Protein adaptations in archaeal extremophiles

Archaea

Volumn 2013, Issue , 2013, Pages

  Reed, Christopher J ^a   Lewis, Hunter ^a   Trejo, Eric ^a   Winston, Vern ^b   Evilia, Caryn ^a  

^a IDAHO STATE UNIVERSITY   (United States)

^b Nucl Eng Idaho State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN;

ADAPTATION; ARCHAEON; CHEMISTRY; COLD; ENVIRONMENT; GENETICS; HEAT; METABOLISM; PH; REVIEW; SALINITY;

ADAPTATION, PHYSIOLOGICAL; ARCHAEA; ARCHAEAL PROTEINS; COLD TEMPERATURE; ENVIRONMENT; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; SALINITY;

EID: 84885602847     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2013/373275     Document Type: Review

References (110)

1. Kletzin A., General Characteristics and Important Model Organisms 2007 Washington, DC, USA ASM Press. Archaea: Molecular and Cellular Biology, Edited by: R. Cavicchioli
2. Schleper C., Jurgens G., Jonuscheit M., Genomic studies of uncultivated archaea. Nature Reviews Microbiology 2005 3 6 479 488 2-s2.0-19144373707 10.1038/nrmicro1159 (Pubitemid 40716174)
3. Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D., Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis. Genome Research 2005 15 10 1336 1343 2-s2.0-25844454133 10.1101/gr.3952905 (Pubitemid 41400899)
4. Baker-Austin C., Dopson M., Life in acid: pH homeostasis in acidophiles. Trends in Microbiology 2007 15 4 165 171 2-s2.0-34047264809 10.1016/j.tim.2007. 02.005 (Pubitemid 46546467)
5. Sharma A., Kawarabayasi Y., Satyanarayana T., Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications. Extremophiles 2012 16 1 1 19 2-s2.0-84155188952 10.1007/s00792-011-0402-3
6. Grant W. D., Life at low water activity. Philosophical Transactions of the Royal Society B 2004 359 1448 1249 1266
7. Ebel C., Costenaro L., Pascu M., Faou P., Kernel B., Proust-De Martin F., Zaccai G., Solvent interactions of halophilic malate dehydrogenase. Biochemistry 2002 41 44 13234 13244 2-s2.0-0037027320 10.1021/bi0258290 (Pubitemid 35244713)
8. Mevarech M., Frolow F., Gloss L. M., Halophilic enzymes: proteins with a grain of salt. Biophysical Chemistry 2000 86 2-3 155 164 2-s2.0-0034734270 10.1016/S0301-4622(00)00126-5 (Pubitemid 30665604)
9. Wright D. B., Banks D. D., Lohman J. R., Hilsenbeck J. L., Gloss L. M., The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. Journal of Molecular Biology 2002 323 2 327 344 2-s2.0-0036408309 10.1016/S0022-2836(02)00916-6 (Pubitemid 35283695)
10. Hauenstein S., Zhang C.-M., Hou Y.-M., Perona J. J., Shape-selective RNA recognition by cysteinyl-tRNA synthetase. Nature Structural and Molecular Biology 2004 11 11 1134 1141 2-s2.0-7544240563 10.1038/nsmb849 (Pubitemid 39453344)
11. Pettersen E. F., Goddard T. D., Huang C. C., Couch G. S., Greenblatt D. M., Meng E. C., Ferrin T. E., UCSF chimera-a visualization system for exploratory research and analysis. Journal of Computational Chemistry 2004 25 13 1605 1612 2-s2.0-4444221565 10.1002/jcc.20084
12. Cacciapuoti G., Fuccio F., Petraccone L., Role of disulfide bonds in conformational stability and folding of 5'-deoxy-5'-methylthioadenosine phosphorylase II from the hyperthermophilic archaeon Sulfolobus solfataricus. Biochimica et Biophysica Acta 2012 1824 10 1136 1143
13. Szilágyi A., Závodszky P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 2000 8 5 493 504 2-s2.0-0039116206 10.1016/S0969-2126(00)00133-7 (Pubitemid 30304547)
14. Vieille C., Zeikus G. J., Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiology and Molecular Biology Reviews 2001 65 1 1 43 2-s2.0-0035098779 10.1128/MMBR.65.1.1-43.2001 (Pubitemid 32204286)
15. Connaris H., Chaudhuri J. B., Danson M. J., Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. Biotechnology and Bioengineering 1999 64 1 38 45 (Pubitemid 29252310)
16. Evilia C., Ming X., Dassarma S., Hou Y.-M., Aminoacylation of an unusual tRNACys from an extreme halophile. RNA 2003 9 7 794 801 2-s2.0-0038382878 10.1261/rna.5320603 (Pubitemid 36734777)
17. Yonezawa Y., Tokunaga H., Ishibashi M., Taura S., Tokunaga M., Cloning, expression, and efficient purification in Escherichia coli of a halophilic nucleoside diphosphate kinase from the moderate halophile Halomonas sp. #593. Protein Expression and Purification 2003 27 1 128 133 2-s2.0-0042284085 10.1016/S1046-5928(02)00594-6 (Pubitemid 37096478)
18. Evilia C., Hou Y.-M., Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase. Biochemistry 2006 45 22 6835 6845 2-s2.0-33744960237 10.1021/bi0521386 (Pubitemid 43856669)
19. Bae E., Phillips G. N. Jr., Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. The Journal of Biological Chemistry 2004 279 27 28202 28208 2-s2.0-3142653228 10.1074/jbc.M401865200 (Pubitemid 38900096)
20. Kumar S., Nussinov R., Different roles of electrostatics in heat and in cold: adaptation by citrate synthase. ChemBioChem 2004 5 3 280 290 2-s2.0-4043175563 10.1002/cbic.200300627 (Pubitemid 39257121)
21. Tehei M., Zaccai G., Adaptation to high temperatures through macromolecular dynamics by neutron scattering. FEBS Journal 2007 274 16 4034 4043 2-s2.0-34547743840 10.1111/j.1742-4658.2007.05953.x (Pubitemid 47228642)
22. Powers E. T., Balch W. E., Diversity in the origins of proteostasis networks-a driver for protein function in evolution. Nature Reviews Molecular Cell Biology 2013 14 4 237 248
23. Dill K. A., Ozkan S. B., Shell M. S., Weikl T. R., The protein folding problem. Annual Review of Biophysics 2008 37 289 316 2-s2.0-48249134448 10.1146/annurev.biophys.37.092707.153558
24. Fitzkee N. C., Fleming P. J., Gong H., Panasik N. Jr., Street T. O., Rose G. D., Are proteins made from a limited parts list? Trends in Biochemical Sciences 2005 30 2 73 80 2-s2.0-13244258557 10.1016/j.tibs.2004.12.005 (Pubitemid 40187299)
25. Tomazic S. J., Klibanov A. M., Mechanisms of irreversible thermal inactivation of Bacillus α -amylases. The Journal of Biological Chemistry 1988 263 7 3086 3091 2-s2.0-0023834870 (Pubitemid 18072756)
26. Mayer F., Küper U., Meyer C., Daxer S., Müller V., Rachel R., Huber H., AMP-forming acetyl coenzyme a synthetase in the outermost membrane of the hyperthermophilic crenarchaeon Ignicoccus hospitalis. Journal of Bacteriology 2012 194 6 1572 1581 2-s2.0-84857961488 10.1128/JB.06130-11
27. Bräsen C., Urbanke C., Schönheit P., A novel octameric AMP-forming acetyl-CoA synthetase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. FEBS Letters 2005 579 2 477 482 2-s2.0-11844296747 10.1016/j.febslet.2004.12.016 (Pubitemid 40092430)
28. Ingram-Smith C., Smith K. S., AMP-forming acetyl-CoA synthetases in Archaea show unexpected diversity in substrate utilization. Archaea 2007 2 2 95 107 2-s2.0-34250832670 (Pubitemid 46972047)
29. Del Vecchio P., Elias M., Merone L., Graziano G., Dupuy J., Mandrich L., Carullo P., Fournier B., Rochu D., Rossi M., Masson P., Chabriere E., Manco G., Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles 2009 13 3 461 470 2-s2.0-67349172630 10.1007/s00792-009-0231-9
30. Park J. T., Song H. N., Jung T. Y., A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus. Biochimica Et Biophysica Acta 2013 1834 1 380 386
31. Park K.-H., Kim T.-J., Cheong T.-K., Kim J.-W., Oh B.-H., Svensson B., Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α -amylase family. Biochimica et Biophysica Acta 2000 1478 2 165 185 2-s2.0-0034705064 10.1016/S0167-4838(00)00041-8 (Pubitemid 30312875)
32. Vihinen M., Relationship of protein flexibility to thermostability. Protein Engineering 1987 1 6 477 480 2-s2.0-0023557882
33. Cacciapuoti G., Porcelli M., Bertoldo C., De Rosa M., Zappia V., Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds. The Journal of Biological Chemistry 1994 269 40 24762 24769 2-s2.0-0027992738
34. Boutz D. R., Cascio D., Whitelegge J., Perry L. J., Yeates T. O., Discovery of a thermophilic protein complex stabilized by topologically interlinked chains. Journal of Molecular Biology 2007 368 5 1332 1344 2-s2.0-34247215529 10.1016/j.jmb.2007.02.078 (Pubitemid 46621191)
35. Woycechowsky K. J., Raines R. T., The CXC motif: a functional mimic of protein disulfide isomerase. Biochemistry 2003 42 18 5387 5394 2-s2.0-0038558159 10.1021/bi026993q (Pubitemid 36560435)
36. Wilkinson B., Gilbert H. F., Protein disulfide isomerase. Biochimica et Biophysica Acta 2004 1699 1-2 35 44 2-s2.0-2542435948 10.1016/j.bbapap.2004.02. 017 (Pubitemid 38680792)
37. Karshikoff A., Ladenstein R., Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends in Biochemical Sciences 2001 26 9 550 556 2-s2.0-0035448574 10.1016/S0968-0004(01)01918-1 (Pubitemid 32823440)
38. Hendsch Z. S., Tidor B., Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Science 1994 3 2 211 226 2-s2.0-0028204490 (Pubitemid 24086354)
39. Chan C.-H., Yu T.-H., Wong K.-B., Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding. PLoS ONE 2011 6 6 2-s2.0-79959612799 10.1371/journal.pone.0021624 e21624
40. Fukuchi S., Nishikawa K., Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. Journal of Molecular Biology 2001 309 4 835 843 2-s2.0-0035876479 10.1006/jmbi.2001.4718 (Pubitemid 32575078)
41. Lee C.-F., Makhatadze G. I., Wong K.-B., Effects of charge-to-alanine substitutions on the stability of ribosomal protein L30e from Thermococcus celer. Biochemistry 2005 44 51 16817 16825 2-s2.0-29344472867 10.1021/bi0519654 (Pubitemid 43007210)
42. Liu Y. F., Zhang N., Liu X., Molecular mechanism underlying the interaction of typical Sac10b family proteins with DNA. PLoS ONE 7 4 e34986 10.1371/journal.pone.0034986
43. Mamat B., Roth A., Grimm C., Ermler U., Tziatzios C., Schubert D., Thauer R. K., Shima S., Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship. Protein Science 2002 11 9 2168 2178 2-s2.0-0036708002 10.1110/ps.0211002 (Pubitemid 34919620)
44. Breitung J., Borner G., Scholz S., Linder D., Stetter K. O., Thauer R. K., Salt dependence, kinetic properties and catalytic mechanism of N -formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri. European Journal of Biochemistry 1992 210 3 971 981 2-s2.0-0027076754 10.1111/j.1432-1033.1992.tb17502.x (Pubitemid 23015799)
45. Unsworth L. D., Van Der Oost J., Koutsopoulos S., Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications. FEBS Journal 2007 274 16 4044 4056 2-s2.0-34547747311 10.1111/j.1742-4658.2007.05954.x (Pubitemid 47228643)
46. De Champdoré M., Staiano M., Rossi M., D'Auria S., Proteins from extremophiles as stable tools for advanced biotechnological applications of high social interest. Journal of the Royal Society Interface 2007 4 13 183 191 2-s2.0-34047100353 10.1098/rsif.2006.0174 (Pubitemid 46513050)
47. Fang J., Zhang L., Bazylinski D. A., Deep-sea piezosphere and piezophiles: geomicrobiology and biogeochemistry. Trends in Microbiology 2010 18 9 413 422 2-s2.0-77956187864 10.1016/j.tim.2010.06.006
48. Hay S., Evans R. M., Levy C., Loveridge E. J., Wang X., Leys D., Allemann R. K., Scrutton N. S., Are the catalytic properties of enzymes from piezophilic organisms pressure adapted? ChemBioChem 2009 10 14 2348 2353 2-s2.0-70350536780 10.1002/cbic.200900367
49. Boonyaratanakornkit B. B., Park C. B., Clark D. S., Pressure effects on intra- and intermolecular interactions within proteins. Biochimica et Biophysica Acta 2002 1595 1-2 235 249 2-s2.0-0037171151 10.1016/S0167-4838(01)00347-8 (Pubitemid 34442647)
50. Di Giulio M., A comparison of proteins from Pyrococcus furiosus and Pyrococcus abyssi: barophily in the physicochemical properties of amino acids and in the genetic code. Gene 2005 346 1 6 2-s2.0-14744303570 10.1016/j.gene.2004.10.008 (Pubitemid 40332618)
51. Mombelli E., Shehi E., Fusi P., Tortora P., Exploring hyperthermophilic proteins under pressure: theoretical aspects and experimental findings. Biochimica et Biophysica Acta 2002 1595 1-2 392 396 2-s2.0-0037171127 10.1016/S0167-4838(01)00361-2 (Pubitemid 34442661)
52. Consonni R., Santomo L., Fusi P., Tortora P., Zetta L., A single-point mutation in the extreme heat- and pressure- resistant Sso7d protein from Sulfolobus solfataricus leads to a major rearrangement of the hydrophobic core. Biochemistry 1999 38 39 12709 12717 2-s2.0-0033613266 10.1021/bi9911280 (Pubitemid 29463267)
53. Fusi P., Goossens K., Consonni R., Extreme heat- and pressure-resistant 7-kDa protein P2 from the archaeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution. Proteins 1997 29 3 381 390 (Pubitemid 27484228)
54. Sun M. M. C., Caillot R., Mak G., Robb F. T., Clark D. S., Mechanism of pressure-induced thermostabilization of proteins: studies of glutamate dehydrogenases from the hyperthermophile Thermococcus litoralis. Protein Science 2001 10 9 1750 1757 2-s2.0-0034853883 10.1110/ps.4001 (Pubitemid 32848771)
55. Rosenbaum E., Gabel F., Durá M. A., Finet S., Cléry-Barraud C., Masson P., Franzetti B., Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii. Archives of Biochemistry and Biophysics 2012 517 2 104 110 2-s2.0-84855450985 10.1016/j.abb.2011.07.017
56. Simonato F., Campanaro S., Lauro F. M., Vezzi A., D'Angelo M., Vitulo N., Valle G., Bartlett D. H., Piezophilic adaptation: a genomic point of view. Journal of Biotechnology 2006 126 1 11 25 2-s2.0-33748749355 10.1016/j.jbiotec.2006.03.038 (Pubitemid 44402769)
57. Abe F., Horikoshi K., The biotechnological potential of piezophiles. Trends in Biotechnology 2001 19 3 102 108 2-s2.0-0035283618 10.1016/S0167- 7799(00)01539-0 (Pubitemid 32155430)
58. Huang Y., Krauss G., Cottaz S., Driguez H., Lipps G., A highly acid-stable and thermostable endo- β -glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus. Biochemical Journal 2005 385 2 581 588 2-s2.0-12944280876 10.1042/BJ20041388 (Pubitemid 40173970)
59. Golyshina O. V., Timmis K. N., Ferroplasma and relatives, recently discovered cell wall-lacking archaea making a living in extremely acid, heavy metal-rich environments. Environmental Microbiology 2005 7 9 1277 1288 2-s2.0-23944456864 10.1111/j.1462-2920.2005.00861.x (Pubitemid 41204922)
60. Jackson B. R., Noble C., Lavesa-Curto M., Bond P. L., Bowater R. P., Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon " Ferroplasma acidarmanus " Fer1. Extremophiles 2007 11 2 315 327 2-s2.0-33847286448 10.1007/s00792-006-0041-2
61. Magnet S., Blanchard J. S., Mechanistic and kinetic study of the ATP-dependent DNA ligase of Neisseria meningitidis. Biochemistry 2004 43 3 710 717 2-s2.0-1642453835 10.1021/bi0355387 (Pubitemid 38114058)
62. Rohwerder T., Gehrke T., Kinzler K., Sand W., Bioleaching review part A: progress in bioleaching: fundamentals and mechanisms of bacterial metal sulfide oxidation. Applied Microbiology and Biotechnology 2003 63 3 239 248 2-s2.0-1642480180 10.1007/s00253-003-1448-7 (Pubitemid 38130572)
63. Luisa Tutino M., Di Prisco G., Marino G., De Pascale D., Cold-adapted esterases and lipases: from fundamentals to application. Protein and Peptide Letters 2009 16 10 1172 1180 2-s2.0-69549097399 10.2174/092986609789071270
64. Smalas A. O., Leiros H. K., Os V., Cold adapted enzymes. Biotechnology Annual Review 2000 6 1 57 (Pubitemid 41081534)
65. Dong X., Chen Z., Psychrotolerant methanogenic archaea: diversity and cold adaptation mechanisms. Science China Life Sciences 2012 55 5 415 421
66. Feller G., Protein stability and enzyme activity at extreme biological temperatures. Journal of Physics 2010 22 32 323101 10.1088/0953-8984/22/32/ 323101
67. Cavicchioli R., Thomas T., Curmi P. M. G., Cold stress response in Archaea. Extremophiles 2000 4 6 321 331 2-s2.0-0034567425
68. Dassarma S., Capes M. D., Karan R., Amino acid substitutions in cold-adapted proteins from Halorubrum lacusprofundi, an extremely halophilic microbe from antarctica. PLoS ONE 2013 8 3 e58587 10.1371/journal.pone.0058587
69. Karan R., Capes M. D., DasSarma P., Cloning, overexpression, purification, and characterization of a polyextremophilic β -galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi. BMC Biotechnology 2013 13 3 10.1186/1472-6750-13-3
70. Thomas T., Cavicchioli R., Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens. FEBS Letters 1998 439 3 281 286 2-s2.0-0031762555 10.1016/S0014-5793(98)01375-1 (Pubitemid 28546660)
71. Saunders N. F. W., Thomas T., Curmi P. M. G., Mattick J. S., Kuczek E., Slade R., Davis J., Franzmann P. D., Boone D., Rusterholtz K., Feldman R., Gates C., Bench S., Sowers K., Kadner K., Aerts A., Dehal P., Detter C., Glavina T., Lucas S., Richardson P., Larimer F., Hauser L., Land M., Cavicchioli R., Mechanisms of thermal adaptatation revealed from genomes of the anatarctic Archaea Methanogenium frigidum and Methanacoccoides burtonii. Genome Research 2003 13 7 1580 1588 2-s2.0-0038824870 10.1101/gr.1180903 (Pubitemid 36874474)
72. D'Amico S., Gerday C., Feller G., Structural determinants of cold adaptation and stability in a large protein. The Journal of Biological Chemistry 2001 276 28 25791 25796 2-s2.0-0035854688 10.1074/jbc.M102741200 (Pubitemid 37412780)
73. Georlette D., Damien B., Blaise V., Depiereux E., Uversky V. N., Gerday C., Feller G., Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. The Journal of Biological Chemistry 2003 278 39 37015 37023 2-s2.0-0141596172 10.1074/jbc.M305142200 (Pubitemid 37175215)
74. Giaquinto L., Curmi P. M. G., Siddiqui K. S., Poljak A., DeLong E., DasSarma S., Cavicchioli R., Structure and function of cold shock proteins in archaea. Journal of Bacteriology 2007 189 15 5738 5748 2-s2.0-34547617526 10.1128/JB.00395-07 (Pubitemid 47206420)
75. Russell R. J. M., Gerike U., Danson M. J., Hough D. W., Taylor G. L., Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 1998 6 3 351 362 2-s2.0-0032521220 (Pubitemid 28159317)
76. Aghajari N., Van Petegem F., Villeret V., Chessa J.-P., Gerday C., Haser R., Van Beeumen J., Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 2003 50 4 636 647 2-s2.0-0037342768 10.1002/prot.10264 (Pubitemid 36330488)
77. D'Amico S., Sohier J. S., Feller G., Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic α -amylase. Journal of Molecular Biology 2006 358 5 1296 1304 2-s2.0-33646087677 10.1016/j.jmb.2006.03.004
78. Hasan F., Shah A. A., Hameed A., Industrial applications of microbial lipases. Enzyme and Microbial Technology 2006 39 2 235 251 2-s2.0-33747518326 10.1016/j.enzmictec.2005.10.016 (Pubitemid 44255568)
79. Karan R., Capes M. D., Dassarma S., Function and biotechnology of extremophilic enzymes in low water activity. Aquatic Biosystems 2012 8 1 4 10.1186/2046-9063-8-4
80. Zhang G., Huihua G., Yi L., Stability of halophilic proteins: from dipeptide attributes to discrimination classifier. International Journal of Biological Macromolecules 2013 53 1 6 10.1016/j.ijbiomac.2012.10.031
81. Britton K. L., Baker P. J., Fisher M., Ruzheinikov S., Gilmour D. J., Bonete M.-J., Ferrer J., Pire C., Esclapez J., Rice D. W., Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei. Proceedings of the National Academy of Sciences of the United States of America 2006 103 13 4846 4851 2-s2.0-33645529310 10.1073/pnas.0508854103
82. Dym O., Mevarech M., Sussman J. L., Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 1995 267 5202 1344 1346 2-s2.0-0028958071
83. Frolow F., Harel M., Sussman J. L., Mevarech M., Shoham M., Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nature Structural Biology 1996 3 5 452 458 2-s2.0-0030444879 (Pubitemid 26139445)
84. Madern D., Ebel C., Zaccai G., Halophilic adaptation of enzymes. Extremophiles 2000 4 2 91 98 2-s2.0-0034166764
85. Zhang G., Ge H., Protein hypersaline adaptation: insight from amino acids with machine learning algorithms. The Protein Journal 2013 32 4 239 245
86. Kastritis P. L., Papandreou N. C., Hamodrakas S. J., Haloadaptation: insights from comparative modeling studies of halophilic archaeal DHFRs. International Journal of Biological Macromolecules 2007 41 4 447 453 2-s2.0-34548286930 10.1016/j.ijbiomac.2007.06.005 (Pubitemid 47331635)
87. Soppa J., From genomes to function: haloarchaea as model organisms. Microbiology 2006 152 3 585 590 2-s2.0-33645103946 10.1099/mic.0.28504-0
88. Tadeo X., López-Méndez B., Trigueros T., Laín A., Castaño D., Millet O., Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biology 2009 7 12 2-s2.0-73949105836 10.1371/journal.pbio.1000257 e1000257
89. Richard S. B., Madern D., Garcin E., Zaccai G., Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 2000 39 5 992 1000 2-s2.0-0034620588 10.1021/bi991001a (Pubitemid 30075326)
90. Qvist J., Ortega G., Tadeo X., Millet O., Halle B., Hydration dynamics of a halophilic protein in folded and unfolded states. Journal of Physical Chemistry B 2012 116 10 3436 3444 2-s2.0-84858317534 10.1021/jp3000569
91. Siglioccolo A., Paiardini A., Piscitelli M., Pascarella S., Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface. BMC Structural Biology 2011 11, article 50 2-s2.0-84055213697 10.1186/1472-6807-11-50
92. Müller-Santos M., de Souza E. M., Pedrosa F. D. O., Mitchell D. A., Longhi S., Carrière F., Canaan S., Krieger N., First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui. Biochimica et Biophysica Acta 2009 1791 8 719 729 2-s2.0-67650462243 10.1016/j.bbalip.2009.03.006
93. Longo L. M., Lee J., Blaber M., Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein. Proceedings of the National Academy of Sciences of the United States of America 2013 110 6 2135 2139
94. Taupin C. M.-J., Härtlein M., Leberman R., Seryl-tRNA synthetase from the extreme halophile Haloarcula marismortui. Isolation, characterization and sequencing of the gene and its expression in Escherichia coli. European Journal of Biochemistry 1997 243 1-2 141 150 2-s2.0-0031030713 (Pubitemid 27060396)
95. Taupin C. M.-J., Leberman R., Archaeabacterial seryl-tRNA synthetases: adaptation to extreme environments and evolutionary analysis. Journal of Molecular Evolution 1999 48 4 408 420 2-s2.0-0033058712 (Pubitemid 29153360)
96. Zaccai G., Cendrin F., Haik Y., Borochov N., Eisenberg H., Stabilization of halophilic malate dehydrogenase. Journal of Molecular Biology 1989 208 3 491 500 2-s2.0-0024962259
97. Marg B.-L., Schweimer K., Sticht H., Oesterhelt D., A two- α -helix extra domain mediates the halophilic character of a plant-type ferredoxin from Halophilic Archaea. Biochemistry 2005 44 1 29 39 2-s2.0-11844249908 10.1021/bi0485169 (Pubitemid 40095704)
98. Oren A., Industrial and environmental applications of halophilic microorganisms. Environmental Technology 2010 31 8-9 825 834 2-s2.0-77953700376 10.1080/09593330903370026
99. Ishibashi M., Hayashi T., Yoshida C., Increase of salt dependence of halophilic nucleoside diphosphate kinase caused by a single amino acid substitution. Extremophiles 2013 17 4 585 591
100. Tokunaga H., Arakawa T., Tokunaga M., Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases. Protein Science 2008 17 9 1603 1610 2-s2.0-50049123899 10.1110/ps.035725.108
101. Enache M., Itoh T., Fukushima T., Usami R., Dumitru L., Kamekura M., Phylogenetic relationships within the family Halobacteriaceae inferred from rpoB′ gene and protein sequences. International Journal of Systematic and Evolutionary Microbiology 2007 57 10 2289 2295 2-s2.0-35648947338 10.1099/ijs.0.65190-0 (Pubitemid 350031704)
102. Ollivier B., Caumette P., Garcia J.-L., Mah R. A., Anaerobic bacteria from hypersaline environments. Microbiological Reviews 1994 58 1 27 38 2-s2.0-0028325766
103. Grant W. D., Half A Lifetime in soda lakes 2004 New York, NY, USA Springer. Halophilic Microorganisms, Edited by: A. Ventosa
104. Horikoshi K., Alkaliphiles: some applications of their products for biotechnology. Microbiology and Molecular Biology Reviews 1999 63 4 735 750 2-s2.0-0032712358
105. Siddaramappa S., Challacombe J. F., De Castro R. E., Pfeiffer F., Sastre D. E., Giménez M. I., Paggi R. A., Detter J. C., Davenport K. W., Goodwin L. A., Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J. A., A comparative genomics perspective on the geneticcontent of the alkaliphilic haloarchaeon Natrialbamagadii ATCC 43099T. BMC Genomics 2012 165 2-s2.0-84860504598 10.1186/1471-2164-13-165
106. Giménez M. I., Studdert C. A., Sánchez J. J., De Castro R. E., Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 2000 4 3 181 188 2-s2.0-0034199501
107. Eswar N., Webb B., Marti-Renom M. A., Madhusudhan M. S., Eramian D., Shen M.-Y., Pieper U., Sali A., Comparative protein structure modeling using Modeller. Current Protocols in Bioinformatics 2006 5 2-s2.0-43749107283 10.1002/0471140864.ps0209s50
108. Humphrey W., Dalke A., Schulten K., VMD: visual molecular dynamics. Journal of Molecular Graphics 1996 14 1 33 38 2-s2.0-0029878720 10.1016/0263-7855(96)00018-5 (Pubitemid 26152973)
109. Goecks J., Nekrutenko A., Taylor J., Galaxy Team T., Galaxy: a comprehensive approach for supporting accessible, reproducible, and transparent computational research in the life sciences. Genome Biology 2010 11 8 R86 2-s2.0-77955801615 10.1186/gb-2010-11-8-r86
110. Eddy S. R., Profile hidden Markov models. Bioinformatics 1998 14 9 755 763 2-s2.0-0031743421 (Pubitemid 28552108)