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Volumn 121, Issue 3, 1997, Pages 448-455

Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site-directed mutagenesis

Author keywords

Bacilli; DNA binding protein HU; Salt bridge; Site directed mutagenesis; Thermostability

Indexed keywords

AMINO ACID; DNA BINDING PROTEIN;

EID: 0031003188     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021609     Document Type: Article
Times cited : (32)

References (34)
  • 1
    • 0029018778 scopus 로고
    • Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis
    • Yu, M.-H., Weissman, J.S., and Kim, P.S. (1995) Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J. Mol. Biol. 249, 383-397
    • (1995) J. Mol. Biol. , vol.249 , pp. 383-397
    • Yu, M.-H.1    Weissman, J.S.2    Kim, P.S.3
  • 2
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews, B.W. (1993) Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62, 139-160
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 3
    • 0028107325 scopus 로고
    • The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease
    • Hardy, F., Vriend, G., van der Vinne, B., Frigerio, F., Grandi, G., Venema, G., and Eijsink, G.H. (1994) The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease. Protein Eng. 7, 425-430
    • (1994) Protein Eng. , vol.7 , pp. 425-430
    • Hardy, F.1    Vriend, G.2    Van der Vinne, B.3    Frigerio, F.4    Grandi, G.5    Venema, G.6    Eijsink, G.H.7
  • 4
    • 0026803109 scopus 로고
    • Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart
    • Kimura, S., Nakamura, H., Hashimoto, T., Oobatake, M., and Kanaya, S. (1992) Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. J. Biol. Chem. 267, 21535-21542
    • (1992) J. Biol. Chem. , vol.267 , pp. 21535-21542
    • Kimura, S.1    Nakamura, H.2    Hashimoto, T.3    Oobatake, M.4    Kanaya, S.5
  • 5
    • 0024974452 scopus 로고
    • Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices
    • Menendez-Arias, L. and Argos, P. (1989) Engineering protein thermal stability. Sequence statistics point to residue substitutions in α-helices. J. Mol. Biol. 206, 397-406
    • (1989) J. Mol. Biol. , vol.206 , pp. 397-406
    • Menendez-Arias, L.1    Argos, P.2
  • 7
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica, K. and Rouviere-Yaniv, J. (1987) Histone-like proteins of bacteria. Microbiol. Rev. 51, 301-319
    • (1987) Microbiol. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 8
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang, D.S. and Kornberg, A. (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J. Biol. Chem. 267, 23083-23086
    • (1992) J. Biol. Chem. , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 9
    • 0024558233 scopus 로고
    • Participation of the hup gene product in site-specific DNA inversion in Escherichia coli
    • Wada, M., Kutsukake, K., Komano, T., Imamoto, F., and Kano, Y. (1989) Participation of the hup gene product in site-specific DNA inversion in Escherichia coli. Gene 76, 345-352
    • (1989) Gene , vol.76 , pp. 345-352
    • Wada, M.1    Kutsukake, K.2    Komano, T.3    Imamoto, F.4    Kano, Y.5
  • 10
    • 0028302290 scopus 로고
    • A second high affinity HU binding site in the phage Mu transpososome
    • Lavoie, B. and Choconas, G. (1994) A second high affinity HU binding site in the phage Mu transpososome. J. Biol. Chem. 269, 15571-15576
    • (1994) J. Biol. Chem. , vol.269 , pp. 15571-15576
    • Lavoie, B.1    Choconas, G.2
  • 11
    • 0028901705 scopus 로고
    • HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps
    • Castaing, B., Zelwer, C., Laval, J., and Boiteux, S. (1995) HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps. J. Biol. Chem. 270, 10291-10296
    • (1995) J. Biol. Chem. , vol.270 , pp. 10291-10296
    • Castaing, B.1    Zelwer, C.2    Laval, J.3    Boiteux, S.4
  • 12
    • 0028226799 scopus 로고
    • DNA chaperons: A solution to a persistent problem
    • Travers, A.A., Ner, S.S., and Churchill, M.E.A. (1994) DNA chaperons: A solution to a persistent problem. Cell 77, 167-169
    • (1994) Cell , vol.77 , pp. 167-169
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.A.3
  • 13
    • 0020029752 scopus 로고
    • Purification and characterization of a small DNA-binding protein, HB, from Bacillus globigii
    • Imber, R., Bachinger, H., and Bickle, T.A. (1982) Purification and characterization of a small DNA-binding protein, HB, from Bacillus globigii. Eur. J. Biochem. 122, 627-632
    • (1982) Eur. J. Biochem. , vol.122 , pp. 627-632
    • Imber, R.1    Bachinger, H.2    Bickle, T.A.3
  • 14
    • 0020519939 scopus 로고
    • On the DNA binding protein II from Bacillus stearothermophilus. I. Purification, studies in solution, and crystallization
    • Dijk, J., White, S.W., Wilson, K.S., and Appelt, K. (1983) On the DNA binding protein II from Bacillus stearothermophilus. I. Purification, studies in solution, and crystallization. J. Biol. Chem. 258, 4003-4006
    • (1983) J. Biol. Chem. , vol.258 , pp. 4003-4006
    • Dijk, J.1    White, S.W.2    Wilson, K.S.3    Appelt, K.4
  • 15
    • 0021286693 scopus 로고
    • 3-A resolution structure of a protein with histone-like properties in procaryotes
    • Tanaka, I., Appelt, K., Dijk, J., White, S.W., and Wilson, K.S. (1984) 3-A resolution structure of a protein with histone-like properties in procaryotes. Nature 310, 376-381
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 17
    • 0028670214 scopus 로고
    • 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- And three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy
    • 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry 33, 14858-14870
    • (1994) Biochemistry , vol.33 , pp. 14858-14870
    • Vis, H.1    Boelens, R.2    Mariani, M.3    Stroop, R.4    Vorgias, C.E.5    Wilson, K.S.6    Kaptein, R.7
  • 19
    • 0029670677 scopus 로고    scopus 로고
    • Glycine-15 in the bend between two α-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus
    • Kawamura, S., Kakuta, Y., Tanaka, I., Hikichi, K., Kuhara, S., Yamasaki, N., and Kimura, M. (1996) Glycine-15 in the bend between two α-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus. Biochemistry 35, 1195-1200
    • (1996) Biochemistry , vol.35 , pp. 1195-1200
    • Kawamura, S.1    Kakuta, Y.2    Tanaka, I.3    Hikichi, K.4    Kuhara, S.5    Yamasaki, N.6    Kimura, M.7
  • 20
    • 0026651448 scopus 로고
    • Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene
    • Groch, N., Schindelin, H., Schdtz, A., Hahn, U., and Heineman, U. (1992) Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene. Eur. J. Biochem. 207, 677-685
    • (1992) Eur. J. Biochem. , vol.207 , pp. 677-685
    • Groch, N.1    Schindelin, H.2    Schdtz, A.3    Hahn, U.4    Heineman, U.5
  • 21
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W.P. and Nickoloff, J.A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200, 81-88
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 23
    • 85007837614 scopus 로고
    • Cloning of the gene encoding DNA binding protein HU from Bacillus stearothermophilus and its expression in Escherichia coli
    • Kawamura, S., Kajiyama, H., Yamasaki, N., and Kimura, M. (1995) Cloning of the gene encoding DNA binding protein HU from Bacillus stearothermophilus and its expression in Escherichia coli. Biosci. Biotech. Biochem. 59, 126-129
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 126-129
    • Kawamura, S.1    Kajiyama, H.2    Yamasaki, N.3    Kimura, M.4
  • 24
    • 0026607456 scopus 로고
    • Salt-dependent and protein-concentration-dependent changes in the solution structure of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis
    • Welfle, H., Misselwitz, R., Welfle, K., Groch, N., and Heineman, U. (1992) Salt-dependent and protein-concentration-dependent changes in the solution structure of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis. Eur. J. Biochem. 204, 1049-1055
    • (1992) Eur. J. Biochem. , vol.204 , pp. 1049-1055
    • Welfle, H.1    Misselwitz, R.2    Welfle, K.3    Groch, N.4    Heineman, U.5
  • 25
    • 0027517954 scopus 로고
    • Conformations and conformational changes of four Phe→Trp variants of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis studied by circular dichroism and fluorescence spectroscopy
    • Welfle, H., Misselwitz, R., Welfle, K., Schindelin, H., Scholtz, A., and Heinemann, U. (1993) Conformations and conformational changes of four Phe→Trp variants of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis studied by circular dichroism and fluorescence spectroscopy. Eur. J. Biochem. 217, 849-856
    • (1993) Eur. J. Biochem. , vol.217 , pp. 849-856
    • Welfle, H.1    Misselwitz, R.2    Welfle, K.3    Schindelin, H.4    Scholtz, A.5    Heinemann, U.6
  • 26
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W.J. and Schellman, J.A. (1987) Protein stability curves. Biopolymers 26, 1859-1877
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 27
    • 0015967881 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y. and Fasman, G. (1974) Prediction of protein conformation. Biochemistry 13, 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.2
  • 28
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double- Mutant cycles
    • Serrano, L., Horovitz, A., Avron, B., Bycroft, M., and Fersht, A.R. (1990) Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double- mutant cycles. Biochemistry 29, 9343-9352
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 29
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A., Serrano, L., Avron, B., Bycroft, M., and Fersht, A.R. (1990) Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 1031-1044
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 30
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little to stability of Barnase
    • Sali, D., Bycroft, M., and Fersht, A.R. (1991) Surface electrostatic interactions contribute little to stability of Barnase. J. Mol. Biol. 220, 779-788
    • (1991) J. Mol. Biol. , vol.220 , pp. 779-788
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 31
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Dao-pin, S., Sauer, U., Nicholson, H., and Matthews, B.W. (1991) Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30, 7142-7153
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Dao-pin, S.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 32
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding
    • Pantoliano, M.W., Whitlow, M., Wood, J.F., Dodd, S.W., Hardman, K.D., Rollence, M.L., and Bryan, P.N. (1989) Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry 28, 7205-7213
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Dodd, S.W.4    Hardman, K.D.5    Rollence, M.L.6    Bryan, P.N.7
  • 33
    • 0023793010 scopus 로고
    • Combining thermostable mutations increases the stability of λ repressor
    • Stearman, R.S., Frankel, A.D., Freire, E., Liu, B., and Pabo, C.O. (1988) Combining thermostable mutations increases the stability of λ repressor. Biochemistry 27, 7571-7574
    • (1988) Biochemistry , vol.27 , pp. 7571-7574
    • Stearman, R.S.1    Frankel, A.D.2    Freire, E.3    Liu, B.4    Pabo, C.O.5
  • 34
    • 0029078751 scopus 로고
    • High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation
    • Akasako, A., Haruki, M., Oobatake, M., and Kanaya, S. (1995) High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. Biochemistry 34, 8115-8122
    • (1995) Biochemistry , vol.34 , pp. 8115-8122
    • Akasako, A.1    Haruki, M.2    Oobatake, M.3    Kanaya, S.4


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