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Volumn 290, Issue 2, 1999, Pages 595-604

Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability

Author keywords

Genomics; Proteome; Sufaceloops; Thermophiles

Indexed keywords

PROTEIN;

EID: 0033538553     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2889     Document Type: Article
Times cited : (257)

References (54)
  • 4
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach G., Huber R., Grättinger M., Zaiss K., Schurig H., Jaenicke R., Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure. 5:1997;1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grättinger, M.3    Zaiss, K.4    Schurig, H.5    Jaenicke, R.6    Jacob, U.7
  • 6
    • 0031837178 scopus 로고    scopus 로고
    • Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brokii alcohol dehydrogenase
    • Bogin O., Peretz M., Hacham Y., Korkhin Y., Frolow F., Kalb (Gilboa) A., Burstein Y. Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brokii alcohol dehydrogenase. Protein Sci. 7:1998;1156-1163.
    • (1998) Protein Sci. , vol.7 , pp. 1156-1163
    • Bogin, O.1    Peretz, M.2    Hacham, Y.3    Korkhin, Y.4    Frolow, F.5    Kalb, A.6    Burstein, Y.7
  • 8
    • 0032509302 scopus 로고    scopus 로고
    • Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 10
    • 0026694167 scopus 로고
    • A model of the molten globule state from molecular dynamics simulations
    • Daggett, Levitt M. A model of the molten globule state from molecular dynamics simulations. Proc. Natl Acad. Sci. USA. 89:1992;5142-5146.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5142-5146
    • Daggett1    Levitt, M.2
  • 11
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41
    • Davail S., Feller G., Narinx E., Gerday C. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem. 269:1994;17448-17453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 18
    • 0027410087 scopus 로고
    • Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolines
    • Hardy F., Vriend G., Veltman O., van der Vinne B., Venema G., Eijsink V. Stabilization of Bacillus stearothermophilus neutral protease by introduction of prolines. FEBS Letters. 317:1993;89-92.
    • (1993) FEBS Letters , vol.317 , pp. 89-92
    • Hardy, F.1    Vriend, G.2    Veltman, O.3    Van Der Vinne, B.4    Venema, G.5    Eijsink, V.6
  • 19
    • 0022965255 scopus 로고
    • Stabilization of lambda repressor against thermal denaturation by site-directed Gly-Ala changes in alpha helix 3
    • Hecht M., Sturtevant J., Sauer R. Stabilization of lambda repressor against thermal denaturation by site-directed Gly-Ala changes in alpha helix 3. Proteins: Struct. Funct. Genet. 1:1986;43-46.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 43-46
    • Hecht, M.1    Sturtevant, J.2    Sauer, R.3
  • 20
    • 10544255079 scopus 로고    scopus 로고
    • Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae
    • Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B., Herr R. Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucl. Acids Res. 24:1996;4420-4449.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4420-4449
    • Himmelreich, R.1    Hilbert, H.2    Plagens, H.3    Pirkl, E.4    Li, B.5    Herr, R.6
  • 21
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 22
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R., Böhm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8:1998;738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structures: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structures: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0029670677 scopus 로고    scopus 로고
    • Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein Hu fromBacillus stearothermophilus
    • Kawamura S., Kakuta Y., Tanaka I., Hikichi K., Kuhura S., Yamasaki N., Kimura M. Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein Hu fromBacillus stearothermophilus. Biochemistry. 35:1996;1195-1200.
    • (1996) Biochemistry , vol.35 , pp. 1195-1200
    • Kawamura, S.1    Kakuta, Y.2    Tanaka, I.3    Hikichi, K.4    Kuhura, S.5    Yamasaki, N.6    Kimura, M.7
  • 29
    • 0031614960 scopus 로고    scopus 로고
    • Proteins from hyperthermophiles: Stability and enzyme catalysis close to the boiling point of water
    • Ladenstein R., Antranikian G. Proteins from hyperthermophiles: stability and enzyme catalysis close to the boiling point of water. Adv. Biochem. Eng. Biotechnol. 61:1998;37-85.
    • (1998) Adv. Biochem. Eng. Biotechnol. , vol.61 , pp. 37-85
    • Ladenstein, R.1    Antranikian, G.2
  • 30
    • 0031467464 scopus 로고    scopus 로고
    • Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin
    • Lazaridis T., Lee I., Karplus M. Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin. Protein Sci. 6:1997;2589-2605.
    • (1997) Protein Sci. , vol.6 , pp. 2589-2605
    • Lazaridis, T.1    Lee, I.2    Karplus, M.3
  • 31
    • 0030589056 scopus 로고    scopus 로고
    • Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyerthermophilic bacterium Thermotoga maritima
    • Macedo-Ribeiro S., Darimont B., Sterner R., Huber R. Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyerthermophilic bacterium Thermotoga maritima. Structure. 4:1996;1291-1301.
    • (1996) Structure , vol.4 , pp. 1291-1301
    • Macedo-Ribeiro, S.1    Darimont, B.2    Sterner, R.3    Huber, R.4
  • 32
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutatins that decrease the entropy of unfolding
    • Matthews B., Nicholson H., Becktel W. Enhanced protein thermostability from site-directed mutatins that decrease the entropy of unfolding. Proc. Natl Acad. Sci. USA. 84:1987;6663-6667.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.1    Nicholson, H.2    Becktel, W.3
  • 33
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix bundle protein
    • Nagi A., Regan L. An inverse correlation between loop length and stability in a four-helix bundle protein. Folding Design. 2:1997;67-75.
    • (1997) Folding Design , vol.2 , pp. 67-75
    • Nagi, A.1    Regan, L.2
  • 34
    • 0031415284 scopus 로고    scopus 로고
    • Subtilisin from psychrophilic antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
    • Narinx E., Baise E., Gerday C. Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 10:1997;1271-1279.
    • (1997) Protein Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 35
    • 0026955827 scopus 로고
    • Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme
    • Nicholson H., Tronrud D., Becktel W., Matthews B. Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. Biopolymers. 32:1992;1421-1441.
    • (1992) Biopolymers , vol.32 , pp. 1421-1441
    • Nicholson, H.1    Tronrud, D.2    Becktel, W.3    Matthews, B.4
  • 36
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz M., Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature. 255:1975;256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.1    Raidt, H.2
  • 37
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov P. Stability of proteins: small globular proteins. Advan. Protein Chem. 33:1979;167-241.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.1
  • 38
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single-chain proteins by linker length and composition mutagenesis
    • Robinson C., Sauer R. Optimizing the stability of single-chain proteins by linker length and composition mutagenesis. Proc. Natl Acad. Sci. USA. 95:1998;5929-5934.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5929-5934
    • Robinson, C.1    Sauer, R.2
  • 39
    • 0028774720 scopus 로고
    • The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum
    • Russell R., Hough D., Danson M., Taylor G. The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum. Structure. 2:1994;1157-1167.
    • (1994) Structure , vol.2 , pp. 1157-1167
    • Russell, R.1    Hough, D.2    Danson, M.3    Taylor, G.4
  • 40
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution
    • Russell R., Ferguson J., Hough D., Danson M., Taylor G. L. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution. Biochemistry. 36:1997a;9983-9994.
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.1    Ferguson, J.2    Hough, D.3    Danson, M.4    Taylor, G.L.5
  • 41
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an antarctic bacterium
    • Russell R., Gerike U., Danson M., Hough D., Taylor G. L. Structural adaptations of the cold-active citrate synthase from an antarctic bacterium. Structure. 6:1997b;351-361.
    • (1997) Structure , vol.6 , pp. 351-361
    • Russell, R.1    Gerike, U.2    Danson, M.3    Hough, D.4    Taylor, G.L.5
  • 42
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • Sakon J., Adney W., Himmel M., Thomas S., Karplus P. Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry. 35:1996;10648-10660.
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.2    Himmel, M.3    Thomas, S.4    Karplus, P.5
  • 47
    • 0031952431 scopus 로고    scopus 로고
    • Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced stability
    • Usher K., De la Cruz A., Dahlquist F., Swanson R., Simon M., Remington S. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced stability. Protein Sci. 7:1998;403-412.
    • (1998) Protein Sci. , vol.7 , pp. 403-412
    • Usher, K.1    De La Cruz, A.2    Dahlquist, F.3    Swanson, R.4    Simon, M.5    Remington, S.6
  • 49
    • 0031406580 scopus 로고    scopus 로고
    • Investigations on the thermostability and function of truncated Thermus aquaticus DNA polymerase fragments
    • Villbrandt B., Sagner G., Schomburg D. Investigations on the thermostability and function of truncated Thermus aquaticus DNA polymerase fragments. Protein Eng. 10:1997;1281-1288.
    • (1997) Protein Eng. , vol.10 , pp. 1281-1288
    • Villbrandt, B.1    Sagner, G.2    Schomburg, D.3
  • 50
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G., Woell S., Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:1997a;631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 51
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing
    • Vogt G., Woell S., Argos P. Protein thermal stability: hydrogen bonds or internal packing. Folding Design. 1:1997b;S40-S46.
    • (1997) Folding Design , vol.1
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 52
    • 0031567156 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with the thermophilic counterpart from Thermus thermophilius
    • Wallon G., Kryger G., Lovett S., Oshima T., Ringe D., Petsko G. Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with the thermophilic counterpart from Thermus thermophilius. J. Mol. Biol. 266:1997;1016-1031.
    • (1997) J. Mol. Biol. , vol.266 , pp. 1016-1031
    • Wallon, G.1    Kryger, G.2    Lovett, S.3    Oshima, T.4    Ringe, D.5    Petsko, G.6
  • 53
    • 0004149831 scopus 로고    scopus 로고
    • Cambridge: Wolfram Media/Cambridge University Press
    • Wolfram S. The Mathematica Book. 1996;Wolfram Media/Cambridge University Press, Cambridge.
    • (1996) The Mathematica Book
    • Wolfram, S.1
  • 54
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
    • Zhang X., Baase W., Shoichet B., Wilson K., Matthews B. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Eng. 8:1995;1017-1022.
    • (1995) Protein Eng. , vol.8 , pp. 1017-1022
    • Zhang, X.1    Baase, W.2    Shoichet, B.3    Wilson, K.4    Matthews, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.