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Volumn 6, Issue 5, 2002, Pages 427-430

The search for traces of life: The protective effect of salt on biological macromolecules

Author keywords

Exobiology; Halophile proteins; Malate dehydrogenase; Salt; Stability; tRNA

Indexed keywords

ARCHAEA; HALOARCULA MARISMORTUI;

EID: 0036783192     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-002-0275-6     Document Type: Article
Times cited : (49)

References (18)
  • 1
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions
    • Bonnete F, Madern D, Zaccai G (1994) Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions. J Mol Biol 244:436-447
    • (1994) J Mol Biol , vol.244 , pp. 436-447
    • Bonnete, F.1    Madern, D.2    Zaccai, G.3
  • 2
    • 0027195301 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui
    • Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M (1993) Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32:4308-4313
    • (1993) Biochemistry , vol.32 , pp. 4308-4313
    • Cendrin, F.1    Chroboczek, J.2    Zaccai, G.3    Eisenberg, H.4    Mevarech, M.5
  • 3
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • Cordone L, Ferrand M, Vitrano E, Zaccai G (1999) Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys J 76:1043-1047
    • (1999) Biophys J , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 4
    • 0032142744 scopus 로고    scopus 로고
    • Was the environment for primordial life hypersaline?
    • Dundas I (1998) Was the environment for primordial life hypersaline? Extremophiles 2:375-377
    • (1998) Extremophiles , vol.2 , pp. 375-377
    • Dundas, I.1
  • 5
    • 0026646179 scopus 로고
    • Biochemical, structural, and molecular genetic aspects of halophilism
    • Eisenberg H, Mevarech M, Zaccai G (1992) Biochemical, structural, and molecular genetic 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
  • 8
    • 0024358140 scopus 로고
    • Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes
    • U S A
    • Iwabe N, Kuma K, Hasegawa M, Osawa S, Miyata T (1989) Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc Natl Acad Sci U S A 86:9355-9359
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 9
    • 0032557608 scopus 로고    scopus 로고
    • The salt of Europa
    • Kargel JS (1998) The salt of Europa. Science 280:1211-1212
    • (1998) Science , vol.280 , pp. 1211-1212
    • Kargel, J.S.1
  • 10
    • 0032497520 scopus 로고    scopus 로고
    • Salinity history of the Earth's early ocean
    • Knauth LP (1998) Salinity history of the Earth's early ocean. Nature 395:554-555
    • (1998) Nature , vol.395 , pp. 554-555
    • Knauth, L.P.1
  • 11
    • 0015875914 scopus 로고
    • The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes
    • Lawrence F, Blanquet S, Poiret M, Robert-Gero M, Waller JP (1973) The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes. Eur J Biochem 36:234-243
    • (1973) Eur J Biochem , vol.36 , pp. 234-243
    • Lawrence, F.1    Blanquet, S.2    Poiret, M.3    Robert-Gero, M.4    Waller, J.P.5
  • 12
    • 0029027430 scopus 로고
    • Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts
    • Madern D, Pfister C, Zaccai G (1995) Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Eur J Biochem 230:1088-1095
    • (1995) Eur J Biochem , vol.230 , pp. 1088-1095
    • Madern, D.1    Pfister, C.2    Zaccai, G.3
  • 14
    • 0028236899 scopus 로고
    • DNA stability at temperatures typical for hyperthermophiles
    • Marguet E, Forterre P (1994) DNA stability at temperatures typical for hyperthermophiles. Nucleic Acids Res 22:1681-1686
    • (1994) Nucleic Acids Res , vol.22 , pp. 1681-1686
    • Marguet, E.1    Forterre, P.2
  • 15
    • 0017383022 scopus 로고
    • Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure
    • Mevarech M, Neumann E (1977) Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry 16:3786-3792
    • (1977) Biochemistry , vol.16 , pp. 3786-3792
    • Mevarech, M.1    Neumann, E.2
  • 16
    • 0034620588 scopus 로고    scopus 로고
    • 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
    • Richard SB, Madern D, Garcin E, Zaccai G (2000) 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 39:992-1000
    • (2000) Biochemistry , vol.39 , pp. 992-1000
    • Richard, S.B.1    Madern, D.2    Garcin, E.3    Zaccai, G.4
  • 17
    • 0034687374 scopus 로고    scopus 로고
    • Isolation of a 250-million-year-old halotolerant bacterium from a primary salt crystal
    • Vreeland RH, Rosenzweig WD, Powers DW (2000) Isolation of a 250-million-year-old halotolerant bacterium from a primary salt crystal. Nature 407:897-900
    • (2000) Nature , vol.407 , pp. 897-900
    • Vreeland, R.H.1    Rosenzweig, W.D.2    Powers, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.