메뉴 건너뛰기




Volumn 71, Issue 1, 2008, Pages 110-118

Osmolyte effect on the stability and folding of a hyperthermophilic protein

Author keywords

Circular dichroism; Guanidine hydrochloride; Protein unfolding; Ribonuclease HII; Thermococcus kodakaraensis; Trimethylamine N oxide

Indexed keywords

GUANIDINE; RIBONUCLEASE H; TRIMETHYLAMINE OXIDE;

EID: 40549104479     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21660     Document Type: Article
Times cited : (54)

References (50)
  • 1
    • 0018641198 scopus 로고
    • Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes
    • Yancey PH, Somero GN. Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes. Biochem J 1979;18:317-323.
    • (1979) Biochem J , vol.18 , pp. 317-323
    • Yancey, P.H.1    Somero, G.N.2
  • 3
    • 0141815727 scopus 로고    scopus 로고
    • Glutamate counteracts the denaturing effect of urea through its effect on the denatured state
    • Mandal AK, Samaddar S, Banerjee R, Lahiri S, Bhattacharyya A, Roy S. Glutamate counteracts the denaturing effect of urea through its effect on the denatured state. J Biol Chem 2003;278:36077-36084.
    • (2003) J Biol Chem , vol.278 , pp. 36077-36084
    • Mandal, A.K.1    Samaddar, S.2    Banerjee, R.3    Lahiri, S.4    Bhattacharyya, A.5    Roy, S.6
  • 5
    • 3142619246 scopus 로고    scopus 로고
    • Mutational and structural-based analyses of the osmolyte effect on protein stability
    • Takano K, Saito M, Morikawa M, Kanaya S. Mutational and structural-based analyses of the osmolyte effect on protein stability. J Biochem 2004;135:701-708.
    • (2004) J Biochem , vol.135 , pp. 701-708
    • Takano, K.1    Saito, M.2    Morikawa, M.3    Kanaya, S.4
  • 6
    • 0029034433 scopus 로고
    • An osmolyte effect on the heat capacity change for protein folding
    • Plaza-del-Pino IM, Sanchez-Ruiz JM. An osmolyte effect on the heat capacity change for protein folding. Biochemistry 1995;34:8621-8630.
    • (1995) Biochemistry , vol.34 , pp. 8621-8630
    • Plaza-del-Pino, I.M.1    Sanchez-Ruiz, J.M.2
  • 7
    • 33746882148 scopus 로고    scopus 로고
    • Metrics that differentiate the origins of osmolyte effects on protein stability: A test of the surface tension proposal
    • Auton M, Ferreon ACM, Bolen DW. Metrics that differentiate the origins of osmolyte effects on protein stability: a test of the surface tension proposal. J Mol Biol 2006;361:983-992.
    • (2006) J Mol Biol , vol.361 , pp. 983-992
    • Auton, M.1    Ferreon, A.C.M.2    Bolen, D.W.3
  • 8
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • Street TO, Bolen DW, Rose GD. A molecular mechanism for osmolyte-induced protein stability. Proc Natl Acad Sci USA 2006;103:13397-14002.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13397-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 9
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff SN. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu Rev Biophys Biomol Struct 1993;22:67-97.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 10
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff SN. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc Natl Acad Sci USA 2002;99:9721-9726.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 11
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang A, Bolen DW. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 1997;36:9101-9108.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 12
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen DW, Baskakov IV. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J Mol Biol 2001;310: 955-963.
    • (2001) J Mol Biol , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 13
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Bohm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998;8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 14
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D, Mueller U, Heinemann U, Schmid FX. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol 2000;7:380-383.
    • (2000) Nat Struct Biol , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 15
    • 16244366490 scopus 로고    scopus 로고
    • Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein L30e
    • Lee CF, Allen MD, Bycroft M, Wong KB. Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein L30e. J Mol Biol 2005;348:419-431.
    • (2005) J Mol Biol , vol.348 , pp. 419-431
    • Lee, C.F.1    Allen, M.D.2    Bycroft, M.3    Wong, K.B.4
  • 16
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 2001;65:1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 17
    • 0036742110 scopus 로고    scopus 로고
    • Compatible solutes of organisms that live in hot saline environments
    • Santos H, da Costa MS. Compatible solutes of organisms that live in hot saline environments. Environ Microbiol 2002;4:501-509.
    • (2002) Environ Microbiol , vol.4 , pp. 501-509
    • Santos, H.1    da Costa, M.S.2
  • 18
    • 10344236053 scopus 로고    scopus 로고
    • Protein stabilization by osmolytes from hyperthermophiles: Effect of mannosylglycerate on the thermal unfolding of recombinant nuclease from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry
    • Faria TQ, Lima JC, Bastos M, Maçanita AL, Santos H. Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry. J Biol Chem 2004;279:48680-48691.
    • (2004) J Biol Chem , vol.279 , pp. 48680-48691
    • Faria, T.Q.1    Lima, J.C.2    Bastos, M.3    Maçanita, A.L.4    Santos, H.5
  • 20
    • 0035083849 scopus 로고    scopus 로고
    • Catalytic center of an archaeal type2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses
    • Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K. Catalytic center of an archaeal type2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses. Protein Sci 2001;10:707-714.
    • (2001) Protein Sci , vol.10 , pp. 707-714
    • Muroya, A.1    Tsuchiya, D.2    Ishikawa, M.3    Haruki, M.4    Morikawa, M.5    Kanaya, S.6    Morikawa, K.7
  • 22
    • 33750349072 scopus 로고    scopus 로고
    • A hyperthermophilic protein acquires function at the cost of stability
    • Mukaiyama A, Haruki M, Ota M, Koga Y, Takano K, Kanaya S. A hyperthermophilic protein acquires function at the cost of stability. Biochemistry 2006;45:12673-12679.
    • (2006) Biochemistry , vol.45 , pp. 12673-12679
    • Mukaiyama, A.1    Haruki, M.2    Ota, M.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 23
    • 0017163943 scopus 로고
    • Intracellular osmoregulatory role of amino acids and urea in marine elasmobranchs
    • Forster RP, Goldstein L. Intracellular osmoregulatory role of amino acids and urea in marine elasmobranchs. Am J Physiol 1976;230:925-931.
    • (1976) Am J Physiol , vol.230 , pp. 925-931
    • Forster, R.P.1    Goldstein, L.2
  • 24
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen BW. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 1988;27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, B.W.2
  • 25
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace CN. Measuring and increasing protein stability. Trends Biotechnol 1990;8:93-98.
    • (1990) Trends Biotechnol , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 27
    • 0030582620 scopus 로고    scopus 로고
    • Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d
    • McCrary BS, Edmondson SP, Shriver JW. Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d. J Mol Biol 264;1996:784-805.
    • (1996) J Mol Biol , vol.264 , pp. 784-805
    • McCrary, B.S.1    Edmondson, S.P.2    Shriver, J.W.3
  • 28
    • 0033596902 scopus 로고    scopus 로고
    • A thermodynamic comparison of mesophilic and thermophilic ribonucleases H
    • Hollien J, Marqusee S. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry 1999;38:3831-3836.
    • (1999) Biochemistry , vol.38 , pp. 3831-3836
    • Hollien, J.1    Marqusee, S.2
  • 29
    • 33645554971 scopus 로고    scopus 로고
    • A thermodynamic comparison of HPr proteins from extremophilic organisms
    • Razvi A, Scholtz JM. A thermodynamic comparison of HPr proteins from extremophilic organisms. Biochemistry 2006;45:4084-4092.
    • (2006) Biochemistry , vol.45 , pp. 4084-4092
    • Razvi, A.1    Scholtz, J.M.2
  • 30
  • 31
    • 4644261149 scopus 로고    scopus 로고
    • Osmolyte induce structure in an early intermediate on the folding pathway of barstar
    • Pradeep L, Udgaonkar JB. Osmolyte induce structure in an early intermediate on the folding pathway of barstar. J Biol Chem 2004;279:40303- 40313.
    • (2004) J Biol Chem , vol.279 , pp. 40303-40313
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 32
    • 0037633978 scopus 로고    scopus 로고
    • Measuring the stability of partly folded proteins using TMAO
    • Mello C, Barrick D. Measuring the stability of partly folded proteins using TMAO. Protein Sci 2003;12:1522-1529.
    • (2003) Protein Sci , vol.12 , pp. 1522-1529
    • Mello, C.1    Barrick, D.2
  • 33
    • 15744404427 scopus 로고    scopus 로고
    • a: Measurement of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide
    • a: measurement of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide. J Biol Chem 280;2005:11035-11042.
    • (2005) J Biol Chem , vol.280 , pp. 11035-11042
    • Singh, R.1    Haque, I.2    Ahmad, F.3
  • 35
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 1995;4:2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 36
    • 22444433527 scopus 로고    scopus 로고
    • Stabilization of the ribosomal protein S6 by Trehalose is counterbalanced by the formation of a putative off-pathway species
    • Chen L, Cabrita GJM, Otzen DE, Melo EP. Stabilization of the ribosomal protein S6 by Trehalose is counterbalanced by the formation of a putative off-pathway species. J Mol Biol 2005;351:402-416.
    • (2005) J Mol Biol , vol.351 , pp. 402-416
    • Chen, L.1    Cabrita, G.J.M.2    Otzen, D.E.3    Melo, E.P.4
  • 37
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP, Freire E. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 1992;43:313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 39
    • 21844431597 scopus 로고    scopus 로고
    • Testing polyol's compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes
    • Haque I, Singh R, Ahmad F, Moosavi-Movahedi AA. Testing polyol's compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes. FEBS Lett 2005;579:3891-3898.
    • (2005) FEBS Lett , vol.579 , pp. 3891-3898
    • Haque, I.1    Singh, R.2    Ahmad, F.3    Moosavi-Movahedi, A.A.4
  • 40
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose
    • Kaushik JK, Bhat R. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J Biol Chem 2003;278:26458-26465.
    • (2003) J Biol Chem , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 41
    • 0030898066 scopus 로고    scopus 로고
    • The kinetic basis for the stabilization of staphylococcal nuclease by xylose
    • Frye KJ, Royer CA. The kinetic basis for the stabilization of staphylococcal nuclease by xylose. Protein Sci 1997;6:789-793.
    • (1997) Protein Sci , vol.6 , pp. 789-793
    • Frye, K.J.1    Royer, C.A.2
  • 43
    • 0041743073 scopus 로고    scopus 로고
    • Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization
    • Russo AT, Rösgen J, Bolen DW. Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization. J Mol Biol 2003;330:851-866.
    • (2003) J Mol Biol , vol.330 , pp. 851-866
    • Russo, A.T.1    Rösgen, J.2    Bolen, D.W.3
  • 44
    • 0014718113 scopus 로고
    • Protein folding: Part C
    • Tanford C. Protein folding: part C. Adv Protein Chem 1970;24:1-95.
    • (1970) Adv Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 45
    • 1342296307 scopus 로고
    • The activated complex and the absolute rate of chemical reactions
    • Eyring H. The activated complex and the absolute rate of chemical reactions. Chem Rev 1935;17:65-77.
    • (1935) Chem Rev , vol.17 , pp. 65-77
    • Eyring, H.1
  • 46
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi H, Fukui T, Kanai T, Morikawa M, Imanaka T. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 2004;1:263-267.
    • (2004) Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 48
    • 0032502317 scopus 로고    scopus 로고
    • Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins
    • Cavagnero S, Debe DA, Zhou ZH, Adams MWW, Chan SI. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins. Biochemistry 1998;37:3369-3376.
    • (1998) Biochemistry , vol.37 , pp. 3369-3376
    • Cavagnero, S.1    Debe, D.A.2    Zhou, Z.H.3    Adams, M.W.W.4    Chan, S.I.5
  • 49
    • 0032534842 scopus 로고    scopus 로고
    • The unusually slow unfolding rate causes the high stability of pyroolidone carboxyl peptidase from a hyperthermophilile Pyrococcus furiosus: Equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding
    • Ogasahara K, Nakamura M, Nakura S, Tsunasawa S, Kato I, Yoshimoto T, Yutani K. The unusually slow unfolding rate causes the high stability of pyroolidone carboxyl peptidase from a hyperthermophilile Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding. Biochemistry 1998;37:17537-17544.
    • (1998) Biochemistry , vol.37 , pp. 17537-17544
    • Ogasahara, K.1    Nakamura, M.2    Nakura, S.3    Tsunasawa, S.4    Kato, I.5    Yoshimoto, T.6    Yutani, K.7
  • 50
    • 0346500473 scopus 로고    scopus 로고
    • Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus
    • Zeeb M, Lipps G, Lilie H, Balbach J. Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus. J Mol Biol 2004;336:227-240.
    • (2004) J Mol Biol , vol.336 , pp. 227-240
    • Zeeb, M.1    Lipps, G.2    Lilie, H.3    Balbach, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.