., a Merlino, A. (2014). Molecular bases of protein halotolerance. Biochimica et Biophysica Acta(BBA) - Proteins and Proteomics, 1844(4), 850–858[2] Sowers, K. R., a Gunsalus, R. P. (1995). Halotolerance in Methanosarcina spp.: Role of N (sup (epsilon))-Acetyl-(beta)-Lysine,(alpha)-Glutamate, Glycine Betaine, and K (sup+) as Compatible Solutes for OsmoticAdaptation. 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引用次数: 0
摘要
嗜盐生物已经进化到可以生活在高盐度的环境中,因此它们的分子机制已经适应了在盐的摩尔浓度下执行其功能。大多数旨在了解这些蛋白质的结构适应性的工作都是利用来自嗜盐菌纲的蛋白质完成的。来自这些生物的蛋白质具有低丰度的碱性残基和大量的酸性残基的特征,这些残基在蛋白质表面积累,并且其分数中大量疏水残基的减少[1]。尽管如此,据报道,在包括其他古菌目在内的各种分类群中都发现了嗜盐生物,但它们的适应机制尚未得到探索。为了评估在盐细菌中发现的蛋白质结构适应性的普遍性,我们从嗜盐和非嗜盐的古细菌目methanosarcinales中建立了adp依赖性激酶的同源模型,并将它们与盐细菌和真核细菌的蛋白质模型进行了比较。我们的研究结果表明,来自Methanosarcinales目的嗜盐生物的蛋白质不表现出在盐杆菌中观察到的氨基酸组成的经典偏倚,如疏水核心的减少和表面负电荷的减少。然而,对嗜盐菌Methanohalobium evestiatum(来自Methanosarcinales目)的adp依赖性磷酸果糖激酶的实验表征证实,该蛋白确实具有耐盐性,并且在嗜盐古菌中常见的渗透物(如甜菜碱)存在时,这种特性会进一步加剧[2]。这些结果表明,在极端盐浓度下维持蛋白质结构和功能所需的适应性在不同的生物体之间差异很大。这些适应并不完全依赖于氨基酸组成,而是蛋白质与其细胞内环境共同进化过程的产物。[1] Graziano, G., a . Merlino, a .(2014)。蛋白质耐盐性的分子基础。[2]张建军,张建军,张建军,等(1995).生物化学与生物物理学报,1844(4),850-858。Methanosarcina的耐盐性:N (sup (epsilon))-乙酰-(β)-赖氨酸,(α)-谷氨酸,甘氨酸甜菜碱和K (sup+)作为渗透适应的相容溶质的作用。微生物学通报,2011(6),482 - 488。
Assessing the halophilic character of ADP-dependent sugar kinases from the archeon order Methanosarcinales
Halophilic organisms have evolved to live in environments of high salinity, therefore theirmolecular machinery has adapted to carry out its functions in presence of molar concentrations ofsalt. Most of the work aimed to understand the structural adaptations of these proteins has beendone using proteins from the archeon class Halobacteria. Proteins from these organisms arecharacterized by a low abundance of basic residues and a high amount of acidic residues, whichaccumulate on the protein surface, coupled with a reduction of bulky hydrophobic residues in itscore [1]. Nevertheless, halophilic organisms have been reported in a wide variety of taxa, includingother archaea orders, which their adaptation mechanisms have not been explored. To evaluate theubiquity of the protein structural adaptations found in Halobacteria, we built homology modelsof ADP-dependent kinases from halophilic and non-halophilic organisms of the archaeal orderMethanosarcinales and compared them to models from Halobacterial and Eucariotic proteins.Our results show that proteins from halophilic organisms of the Methanosarcinales order do notshow the classical bias in amino acid composition observed in Halobacteria, like the reduction ofthe hydrophobic core and negative surface charge. However, experimental characterization of theADP-dependent phosphofructokinase of the halophilic organism Methanohalobium evestigatum(from Methanosarcinales order) confirmed that the protein is indeed halotolerant, and thischaracter can be further exacerbated in presence of osmolytes commonly found on halophilicarchaea, like betaine [2]. These results suggest that the adaptations required to maintain thestructure and function of a protein in extreme salt concentrations can vary widely betweendifferent organisms. These adaptations do not rely exclusively on the amino acidic composition,being instead a product of the coevolutionary process between the protein and its intracellularenvironment. Fondecyt 1150460
References
[1] Graziano, G., a Merlino, A. (2014). Molecular bases of protein halotolerance. Biochimica et Biophysica Acta(BBA) - Proteins and Proteomics, 1844(4), 850–858[2] Sowers, K. R., a Gunsalus, R. P. (1995). Halotolerance in Methanosarcina spp.: Role of N (sup (epsilon))-Acetyl-(beta)-Lysine,(alpha)-Glutamate, Glycine Betaine, and K (sup+) as Compatible Solutes for OsmoticAdaptation. Applied and environmental microbiology, 61(12), 4382-4388.