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Volumn 6, Issue 2, 2002, Pages 135-142

Stability of Natrialba magadii NDP kinase: Comparisons with other halophilic proteins

Author keywords

Archaea; Differential scanning calorimetry; Haloalkaliphiles; Nucleoside diphosphate kinase; Stability

Indexed keywords

ARCHAEA; NATRIALBA MAGADII;

EID: 0036549959     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s007920100232     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0025612249 scopus 로고
    • Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase
    • Biggs J, Hersperger E, Steeg PS, Liotta LA, Shearn A (1990) Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase. Cell 63:933-940
    • (1990) Cell , vol.63 , pp. 933-940
    • Biggs, J.1    Hersperger, E.2    Steeg, P.S.3    Liotta, L.A.4    Shearn, A.5
  • 4
    • 0030760841 scopus 로고    scopus 로고
    • Evolutionary divergence and salinity mediated selection in halophilic Archaea
    • Dennis PP, Shimmin LC (1997) Evolutionary divergence and salinity mediated selection in halophilic Archaea. Microbiol Mol Biol Rev 61:90-104
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 90-104
    • Dennis, P.P.1    Shimmin, L.C.2
  • 5
    • 0028158534 scopus 로고
    • Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1
    • Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C (1994) Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet 93:63-66
    • (1994) Hum Genet , vol.93 , pp. 63-66
    • Dooley, S.1    Seib, T.2    Engel, M.3    Theisinger, B.4    Janz, H.5    Piontek, K.6    Zang, K.D.7    Welter, C.8
  • 7
    • 0028076138 scopus 로고
    • Protein and nucleic acid hydration and cosolvent interactions: Establishment of reliable baseline values at high cosolvent concentrations
    • Eisenberg H (1994) Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable baseline values at high cosolvent concentrations. Biophys Chem 53:57-68
    • (1994) Biophys Chem , vol.53 , pp. 57-68
    • Eisenberg, H.1
  • 8
    • 0026646179 scopus 로고
    • Biochemical, structural and molecular genetics aspects of halophilism
    • Eisenberg H, Mevarech M, Zaccai G (1992) Biochemical, structural and molecular genetics aspects of halophilism. Adv Protein Chem 43:1-62
    • (1992) Adv Protein Chem , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zaccai, G.3
  • 9
    • 0013592939 scopus 로고
    • Thermodynamic analysis of scanning microcalorimetry data. Algorithms for the deconvolution of complex heat absorption curves
    • USSR
    • Filimonov VV, Potekhin SA, Matveev SV, Privalov PL (1982) Thermodynamic analysis of scanning microcalorimetry data. Algorithms for the deconvolution of complex heat absorption curves. Mol Biol (USSR) 16:345-444
    • (1982) Mol Biol , vol.16 , pp. 345-444
    • Filimonov, V.V.1    Potekhin, S.A.2    Matveev, S.V.3    Privalov, P.L.4
  • 10
    • 0029894585 scopus 로고    scopus 로고
    • Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases: Effect of subunit interaction
    • Giartosio A, Erent M, Cervoni L, Morera S, Janin J, Konrad M, Lascu I (1996) Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases: effect of subunit interaction. J Biol Chem 271:17845-17851
    • (1996) J Biol Chem , vol.271 , pp. 17845-17851
    • Giartosio, A.1    Erent, M.2    Cervoni, L.3    Morera, S.4    Janin, J.5    Konrad, M.6    Lascu, I.7
  • 11
    • 0001447366 scopus 로고
    • Malate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. Reconstitution of the enzyme after denaturation and dissociation in various denaturants
    • Hecht K, Jaenicke R (1989) Malate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. Reconstitution of the enzyme after denaturation and dissociation in various denaturants. Biochemistry 28:4979-4985
    • (1989) Biochemistry , vol.28 , pp. 4979-4985
    • Hecht, K.1    Jaenicke, R.2
  • 12
    • 0021800059 scopus 로고
    • Nucleotide sequence of the Bacillus subtilis tryptophan operon
    • Henner DJ, Band L, Shimotsu H (1985) Nucleotide sequence of the Bacillus subtilis tryptophan operon. Gene 34:169-177
    • (1985) Gene , vol.34 , pp. 169-177
    • Henner, D.J.1    Band, L.2    Shimotsu, H.3
  • 14
    • 0030807963 scopus 로고    scopus 로고
    • Diversity of alkaliphilic halobacteria: Proposals for transfer of Natronobacterium vacuolatum, Natronobacterium magadii, and Natronobacterium pharaonis to Halorubrum, Natrialba, and Natronomonas gen. nov., respectively, as Halorubrum vacuolatum comb. nov., Natrialba magadii comb. nov., and Natronomonas pharaonis comb. nov., respectively
    • Kamekura M, Dyall-Smith ML, Upasani V, Ventosa A, Kates M (1997) Diversity of alkaliphilic halobacteria: proposals for transfer of Natronobacterium vacuolatum, Natronobacterium magadii, and Natronobacterium pharaonis to Halorubrum, Natrialba, and Natronomonas gen. nov., respectively, as Halorubrum vacuolatum comb. nov., Natrialba magadii comb. nov., and Natronomonas pharaonis comb. nov., respectively. Int J Syst Bacteriol 47:853-857
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 853-857
    • Kamekura, M.1    Dyall-Smith, M.L.2    Upasani, V.3    Ventosa, A.4    Kates, M.5
  • 18
    • 0001300343 scopus 로고
    • Physiology of halophilic eubacteria
    • Rodriguez-Valdera F (ed) CRC, Boca Raton
    • Kushner DJ, Kamekura M (1988) Physiology of halophilic eubacteria. In: Rodriguez-Valdera F (ed) Halophilic bacteria, vol 1. CRC, Boca Raton, pp 109-140
    • (1988) Halophilic Bacteria , vol.1 , pp. 109-140
    • Kushner, D.J.1    Kamekura, M.2
  • 20
    • 0025287814 scopus 로고
    • Functional cloning of a nucleoside diphosphate kinase from Dictyostelium discoideum
    • Lacombe M, Wallet V, Troll H, Veron M (1990) Functional cloning of a nucleoside diphosphate kinase from Dictyostelium discoideum. J Biol Chem 265:10012-10018
    • (1990) J Biol Chem , vol.265 , pp. 10012-10018
    • Lacombe, M.1    Wallet, V.2    Troll, H.3    Veron, M.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi JK (1974) Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev 38:272-290
    • (1974) Bacteriol Rev , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 23
    • 0031891493 scopus 로고    scopus 로고
    • Subdomain interactions as a determinant in the folding and stability of T4 lysozyme
    • Llinas M, Marqusee S (1998) Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Sci 7:96-104
    • (1998) Protein Sci , vol.7 , pp. 96-104
    • Llinas, M.1    Marqusee, S.2
  • 24
    • 0029027430 scopus 로고
    • A single acidic amino acid mutation enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui
    • Madern D, Pfister C, Zaccai G (1995) A single acidic amino acid mutation enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui. Eur J Biochem 230:1088-1095
    • (1995) Eur J Biochem , vol.230 , pp. 1088-1095
    • Madern, D.1    Pfister, C.2    Zaccai, G.3
  • 26
    • 0033152499 scopus 로고    scopus 로고
    • Thermophilic and halophilic extremophiles
    • Madigan MT, Oren A (1999) Thermophilic and halophilic extremophiles. Curr Opin Microbiol 2:265-269
    • (1999) Curr Opin Microbiol , vol.2 , pp. 265-269
    • Madigan, M.T.1    Oren, A.2
  • 27
    • 0025830324 scopus 로고
    • Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei
    • Muriana FJ, Alvarez-Ossorio MC, Relimpio AM (1991) Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei. Biochem J 278:149-154
    • (1991) Biochem J , vol.278 , pp. 149-154
    • Muriana, F.J.1    Alvarez-Ossorio, M.C.2    Relimpio, A.M.3
  • 29
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki Y, Tanford C (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem 246:2211-2217
    • (1971) J Biol Chem , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 30
    • 0033022073 scopus 로고    scopus 로고
    • Bioenergetic aspects of halophilism
    • Oren A (1999) Bioenergetic aspects of halophilism. Microbiol Mol Biol Rev 63:334-348
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 334-348
    • Oren, A.1
  • 31
    • 0032143972 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase from haloakaliphilic archaeon Natronobacterium magadii: Purification and characterisation
    • Polosina YY, Jarrell KF, Fedorov OV, Kostyukova AS (1998) Nucleoside diphosphate kinase from haloakaliphilic archaeon Natronobacterium magadii: purification and characterisation. Extremophiles 2:333-338
    • (1998) Extremophiles , vol.2 , pp. 333-338
    • Polosina, Y.Y.1    Jarrell, K.F.2    Fedorov, O.V.3    Kostyukova, A.S.4
  • 33
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL (1979) Stability of proteins: small globular proteins. Adv Protein Chem 33:167-241
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 34
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86:665-684
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 35
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov PL, Potekhin SA (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 131:4-51
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 36
    • 0019618128 scopus 로고
    • Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration
    • Pundak S, Eisenberg H (1981) Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration, Eur J Biochem 118:463-470
    • (1981) Eur J Biochem , vol.118 , pp. 463-470
    • Pundak, S.1    Eisenberg, H.2
  • 37
    • 0019616694 scopus 로고
    • Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability
    • Pundak S, Aloni H, Eisenberg H (1981) Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability. Eur J Biochem 118:471-477
    • (1981) Eur J Biochem , vol.118 , pp. 471-477
    • Pundak, S.1    Aloni, H.2    Eisenberg, H.3
  • 38
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Sanchez-Ruiz JM (1995) Differential scanning calorimetry of proteins. Subcell Biochem 24:133-176
    • (1995) Subcell Biochem , vol.24 , pp. 133-176
    • Sanchez-Ruiz, J.M.1
  • 39
    • 0028986376 scopus 로고
    • Unfolding of tertiary structure of Halobacterium halobium flagellins does not result in flagella destruction
    • Tarasov VY, Kostyukova AS, Tiktopulo EI, Pyatibratov MG, Fedorov OV (1995) Unfolding of tertiary structure of Halobacterium halobium flagellins does not result in flagella destruction. J Protein Chem 14:27-31
    • (1995) J Protein Chem , vol.14 , pp. 27-31
    • Tarasov, V.Y.1    Kostyukova, A.S.2    Tiktopulo, E.I.3    Pyatibratov, M.G.4    Fedorov, O.V.5
  • 41
    • 0023103028 scopus 로고
    • Physiological correlation between NDP-kinase and the enzyme-associated guanine nucleotide binding proteins
    • Uesaka H, Yokoyama M, Ohtsuki K (1987) Physiological correlation between NDP-kinase and the enzyme-associated guanine nucleotide binding proteins. Biochem Biophys Res Commun143:552-559
    • (1987) Biochem Biophys Res Commun , vol.143 , pp. 552-559
    • Uesaka, H.1    Yokoyama, M.2    Ohtsuki, K.3
  • 42
    • 0031810562 scopus 로고    scopus 로고
    • Biology of moderately halophilic aerobic bacteria
    • Ventosa A, Nieto JJ, Oren A (1998) Biology of moderately halophilic aerobic bacteria. Microbiol Mol Biol Rev 62:504-544
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 504-544
    • Ventosa, A.1    Nieto, J.J.2    Oren, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.