Adaptation to extreme environments: Macromolecular dynamics in bacteria compared in vivo by neutron scattering

EMBO Reports

Volumn 5, Issue 1, 2004, Pages 66-70

  Tehei, Moeava ^a   Franzetti, Bruno ^a   Madern, Dominique ^a   Ginzburg, Margaret ^b   Ginzburg, Ben Z ^b   Giudici Orticoni, Marie Thérèse ^c   Bruschi, Mireille ^c   Zaccai, Giuseppe ^a,d  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^c AIX MARSEILLE UNIVERSITÉ   (France)

^d INSTITUT LAUE LANGEVIN   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CONSTANTS AND COEFFICIENTS; CONTROLLED STUDY; ENERGY; ENTHALPY; ENTROPY; ENVIRONMENTAL FACTOR; ESCHERICHIA COLI; EVOLUTIONARY ADAPTATION; FORCE; HEAT TOLERANCE; HIGH TEMPERATURE; IN VIVO STUDY; MACROMOLECULE; MICROBIAL ACTIVITY; MOLECULAR DYNAMICS; MOLECULAR STABILITY; NEUTRON SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEUS MIRABILIS; QUANTITATIVE ANALYSIS; TEMPERATURE MEASUREMENT; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS;

ADAPTATION, PSYCHOLOGICAL; BACTERIA; ESCHERICHIA COLI; MACROMOLECULAR SUBSTANCES; MODELS, STATISTICAL; NEUTRONS; OXALOBACTERACEAE; PROTEUS MIRABILIS; SCATTERING, RADIATION; TEMPERATURE; THERMODYNAMICS; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MIRABILIS; PROTEUS MIRABILIS; THERMUS THERMOPHILUS;

EID: 1242343625     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400049     Document Type: Article

References (37)

1. Aghajari N, Feller G, Gerday C, Haser R (1998) Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Structure 6: 1503-1516
2. Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH (1997) Crystal structure of the β-glycosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J Mol Biol 271: 782-802
3. Arnold FH, Wintrode PL, Miyazaki K, Gershenson A (2001) How enzymes adapt: lessons from directed evolution. Trends Biochem Sci 26: 100-106
4. Auerbach G, Ostendorp R, Prade L, Korndorfer I, Dams T, Huber R, Jaenicke R (1998) Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1A resolution reveals strategies for intrinsic protein stabilizalion. Structure 6: 769-781
5. Bell GS, Russell RJM, Connaris H, Hough DW, Danson MJ, Taylor GL (2002) Stepwise adaptations of citrate synthase to survival at life's extremes. Eur J Biochem 269: 6250-6260
6. Bicout DJ, Field MJ (1996) Stochastic dynamics simulations of macromolecular diffusion in a model of the cytoplasm of Escherichia coli. J Phys Chem 100: 2489-2497
7. Bicout DJ, Zaccai G (2001) Protein flexibility from the dynamical transition: a force constant analysis. Biophys J 80; 1115-1123
8. Bon C, Lehmann MS, Wilkinson C (1999) Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme. Acta Crystallogr D Biol Crystallogr 55: 978-987
9. Bonneté F, Madern D, Zaccai G (1994) Stability against denaturation mechanisms in halophilic malate dethydrogenase 'adapt' to solvent conditions. J Mol Biol 244: 436-447
10. Brooks CL, Karplus M, Pettitt BM (1988) Proteins; a theoretical perspective of dynamics, structure and thermodynamics. Adv Chem Phys 71: 74-95
11. Bu Z, Neumann DA, Lee SH, Brown CM, Engelman DM, Hall CC (2000) A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering. J Mol Biol 301: 525-536
12. Bu Z, Cook J, Callaway DJ (2001) Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin. J Mol Biol 312: 865-873
13. Butler BJ, McCallum KL, Iniss WE (1989) Characterization of Aquaspirillum acrticum sp. nov., a new psychrophilic bacterium. System Appl Microbiol 12: 263-266
14. Cambillau C, Claverie JM (2000) Structural and genomic correlates of hyperthermostability. J Biol Chem 275: 32383-32386
15. Doster W, Cusack S, Petry W (1989) Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature 337: 754-756
16. Fitter J, Heberle J (2000) Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase. Biophys J 79: 1629-1636
17. Gabel F, Bicout D, Lehnert U, Tehei M, Weik M, Zaccai G (2002) Protein dynamics studied by neutron scattering. Q Rev Biophys 35: 327-367
18. Gianese G, Bossa F, Pascarella S (2002) Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins: Struct Funct Genet 47: 236-249
19. Haney PJ, Badger JH, Buldak GL, Reich CI, Woese CR, Olsen GJ (1999) Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc Natl Acad Sci USA 96: 3578-3583
20. Hernandez G, Jenney Jr FE, Adams MW, LeMaster DM (2000) Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc Natl Acad Sci USA 97: 3166-3170
21. Jaenicke R (2000) Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc Natl Acad Sci USA 97: 2962-2964
22. Lehnert U, Reat V, Weik M, Zaccai G, Pfister C (1998) Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes. Biophys J 75: 1945-1952
23. Linke WA, Granzier H (1998) A spring tale: new facts on titin elasticity. Biophys J 75: 2613-2614
24. Lonhienne T, Gerday C, Feller G (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta 1543: 1-10
25. Oesterhelt F, Oesterhelt D, Pfeiffer M, Engel A, Gaub HE, Muller DJ (2000) Unfolding pathways of individual bacteriorhodopsins. Science 288: 143-146
26. Petrescu I, Lamotte-Brasseur J, Chessa JP, Ntarima P, Claeyssens M, Devreese B, Marino G, Gerday C (2000) Xylanase from the psychrophilic yeast Cryptococcus adeliae. Extremophiles 4: 137-144
27. Price PB (2000) A habitat for psychrophiles in deep Antarctic ice. Proc Natl Acad Sci USA 97: 1247-1251
28. Receveur V, Calmettes P, Smith JC, Desmadril M, Coddens G, Durand D (1997) Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering. Proteins 28: 380-387
29. Rosen R, Ron EZ (2002) Proteome analysis in the study of heat-shock response. Mass Spectrom Rev 21: 244-265
30. Russell NJ (2000) Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 4: 83-90
31. Smith JC (1991) Protein dynamics: comparison of simulations with inelastic neutron scattering experiments. Q Rev Biophys 24: 227-291
32. Tehei M, Madern D, Pfister C, Zaccai G (2001) Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. Proc Natl Acad Sci USA 98: 14356-14361
33. Trantham EC, Rorschach HE, Clegg JS, Hazlewood CF, Nicklow RM, Wakabayashi N (1984) Diffusive properties of water in Artemia cysts as determined from quasi-elastic neutron scattering spectra. Biophys J 45: 927-938
34. Zaccai G (2000) How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science 288: 1604-1607
35. Zaccai G, Tehei M, Scherbakova I, Serdyuk I, Gerez C, Pfister C (2000) Incoherent elastic neutron scattering as a function of temperature: a fast way to characterise in situ biological dynamics in complex solutions. J Phys IV 10: Pr7-283-Pr7-287
36. Zavodszky P, Kardos J, Svingor A, Petsko GA (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA 95: 7406-7411
37. Zidek L, Novotny MV, Stone MJ (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nature Struct Biol 6: 1118-1121