Pressure dependence of activity and stability of dihydrofolate reductases of the deep-sea bacterium Moritella profunda and Escherichia coli

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1824, Issue 3, 2012, Pages 511-519

  Ohmae, Eiji ^a   Murakami, Chiho ^a,d   Tate, Shin Ichi ^a   Gekko, Kunihiko ^a   Hata, Kazumi ^b   Akasaka, Kazuyuki ^b,e   Kato, Chiaki ^c  

^a HIROSHIMA UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

^c JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

^d NATIONAL RESEARCH INSTITUTE OF BREWING   (Japan)

^e RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

Cavity; Deep sea; Dihydrofolate reductase; Hydration; Molecular adaptation; Moritella profunda

Indexed keywords

DIHYDROFOLATE REDUCTASE;

ARTICLE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; DEEP SEA; ENZYME ACTIVITY; ENZYME STABILITY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; MORITELLA PROFUNDA; PRIORITY JOURNAL; PSYCHROPHILIC BACTERIUM; THERMODYNAMICS;

BACTERIAL PROTEINS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESCHERICHIA COLI; HYDROSTATIC PRESSURE; KINETICS; MORITELLA; OCEANS AND SEAS; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; UREA; WATER;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MORITELLA PROFUNDA;

EID: 84857072552     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.01.001     Document Type: Article

References (36)

1. T. Dams, G. Bohm, G. Auerbach, G. Bader, H. Schurig, and R. Jaenicke Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability Biol. Chem. 379 1998 367 371 (Pubitemid 28152102)
2. U. Pieper, G. Kapadia, M. Mevarech, and O. Helzberg Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii Structure 15 1998 75 88 (Pubitemid 28084401)
3. J.T. Bolin, D.J. Filman, D.A. Matthews, R.C. Hamlin, and J. Kraut Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate J. Biol. Chem. 257 1982 13650 13662 (Pubitemid 13187127)
4. M.R. Sawaya, and J. Kraut Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence Biochemistry 36 1997 586 603 (Pubitemid 27057006)
5. B.C. Bennett, H. Xu, R.F. Simmerman, R.E. Lee, and C.G. Dealwis Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase J. Med. Chem. 50 2007 4374 4381 (Pubitemid 47378835)
6. K.M. Frey, J. Liu, M.N. Lombardo, D.B. Bolstad, D.L. Wright, and A.C. Anderson Crystal structures of wild-type and mutant methicillin-resistant Staphylococcus aureus dihydrofolate reductase reveal an alternate conformation of NADPH that may be linked to trimethoprim resistance J. Mol. Biol. 387 2009 1298 1308
7. Y. Xu, Y. Nogi, C. Kato, Z. Liang, H.J. Rüger, D. De Kegel, and N. Glansdorff Moritella profunda sp. nov. and Moritella abyssi sp. nov., two psychropiezophilic organisms isolated from deep Atlantic sediments Int. J. Syst. Evol. Microbiol. 53 2003 533 538 (Pubitemid 36416762)
8. S. Hay, R.M. Evans, C. Levy, E.J. Loveridge, X. Wang, D. Leys, R.K. Allemann, and N.S. Scrutton Are the catalytic properties of enzymes from piezophilic organisms pressure adapted? ChemBioChem 10 2009 2348 2353
9. E. Ohmae, K. Kubota, K. Nakasone, C. Kato, and K. Gekko Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12 Chem. Lett. 33 2004 798 799 (Pubitemid 39295744)
10. C. Murakami, E. Ohmae, S. Tate, K. Gekko, K. Nakasone, and C. Kato Cloning and characterization of dihydrofolate reductases from deep-sea bacteria J. Biochem. 147 2010 591 595
11. C. Murakami, E. Ohmae, S. Tate, K. Gekko, K. Nakasone, and C. Kato Comparative study on dihydrofolate reductases from Shewanella species living in deep-sea and ambient atmospheric environments Extremophiles 15 2011 165 175
12. C. Kato, T. Sato, and K. Horikoshi Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples Biodivers. Conserv. 4 1995 1 9
13. C. Kato, L. Li, Y. Nogi, Y. Nakamura, J. Tamaoka, and K. Horikoshi Extremely barophilic bacteria isolated from the Mariana Trench, Challenger Deep, at a depth of 11,000 meters Appl. Environ. Microbiol. 64 1998 1510 1513 (Pubitemid 28188420)
14. K. Venkateswaran, D.P. Moser, M.E. Dollhopf, D.P. Lies, D.A. Saffarini, B.J. MacGregor, D.B. Ringelberg, D.C. White, M. Nishijima, H. Sano, J. Burghardt, E. Stackebrandt, and K.H. Nealson Polyphasic taxonomy of the genus Shewanella and description of Shewanella oneidensis sp. nov. Int. J. Syst. Bacteriol. 49 1999 705 724
15. C. Balny, P. Masson, and K. Heremans Frontiers in High Pressure Biochemistry and Biophysics Biochim. Biophys. Acta 1595 (1-2) 2002
16. E. Ohmae, K. Iriyama, S. Ichihara, and K. Gekko Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function J. Biochem. 119 1996 946 953
17. C.A. Fierke, K.A. Johnson, and S.J. Benkovic Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli Biochemistry 26 1987 4085 4092
18. E. Ohmae, M. Tatsuta, F. Abe, C. Kato, N. Tanaka, S. Kunugi, and K. Gekko Effects of pressure on enzyme function of Escherichia coli dihydrofolate reductase Biochim. Biophys. Acta 1784 2008 1115 1121
19. R.M.C. Dawson, D.C. Elliot, W.H. Elliot, and K.M. Jones Data for Biochemical Research 1969 Oxford University Press Oxford
20. G.J.A. Vidugiris, and C.A. Royer Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states Biophys. J. 75 1998 463 470 (Pubitemid 28311836)
21. C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves C.H.W. Hirs, S.N. Timasheff, Methods in Enzymology Vol. 131 1985 Academic Press New York 267 280
22. K. Kuwajima, E.P. Garvey, B.E. Finn, C.R. Matthews, and S. Sugai Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy Biochemistry 30 1991 7693 7703
23. E. Ohmae, Y. Sasaki, and K. Gekko Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductase J. Biochem. 130 2001 439 447 (Pubitemid 32845699)
24. K. Gekko, Y. Kunori, H. Takeuchi, S. Ichihara, and M. Kodama Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function J. Biochem. 116 1994 34 41 (Pubitemid 24230779)
25. E. Ohmae, Y. Fukumizu, M. Iwakura, and K. Gekko Effects of mutation at methionine-42 of Escherichia coli dihydrofolate reductase on stability and function: implication of hydrophobic interactions J. Biochem. 137 2005 643 652 (Pubitemid 40874543)
26. R.M. Evans, E.M. Behiry, L.H. Tey, J. Guo, E.J. Loveridge, and R.K. Allemann Catalysis by dihydrofolate reductase from the psychropiezophile Moritella profunda ChemBioChem 11 2010 2010 2017
27. E. Ohmae, T. Kurumiya, S. Makino, and K. Gekko Acid and thermal unfolding of Escherichia coli dihydrofolate reductase J. Biochem. 120 1996 946 953 (Pubitemid 26400016)
28. N. Greenfield, and G.D. Fasman Computed circular dichroism spectra for the evaluation of protein conformation Biochemistry 8 1969 4108 4116
29. Y. Xu, G. Feller, C. Gerday, and N. Glansdorff Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? J. Bacteriol. 185 2003 5519 5526 (Pubitemid 37082409)
30. D. Ishimaru, L.R. Andrade, L.S. Teixeira, P.A. Quesado, L.M. Maiolino, P.M. Lopez, Y. Cordeiro, L.T. Costa, W.M. Heckl, G. Weissmüller, D. Foguel, and J.L. Silva Fibrillar aggregates of the tumor suppressor p53 core domain Biochemistry 42 2003 9022 9027 (Pubitemid 36935410)
31. D. Ishimaru, L.M. Lima, L.F. Maia, P.M. Lopez, A.P. Ano Bom, A.P. Valente, and J.L. Silva Reversible aggregation plays a crucial role on the folding landscape of p53 core domain Biophys. J. 87 2004 2691 2700
32. K. Hata, R. Kono, M. Fujisawa, R. Kitahara, Y.O. Kamatari, K. Akasaka, and Y. Xu High pressure NMR study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda Cell Mol. Biol. (Noisy-le-grand) 50 2004 311 316
33. G. Dreyfus, H. Guimaraes-Motta, and J.L. Silva Effect of hydrostatic pressure on the mitochondrial ATP synthase Biochemistry 27 1988 6704 6710
34. W. Kauzmann Some factors in the interpretation of protein denaturation Adv. Protein Chem. 14 1959 1 63
35. E. Ohmae, C. Murakami, K. Gekko, and C. Kato Pressure effects on enzyme functions J. Biol. Macromol. 7 2007 23 29
36. R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comput. Chem. 19 1998 319 333 (Pubitemid 128592649)