First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1791, Issue 8, 2009, Pages 719-729

  Müller Santos, Marcelo ^a   de Souza, Emanuel M ^a   Pedrosa, Fabio de O ^a   Mitchell, David Alexander ^a   Longhi, Sonia ^b   Carrière, Frédéric ^c   Canaan, Stéphane ^c   Krieger, Nadia ^a  

^a FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

^b Centre National de la Recherche Scientifique   (France)

^c Centre National de la Recherche Scientifique   (France)

Author keywords

Enzyme; Esterase; Haloadaptation; Haloarchaea; Hormone sensitive lipase; Protein folding

Indexed keywords

5 METHOXY 3 (4 PHENOXYPHENYL) 3H [1,3,4]OXADIAZOL 2 ONE; BENZYLSULFONYL FLUORIDE; DIETHYL P NITROPHENYL PHOSPHATE; ESTERASE; POTASSIUM CHLORIDE; RECOMBINANT PROTEIN; RECOMBINANT PROTEIN HM EST; SHORT CHAIN FATTY ACID; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CLONOGENESIS; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FUNCTIONAL PROTEOMICS; GENE OVEREXPRESSION; HALOARCULA MARISMORTUI; NONHUMAN; NUCLEOTIDE SEQUENCE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SALT TOLERANCE; SURFACE PROPERTY; THERMOSTABILITY;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; CLONING, MOLECULAR; COMPUTATIONAL BIOLOGY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; ENZYME INHIBITORS; ENZYME STABILITY; ESTERASES; HALOARCULA MARISMORTUI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POTASSIUM CHLORIDE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SODIUM CHLORIDE; STATIC ELECTRICITY; SUBSTRATE SPECIFICITY; SURFACE PROPERTIES; TEMPERATURE; TIME FACTORS;

ESCHERICHIA COLI; HALOARCULA MARISMORTUI; HALOBACTERIA;

EID: 67650462243     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2009.03.006     Document Type: Article

References (61)

1. Gotor-Fernandez V., Brieva R., and Gotor V. Lipases: useful biocatalysts for the preparation of pharmaceuticals. J. Mol. Catal., B Enzym. 40 (2006) 111-120
2. Panda T., and Gowrishankar B.S. Production and applications of esterases. Appl. Microbiol. Biotechnol. 67 (2005) 160-169
3. Bornscheuer U.T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev. 26 (2002) 73-81
4. Ferrer M., Golyshina O., Beloqui A., and Golyshin P.N. Mining enzymes from extreme environments. Curr. Opin. Microbiol. 10 (2007) 207-214
5. Hough D.W., and Danson M.J. Extremozymes. Curr. opin. chem. biol. 3 (1999) 39-46
6. Eichler J. Biotechnological uses of archaeal extremozymes. Biotechnol. Adv. 19 (2001) 261-278
7. Sellek G.A., and Chaudhuri J.B. Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microb. Technol. 25 (1999) 471-482
8. R.V. Almeida, S.M.C. Alqueres, A.L. Larentis, S.C. Rossle, A.M. Cardoso, W.I. Almeida, P.M. Bisch, T.L.M. Alves, O.B. Martins, Cloning, expression, partial characterization and structural modeling of a novel esterase from Pyrococcus furiosus, Vol. 39 2006.
9. Park Y.J., Choi S.Y., and Lee H.B. A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression. Biochim. Biophys. Acta 1760 (2006) 820-828
10. Gao R.J., Feng Y., Ishikawa K., Ishida H., Ando S., Kosugi Y., and Cao S.G. Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1. J. Mol. Catal., B Enzym. 24-25 (2003) 1-8
11. Manco G., Giosue E., D'Auria S., Herman P., Carrea G., and Rossi M. Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus. A. Biochem. Biophys. 373 (2000) 182-192
12. Kim S., and Lee S.B. Thermostable esterase from a thermoacidophilic archaeon: purification and characterization for enzymatic resolution of a chiral compound. Biosci. Biotechnol. Biochem. 68 (2004) 2289-2298
13. Oren A. Diversity of halophilic microorganisms: environments, phylogeny, physiology, and applications. J. Ind. Microbiol. Biotech. 28 (2002) 56-63
14. Madern D., Ebel C., and Zaccai G. Halophilic adaptation of enzymes. Extremophiles 4 (2000) 91-98
15. Mevarech M., Frolow F., and Gloss L.M. Halophilic enzymes: proteins with a grain of salt. Biophys. Chemist. 86 (2000) 155-164
16. Danson M.J., and Hough D.W. The structural basis of protein halophilicity. Comp. Biochem. Physiol. a-Physiology 117 (1997) 307-312
17. Gonzalez C., and Gutierrez C. Presence of lipase among species of extremely halophilic bacteria. Can. J. Microbiol. 16 (1970) 1165-1166
18. Boutaiba S., Bhatnagar T., Hacene H., Mitchell D.A., and Baratti J.C. Preliminary characterisation of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp. J. Mol. Catal., B Enzym. 41 (2006) 21-26
19. Connaris H., Chaudhuri J.B., Danson M.J., and Hough D.W. Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. Biotechnol. Bioeng. 64 (1999) 38-45
20. Thompson J.D., Higgins D.G., and Gibson T.J. Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
21. Altschul S.F., Wootton J.C., Gertz E.M., Agarwala R., Morgulis A., Schaffer A.A., and Yu Y.K. Protein database searches using compositionally adjusted substitution matrices. FEBS J. 272 (2005) 5101-5109
22. Cserzo M., Wallin E., Simon I., vonHeijne G., and Elofsson A. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Prot. Engineering 10 (1997) 673-676
23. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340 (2004) 783-795
24. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M., Appel R., and Bairoch A. In: M., and W.J. (Eds). The Proteomics Protocols Handbook (2005), Humana Press, New Jersey 571-607
25. Karchin R., Cline M., and Karplus K. Evaluation of local structure alphabets based on residue burial. Proteins 55 (2004) 508-518
26. Karchin R., Cline M., Mandel-Gutfreund Y., and Karplus K. Hidden Markov models that use predicted local structure for fold recognition: alphabets of backbone geometry. Proteins 51 (2003) 504-514
27. Karplus K., Karchin R., Draper J., Casper J., Mandel-Gutfreund Y., Diekhans M., and Hughey R. Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 53 Suppl 6 (2003) 491-496
28. Karplus K., Karchin R., Barrett C., Tu S., Cline M., Diekhans M., Grate L., Casper J., and Hughey R. What is the value added by human intervention in protein structure prediction?. Proteins Suppl. 5 (2001) 86-91
29. Karplus K., Katzman S., Shackleford G., Koeva M., Draper J., Barnes B., Soriano M., and Hughey R. SAM-T04: what is new in protein-structure prediction for CASP6. Proteins 61 Suppl 7 (2005) 135-142
30. Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., Shindyalov I.N., and Bourne P.E. The Protein Data Bank. Nucleic Acids Res. 28 (2000) 235-242
31. van Gunsteren W.F., Hünenberojer P.H., Mark A.E., Smith P.E., and Tironi I.G. Computer simulation of protein motion. Comput. Phys. Commun. 91 (1995) 305-319
32. Vriend G. What if - a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
33. DeLano W.L. The PyMOL molecular graphics system. Proteins 30 (2002) 442-454
34. Rocchia W., Alexov E., and Honig B. Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions. J. Phys. Chem. B 105 (2001) 6507-6514
35. Klapper I., Hagstrom R., Fine R., Sharp K., and Honig B. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification. Proteins 1 (1986) 47-59
36. Roussel A., and Cambillau C. Turbo Frodo. In: Graphics S. (Ed). Silicon Graphics Geometry Partners Directory (1991), Silicon Graphics, Mountain View, CA, USA 86
37. De Simone G., Menchise V., Alterio V., Mandrich L., Rossi M., Manco G., and Pedone C. The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family. J. Mol. Biol. 343 (2004) 137-146
38. Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2256-2268
39. Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
40. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
41. Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227 (1970) 680-685
42. Whitmore L., and Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89 (2008) 392-400
43. Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-W673
44. Ben Ali Y., Chahinian H., Petry S., Muller G., Lebrun R., Verger R., Carriere F., Mandrich L., Rossi M., Manco G., Sarda L., and Abousalham A. Use of an inhibitor to identify members of the hormone-sensitive lipase family. Biochemistry 45 (2006) 14183-14191
45. Ransac S., Gargouri Y., Marguet F., Buono G., Beglinger C., Hildebrand P., Lengsfeld H., Hadvary P., and Verger R. Covalent inactivation of lipases. Methods Enzymol. 286 (1997) 190-231
46. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J., Sussman J.L., Verschueren K.H.G., and Goldman A. The alpha/beta-hydrolase fold. Protein Eng. 5 (1992) 197-211
47. Madern D., and Zaccai G. Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Biochimie 86 (2004) 295-303
48. Eddy M.L., and Jablonski P.E. Purification and characterization of a membrane-associated ATPase from Natronococcus occultus, a haloalkaliphilic archaeon. FEMS Microbiol. Lett. 189 (2000) 211-214
49. Bennett-Lovsey R.M., Herbert A.D., Sternberg M.J., and Kelley L.A. Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70 (2008) 611-625
50. Lieutaud P., Canard B., and Longhi S. MeDor: a metaserver for predicting protein disorder. BMC Genomics 6 (2008) 9 Suppl 2:S25
51. Liu J., and Rost B. NORSp: predictions of long regions without regular secondary structure. Nucleic Acids Res. 31 (2003) 3833-3835
52. Britton K.L., Baker P.J., Fisher M., Ruzheinikov S., Gilmour D.J., Bonete M.J., Ferrer J., Pire C., Esclapez J., and Rice D.W. Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4846-4851
53. Ferrer M., Golyshina O.V., Chernikova T.N., Khachane A.N., Martins Dos Santos V.A., Yakimov M.M., Timmis K.N., and Golyshin P.N. Microbial enzymes mined from the Urania deep-sea hypersaline anoxic basin. Chem. Biol. 12 (2005) 895-904
54. Bornscheuer U.T. Deep sea mining for unique biocatalysts. Chem. Biol. 12 (2005) 859-860
55. Premkumar L., Greenblatt H.M., Bageshwar U.K., Savchenko T., Gokhman I., Sussman J.L., and Zamir A. Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 7493-7498
56. Fukuchi S., Yoshimune K., Wakayama M., Moriguchi M., and Nishikawa K. Unique amino acid composition of proteins in halophilic bacteria. J. Mol. Biol. 327 (2003) 347-357
57. Azam F., and Malfatti F. Microbial structuring of marine ecosystems. Nat. Rev. Microbio. 5 (2007) 782-791
58. Pire C., Esclapez J., Ferrer J., and Bonete M.J. Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family. FEMS Microbiol. Lett. 200 (2001) 221-227
59. Hayden B.M., Bonete M.J., Brown P.E., Moir A.J.G., and Engel P.C. Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene sequence currently assigned to the NADP(+)-dependent enzyme is in fact that of the NAD(+)-dependent glutamate dehydrogenase. FEMS Microbiol. Letters 211 (2002) 37-41
60. Shi W.L., Tang X.F., Huang Y.P., Gan F., Tang B., and Shen P. An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp J7: gene cloning, expression and characterization. Extremophiles 10 (2006) 599-606
61. Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27 (2002) 527-533