메뉴 건너뛰기




Volumn 279, Issue 1, 2012, Pages 78-90

Role of charged residues in stabilization of Pyrococcus horikoshii CutA1, which has a denaturation temperature of nearly 150 °c

Author keywords

CutA1; DSC; heat stability of protein; hyperthermophile; ion ion interaction

Indexed keywords

BACTERIAL PROTEIN; MUTANT PROTEIN; PYROCOCCUS HORIKOSHII CUTA1 PROTEIN; UNCLASSIFIED DRUG;

EID: 83655161388     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08400.x     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 0037931826 scopus 로고    scopus 로고
    • Genomic correlates of hyperthermostability, an update
    • Suhre K, &, Claverie JM, (2003) Genomic correlates of hyperthermostability, an update. J Biol Chem 278, 17198-171202.
    • (2003) J Biol Chem , vol.278 , pp. 17198-171202
    • Suhre, K.1    Claverie, J.M.2
  • 2
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer I, Steipe B, Huber R, Tomschy A, &, Jaenicke R, (1995) The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J Mol Biol 246, 511-521.
    • (1995) J Mol Biol , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 3
    • 0028994307 scopus 로고
    • 2.0 Angstrom structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • DOI 10.1016/S0969-2126(01)00267-2
    • Hennig M, Darimont B, Sterner R, Kirschner K, &, Jansonius JN, (1995) 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 3, 1295-1306. (Pubitemid 3012260)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 4
    • 0031570334 scopus 로고    scopus 로고
    • Formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - New insights into salt-dependence and thermostability
    • Ermler U, Merckel MC, Thauer RK, &, Shima S, (1997) Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri- new insights into salt-dependence and thermostability. Structure 5, 635-646. (Pubitemid 27236263)
    • (1997) Structure , vol.5 , Issue.5 , pp. 635-646
    • Ermler, U.1    Merckel, M.C.2    Thauer, R.K.3    Shima, S.4
  • 5
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the -glycosidase from the hyperthermophilic archeon sulfolobus solfataricus: Resilience as a key factor in thermostability
    • DOI 10.1006/jmbi.1997.1215
    • Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, &, Pearl LH, (1997) Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J Mol Biol 271, 789-802. (Pubitemid 27376054)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.5 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7
  • 6
    • 0032574696 scopus 로고    scopus 로고
    • Electrostatic stabilization in methionine aminopeptidase from hyperthermophile Pyrococcus furiosus
    • DOI 10.1021/bi973172q
    • Ogasahara K, Lapshina EA, Sakai M, Izu Y, Tsunasawa S, Kato I, &, Yutani K, (1998) Electrostatic stabilization in methionine aminopeptidase from hyperthermophile Pyrococcus furiosus. Biochemistry 37, 5939-5946. (Pubitemid 28196746)
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 5939-5946
    • Ogasahara, K.1    Lapshina, E.A.2    Sakai, M.3    Izu, Y.4    Tsunasawa, S.5    Kato, I.6    Yutani, K.7
  • 9
    • 0344609869 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: Contribution of salt bridges to thermostability
    • DOI 10.1006/jmbi.1998.2397
    • de Bakker PI, Hünenberger PH, &, McCammon JA, (1999) Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability. J Mol Biol 285, 1811-1830. (Pubitemid 29060473)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1811-1830
    • De Bakker, P.I.W.1    Hunenberger, P.H.2    McCammon, J.A.3
  • 10
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A 'traffic rule' for hot roads
    • DOI 10.1016/S0968-0004(01)01918-1, PII S0968000401019181
    • Karshikoff A, &, Ladenstein R, (2001) Ion pairs and the thermotolerance of proteins from hyperthermophiles: a 'traffic rule' for hot roads. Trends Biochem Sci 26, 550-556. (Pubitemid 32823440)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.9 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 11
    • 0035815708 scopus 로고    scopus 로고
    • Entropic stabilization of the tryptophan synthase -subunit from a hyperthermophile, Pyrococcus furiosus: X-ray analysis and calorimetry
    • DOI 10.1074/jbc.M009987200
    • Yamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, &, Yutani K, (2001) Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus: X-ray analysis and calorimetry. J Biol Chem 276, 11062-11071. (Pubitemid 38089288)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11062-11071
    • Yamagata, Y.1    Ogasahara, K.2    Hioki, Y.3    Lee, S.J.4    Nakagawa, A.5    Nakamura, H.6    Ishida, M.7    Kuramitsu, S.8    Yutani, K.9
  • 12
    • 30844449653 scopus 로고    scopus 로고
    • Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: Lessons from structural genomics of Thermotoga maritima
    • DOI 10.1016/j.jmb.2005.11.065, PII S0022283605014798
    • Robinson-Rechavi M, Alibés A, &, Godzik A, (2006) Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima. J Mol Biol 356, 547-557. (Pubitemid 43102585)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.2 , pp. 547-557
    • Robinson-Rechavi, M.1    Alibes, A.2    Godzik, A.3
  • 14
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B, &, Yang AS, (1995) Free energy balance in protein folding. Adv Protein Chem 46, 27-58.
    • (1995) Adv Protein Chem , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 15
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • DOI 10.1038/nsb0295-122
    • Waldburger CD, Schildbach JF, &, Sauer RT, (1995) Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol 2, 122-128. (Pubitemid 26040648)
    • (1995) Nature Structural Biology , vol.2 , Issue.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 16
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace CN, Shirley BA, McNutt M, &, Gajiwala K, (1996) Forces contributing to the conformational stability of proteins. FASEB J 10, 75-83. (Pubitemid 26035509)
    • (1996) FASEB Journal , vol.10 , Issue.1 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    Mcnutt, M.3    Gajiwala, K.4
  • 17
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov PL, &, Gill SJ, (1988) Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39, 191-234.
    • (1988) Adv Protein Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 18
    • 0036290245 scopus 로고    scopus 로고
    • The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus
    • DOI 10.1006/jmbi.2001.5355
    • Kaushik JK, Ogasahara K, &, Yutani K, (2002) The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus. J Mol Biol 316, 991-1003. (Pubitemid 34722136)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.4 , pp. 991-1003
    • Kaushik, J.K.1    Ogasahara, K.2    Yutani, K.3
  • 19
    • 0023368698 scopus 로고
    • Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α-subunit
    • Yutani K, Ogasahara K, Tsujita T, &, Sugino Y, (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α-subunit. Proc Natl Acad Sci USA 84, 4441-4444.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4441-4444
    • Yutani, K.1    Ogasahara, K.2    Tsujita, T.3    Sugino, Y.4
  • 20
    • 0028786432 scopus 로고
    • Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants
    • Takano K, Ogasahara K, Kaneda H, Yamagata Y, Fujii S, Kanaya E, Kikuchi M, Oobatake M, &, Yutani K, (1995) Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J Mol Biol 254, 62-76.
    • (1995) J Mol Biol , vol.254 , pp. 62-76
    • Takano, K.1    Ogasahara, K.2    Kaneda, H.3    Yamagata, Y.4    Fujii, S.5    Kanaya, E.6    Kikuchi, M.7    Oobatake, M.8    Yutani, K.9
  • 21
    • 0032581023 scopus 로고    scopus 로고
    • Contribution of hydrogen bonds to the conformational stability of human lysozyme: Calorimetry and X-ray analysis of six tyrosine phenylalanine mutants
    • DOI 10.1021/bi980431i
    • Yamagata Y, Kubota M, Sumikawa Y, Funahashi J, Takano K, Fujii S, &, Yutani K, (1998) Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine → phenylalanine mutants. Biochemistry 37, 9355-9362. (Pubitemid 28307689)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9355-9362
    • Yamagata, Y.1    Kubota, M.2    Sumikawa, Y.3    Funahashi, J.4    Takano, K.5    Fujii, S.6    Yutani, K.7
  • 22
    • 0035037981 scopus 로고    scopus 로고
    • Are the parameters of various stabilization factors estimated from mutant human lysozymes compatible with other proteins?
    • Funahashi J, Takano K, &, Yutani K, (2001) Are the parameters of various stabilization factors estimated from mutant human lysozymes compatible with other proteins? Protein Eng 14, 127-134. (Pubitemid 32397559)
    • (2001) Protein Engineering , vol.14 , Issue.2 , pp. 127-134
    • Funahashi, J.1    Takano, K.2    Yutani, K.3
  • 23
    • 0034798511 scopus 로고    scopus 로고
    • A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins
    • Takano K, &, Yutani K, (2001) A new scale for side chain contribution to protein stability based on the empirical stability analysis of mutant proteins. Protein Eng 14, 525-528. (Pubitemid 32959475)
    • (2001) Protein Engineering , vol.14 , Issue.8 , pp. 525-528
    • Takano, K.1    Yutani, K.2
  • 24
    • 0028965483 scopus 로고
    • Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12
    • Fong ST, Camakaris J, &, Lee BT, (1995) Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol Microbiol 15, 1127-1137.
    • (1995) Mol Microbiol , vol.15 , pp. 1127-1137
    • Fong, S.T.1    Camakaris, J.2    Lee, B.T.3
  • 26
    • 38849117701 scopus 로고    scopus 로고
    • Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii, Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures
    • DOI 10.1021/bi701761m
    • Sawano M, Yamamoto H, Ogasahara K, Kidokoro S, Katoh S, Ohnuma T, Katoh E, Yokoyama S, &, Yutani K, (2008) Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii, Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures. Biochemistry 47, 721-730. (Pubitemid 351195443)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 721-730
    • Sawano, M.1    Yamamoto, H.2    Ogasahara, K.3    Kidokoro, S.-I.4    Katoh, S.5    Ohnuma, T.6    Katoh, E.7    Yokoyama, S.8    Yutani, K.9
  • 27
    • 0020172455 scopus 로고
    • α-Helix dipole model and electrostatic stabilization of 4-α-helical proteins
    • Sheridan RP, Levy RM, &, Salemme FR, (1982) α-Helix dipole model and electrostatic stabilization of 4-α-helical proteins. Proc Natl Acad Sci USA 79, 4545-4549.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4545-4549
    • Sheridan, R.P.1    Levy, R.M.2    Salemme, F.R.3
  • 28
    • 0023726958 scopus 로고
    • Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain
    • Sali D, Bycroft M, &, Fersht AR, (1988) Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain. Nature 335, 740-743.
    • (1988) Nature , vol.335 , pp. 740-743
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 29
    • 0025973269 scopus 로고
    • Dipoles localized at helix termini of proteins stabilize charges
    • Aqvist J, Luecke H, Quiocho FA, &, Warshel A, (1991) Dipoles localized at helix termini of proteins stabilize charges. Proc Natl Acad Sci USA 88, 2026-2030.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2026-2030
    • Aqvist, J.1    Luecke, H.2    Quiocho, F.A.3    Warshel, A.4
  • 30
    • 77956727554 scopus 로고
    • The interpretation of hydrogen ion titration curves of proteins
    • Tanford C, (1962) The interpretation of hydrogen ion titration curves of proteins. Adv Protein Chem 17, 69-165.
    • (1962) Adv Protein Chem , vol.17 , pp. 69-165
    • Tanford, C.1
  • 31
    • 33745019845 scopus 로고    scopus 로고
    • Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles
    • DOI 10.1021/bi052610n
    • Kaushik JK, Iimura S, Ogasahara K, Yamagata Y, Segawa S, &, Yutan K, (2006) Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles. Biochemistry 45, 7100-7112. (Pubitemid 43877398)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7100-7112
    • Kaushik, J.K.1    Iimura, S.2    Ogasahara, K.3    Yamagata, Y.4    Segawa, S.-I.5    Yutani, K.6
  • 32
    • 79958769952 scopus 로고    scopus 로고
    • Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges
    • Bush J, &, Makhatadze GI, (2011) Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges. Proteins 79, 2027-2032.
    • (2011) Proteins , vol.79 , pp. 2027-2032
    • Bush, J.1    Makhatadze, G.I.2
  • 33
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • DOI 10.1016/S0022-2836(02)00442-4
    • Guerois R, Nielsen JE, &, Serrano L, (2002) Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J Mol Biol 320, 369-387. (Pubitemid 34722226)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.2 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 35
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • DOI 10.1006/jmbi.1998.2159
    • Elcock AH, (1998) The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J Mol Biol 284, 489-502. (Pubitemid 28542468)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.2 , pp. 489-502
    • Elcock, A.H.1
  • 37
    • 59649107985 scopus 로고    scopus 로고
    • A computational approach for the rational design of stable proteins and enzymes: Optimization of surface charge-charge interactions
    • Schweiker KL, &, Makhatadze GI, (2009) A computational approach for the rational design of stable proteins and enzymes: optimization of surface charge-charge interactions. Methods Enzymol 454, 175-211.
    • (2009) Methods Enzymol , vol.454 , pp. 175-211
    • Schweiker, K.L.1    Makhatadze, G.I.2
  • 38
    • 33947468892 scopus 로고
    • Theory of protein titration curves. I. General equations for impenetrable spheres
    • Tanford C, &, Kirkwood JG, (1957) Theory of protein titration curves. I. General equations for impenetrable spheres. J Am Chem Soc 79, 5333-5339.
    • (1957) J Am Chem Soc , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 42
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, &, Gray T, (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4, 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.