메뉴 건너뛰기




Volumn 413, Issue 1, 2011, Pages 150-161

Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations

Author keywords

apparent protein stability; protein engineering; TOM complex; Tom40; barrel

Indexed keywords

BETA BARREL PROTEIN; MEMBRANE PROTEIN; PORIN; TOM40A PROTEIN; UNCLASSIFIED DRUG;

EID: 80053324844     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.054     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia T., and Freire E. Forces and factors that contribute to the structural stability of membrane proteins Biochim. Biophys. Acta 1228 1995 1 27
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 2
    • 34250187443 scopus 로고    scopus 로고
    • The Role of a Hydrogen Bonding Network in the Transmembrane β-Barrel OMPLA
    • DOI 10.1016/j.jmb.2007.05.009, PII S0022283607006213
    • Stanley A., and Fleming K. The role of a hydrogen bonding network in the transmembrane beta-barrel OMPLA J. Mol. Biol. 370 2007 912 924 (Pubitemid 46899067)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.5 , pp. 912-924
    • Stanley, A.M.1    Fleming, K.G.2
  • 3
    • 69149083388 scopus 로고    scopus 로고
    • Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins
    • Naveed H., Jackups R. Jr., and Liang J. Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins Proc. Natl Acad. Sci. USA 106 2009 12735 12740
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 12735-12740
    • Naveed, H.1    Jackups, Jr.R.2    Liang, J.3
  • 4
    • 79751537491 scopus 로고    scopus 로고
    • Evolutionary conservation of lipid-binding sites in membrane proteins
    • Adamian L., Naveed H., and Liang J. Evolutionary conservation of lipid-binding sites in membrane proteins Biochim. Biophys. Acta, Biomembr. 1808 2011 1092 1102
    • (2011) Biochim. Biophys. Acta, Biomembr. , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 8
    • 33745670602 scopus 로고    scopus 로고
    • Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP
    • DOI 10.1021/ja0610075
    • Evanics F., Hwang P.M., Cheng Y., Kay L.E., and Prosser R.S. Topology of an outer-membrane enzyme: measuring oxygen and water contacts in solution NMR studies of PagP J. Am. Chem. Soc. 128 2006 8256 8264 (Pubitemid 43967770)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.25 , pp. 8256-8264
    • Evanics, F.1    Hwang, P.M.2    Cheng, Y.3    Kay, L.E.4    Prosser, R.S.5
  • 9
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • DOI 10.1083/jcb.153.6.1151
    • Ahting U., Thieffry M., Engelhardt H., Hegerl R., Neupert W., and Nussberger S. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria J. Cell Biol. 153 2001 1151 1160 (Pubitemid 34289255)
    • (2001) Journal of Cell Biology , vol.153 , Issue.6 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 10
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • DOI 10.1038/26780
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., and Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins Nature 395 1998 516 521 (Pubitemid 28462448)
    • (1998) Nature , vol.395 , Issue.6701 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martint, F.5    Wagner, R.6    Pfanner, N.7
  • 11
    • 38449097898 scopus 로고    scopus 로고
    • Identification and characterization of a new Tom40 isoform, a central component of mitochondrial outer membrane translocase
    • DOI 10.1093/jb/mvm097
    • Kinoshita J.Y., Mihara K., and Oka T. Identification and characterization of a new tom40 isoform, a central component of mitochondrial outer membrane translocase J. Biochem. (Tokyo) 141 2007 897 906 (Pubitemid 351455330)
    • (2007) Journal of Biochemistry , vol.141 , Issue.6 , pp. 897-906
    • Kinoshita, J.-Y.1    Mihara, K.2    Oka, T.3
  • 13
    • 0034531390 scopus 로고    scopus 로고
    • Characterization of rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membrane
    • DOI 10.1074/jbc.M006558200
    • Suzuki H., Okazawa Y., Komiya T., Saeki K., Mekada E., and Kitada S. Characterization of rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membrane J. Biol. Chem. 275 2000 37930 37936 (Pubitemid 32004913)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37930-37936
    • Suzuki, H.1    Okazawa, Y.2    Komiya, T.3    Saeki, K.4    Mekada, E.5    Kitada, S.6    Ito, A.7    Mihara, K.8
  • 14
    • 0038687177 scopus 로고    scopus 로고
    • Identification of novel subunits of the TOM complex from Arabidopsis thaliana
    • DOI 10.1016/S0981-9428(03)00047-0
    • Werhahn W., Jänsch L., and Braun H.P. Identification of novel subunits of the TOM complex of Arabidopsis thaliana Plant Physiol. Biochem. 41 2003 407 416 (Pubitemid 36708596)
    • (2003) Plant Physiology and Biochemistry , vol.41 , Issue.5 , pp. 407-416
    • Werhahn, W.1    Jansch, L.2    Braun, H.-P.3
  • 16
    • 60149110944 scopus 로고    scopus 로고
    • The single mitochondrial porin of Trypanosoma brucei is the main metabolite transporter in the outer mitochondrial membrane
    • Pusnik M., Charriere F., Maser P., Waller R.F., Dagley M.J., Lithgow T., and Schneider A. The single mitochondrial porin of Trypanosoma brucei is the main metabolite transporter in the outer mitochondrial membrane Mol. Biol. Evol. 26 2009 671 680
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 671-680
    • Pusnik, M.1    Charriere, F.2    Maser, P.3    Waller, R.F.4    Dagley, M.J.5    Lithgow, T.6    Schneider, A.7
  • 17
    • 77953811604 scopus 로고    scopus 로고
    • Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology
    • Zeth K. Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology Biochim. Biophys. Acta 1797 2010 1292 1299
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1292-1299
    • Zeth, K.1
  • 19
    • 33846207499 scopus 로고    scopus 로고
    • L
    • DOI 10.1021/bi061577h
    • Malia T.J., and Wagner G. NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL Biochemistry 46 2007 514 525 (Pubitemid 46105440)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 20
    • 28444482763 scopus 로고    scopus 로고
    • Interstrand pairing patterns in β-barrel membrane proteins: The positive-outside rule, aromatic rescue, and strand registration prediction
    • DOI 10.1016/j.jmb.2005.09.094, PII S0022283605011654
    • Jackups R. Jr., and Liang J. Interstrand pairing patterns in beta-barrel membrane proteins: the positive-outside rule, aromatic rescue, and strand registration prediction J. Mol. Biol. 354 2005 979 993 (Pubitemid 41735517)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 979-993
    • Jackups Jr., R.1    Liang, J.2
  • 21
    • 9644263992 scopus 로고    scopus 로고
    • Membrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched β-structure
    • DOI 10.1074/jbc.M408604200
    • Suzuki H., Kadowaki T., Maeda M., Sasaki H., Nabekura J., Sakaguchi M., and Mihara K. Membrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched beta-structure J. Biol. Chem. 279 2004 50619 50629 (Pubitemid 39577879)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 50619-50629
    • Suzuki, H.1    Kadowaki, T.2    Maeda, M.3    Sasaki, H.4    Nabekura, J.5    Sakaguchi, M.6    Mihara, K.7
  • 22
  • 23
    • 53549105800 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of a yeast mitochondrial preprotein translocase
    • Model K., Meisinger C., and Kuhlbrandt W. Cryo-electron microscopy structure of a yeast mitochondrial preprotein translocase J. Mol. Biol. 383 2008 1049 1057
    • (2008) J. Mol. Biol. , vol.383 , pp. 1049-1057
    • Model, K.1    Meisinger, C.2    Kuhlbrandt, W.3
  • 24
    • 41149113810 scopus 로고    scopus 로고
    • Identification of Tom5 and Tom6 in the preprotein translocase complex of human mitochondrial outer membrane
    • Kato H., and Mihara K. Identification of Tom5 and Tom6 in the preprotein translocase complex of human mitochondrial outer membrane Biochem. Biophys. Res. Commun. 369 2008 958 963
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 958-963
    • Kato, H.1    Mihara, K.2
  • 25
    • 24344508557 scopus 로고    scopus 로고
    • Functions of the small proteins in the TOM complex of Neurospora crasssa
    • DOI 10.1091/mbc.E05-03-0187
    • Sherman E.L., Go N.E., and Nargang F.E. Functions of the small proteins in the TOM complex of Neurospora crasssa Mol. Biol. Cell 16 2005 4172 4182 (Pubitemid 41262887)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4172-4182
    • Sherman, E.L.1    Go, N.E.2    Nargang, F.E.3
  • 26
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • DOI 10.1038/35093038
    • Bayley H., and Cremer P.S. Stochastic sensors inspired by biology Nature 413 2001 226 230 (Pubitemid 32867888)
    • (2001) Nature , vol.413 , Issue.6852 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 27
    • 34547662332 scopus 로고    scopus 로고
    • 8-Barrel Protein Designed from Identical Half Barrels
    • DOI 10.1016/j.jmb.2007.06.036, PII S0022283607008303
    • Seitz T., Bocola M., Claren J., and Sterner R. Stabilisation of a (betaalpha)8-barrel protein designed from identical half barrels J. Mol. Biol. 372 2007 114 129 (Pubitemid 47223222)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.1 , pp. 114-129
    • Seitz, T.1    Bocola, M.2    Claren, J.3    Sterner, R.4
  • 28
    • 64349124286 scopus 로고    scopus 로고
    • High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels
    • Hocker B., Lochner A., Seitz T., Claren J., and Sterner R. High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels Biochemistry 48 2009 1145 1147
    • (2009) Biochemistry , vol.48 , pp. 1145-1147
    • Hocker, B.1    Lochner, A.2    Seitz, T.3    Claren, J.4    Sterner, R.5
  • 29
    • 77957969243 scopus 로고    scopus 로고
    • Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening
    • Seitz T., Thoma R., Schoch G.A., Stihle M., Benz J., and D'Arcy B. Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening J. Mol. Biol. 403 2010 562 577
    • (2010) J. Mol. Biol. , vol.403 , pp. 562-577
    • Seitz, T.1    Thoma, R.2    Schoch, G.A.3    Stihle, M.4    Benz, J.5    D'Arcy, B.6
  • 30
  • 31
    • 72449155682 scopus 로고    scopus 로고
    • Prediction of membrane spanning segments and topology in beta-barrel membrane proteins at better accuracy
    • Ou Y.Y., Chen S.A., and Gromiha M.M. Prediction of membrane spanning segments and topology in beta-barrel membrane proteins at better accuracy J. Comput. Chem. 31 2010 217 223
    • (2010) J. Comput. Chem. , vol.31 , pp. 217-223
    • Ou, Y.Y.1    Chen, S.A.2    Gromiha, M.M.3
  • 32
    • 0036899035 scopus 로고    scopus 로고
    • Experimental and computational studies of determinants of membrane-protein folding
    • DOI 10.1016/S1367-5931(02)00393-9
    • Liang J. Experimental and computational studies of determinants of membrane-protein folding Curr. Opin. Chem. Biol. 6 2002 878 884 (Pubitemid 35449351)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.6 , pp. 878-884
    • Liang, J.1
  • 33
    • 77955466614 scopus 로고    scopus 로고
    • Combinatorial analysis for sequence and spatial motif discovery in short sequence fragments
    • Jackups R. Jr, and Liang J. Combinatorial analysis for sequence and spatial motif discovery in short sequence fragments IEEE/ACM Trans. Comput. Biol. Bioinform. 7 2010 524 536
    • (2010) IEEE/ACM Trans. Comput. Biol. Bioinform. , vol.7 , pp. 524-536
    • Jackups, Jr.R.1    Liang, J.2
  • 34
    • 33749140136 scopus 로고    scopus 로고
    • Sequence Motifs and Antimotifs in β-Barrel Membrane Proteins from a Genome-Wide Analysis: The Ala-Tyr Dichotomy and Chaperone Binding Motifs
    • DOI 10.1016/j.jmb.2006.07.095, PII S0022283606010278
    • Jackups R. Jr, Cheng S., and Liang J. Sequence motifs and antimotifs in beta-barrel membrane proteins from a genome-wide analysis: the Ala-Tyr dichotomy and chaperone binding motifs J. Mol. Biol. 363 2006 611 623 (Pubitemid 44467881)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.2 , pp. 611-623
    • Jackups Jr., R.1    Cheng, S.2    Liang, J.3
  • 35
    • 79960574201 scopus 로고    scopus 로고
    • Functional refolding and characterization of two Tom40 isoforms from human mitochondria
    • F. Mager, D. Gessmann, S. Nussberger, and K. Zeth Functional refolding and characterization of two Tom40 isoforms from human mitochondria J. Membr. Biol. 242 2011 11 21
    • (2011) J. Membr. Biol. , vol.242 , pp. 11-21
    • Mager, F.1    Gessmann, D.2    Nussberger, S.3    Zeth, K.4
  • 36
    • 0347972670 scopus 로고
    • Cloning of cDNA coding for human tissue-type plasminogen activator and its expression in Escherichia coli
    • Harris T.J., Patel T., Marston F.A., Little S., Emtage J.S., and Opdenakker G. Cloning of cDNA coding for human tissue-type plasminogen activator and its expression in Escherichia coli Mol. Biol. Med. 3 1986 279 292
    • (1986) Mol. Biol. Med. , vol.3 , pp. 279-292
    • Harris, T.J.1    Patel, T.2    Marston, F.A.3    Little, S.4    Emtage, J.S.5    Opdenakker, G.6
  • 37
    • 80053339564 scopus 로고
    • DNA cloning: A practical approach
    • Engel J. DNA cloning: a practical approach Acta Biotechnol. 9 1987 254
    • (1987) Acta Biotechnol. , vol.9 , pp. 254
    • Engel, J.1
  • 39
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260 (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 40
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of betaI- and betaII-proteins
    • Sreerama N., and Woody R.W. Structural composition of betaI- and betaII-proteins Protein Sci. 12 2003 384 388
    • (2003) Protein Sci. , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 41
    • 1642546383 scopus 로고    scopus 로고
    • Computation and Analysis of Protein Circular Dichroism Spectra
    • DOI 10.1016/S0076-6879(04)83013-1
    • Sreerama N., and Woody R.W. Computation and analysis of protein circular dichroism spectra Methods Enzymol. 383 2004 318 351 (Pubitemid 38401795)
    • (2004) Methods in Enzymology , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 45
    • 78650223921 scopus 로고    scopus 로고
    • An improved method for measuring the stability of a three-state unfolding protein
    • Zheng X.Y., and Yang B.S. An improved method for measuring the stability of a three-state unfolding protein Chinese Sci. Bull. 55 2010 4120 4124
    • (2010) Chinese Sci. Bull. , vol.55 , pp. 4120-4124
    • Zheng, X.Y.1    Yang, B.S.2
  • 46
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin A.S., Jayasinghe S., and White S.H. How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 285 2000 235 245
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 47
    • 67650489237 scopus 로고    scopus 로고
    • Substrate-induced conformational change of the Escherichia coli membrane insertase YidC
    • Winterfeld S., Imhof N., Roos T., Bar G., Kuhn A., and Gerken U. Substrate-induced conformational change of the Escherichia coli membrane insertase YidC Biochemistry 48 2009 6684 6691
    • (2009) Biochemistry , vol.48 , pp. 6684-6691
    • Winterfeld, S.1    Imhof, N.2    Roos, T.3    Bar, G.4    Kuhn, A.5    Gerken, U.6
  • 48
    • 10244225308 scopus 로고    scopus 로고
    • TMRPres2D: High quality visual representation of transmembrane protein models
    • DOI 10.1093/bioinformatics/bth358
    • Spyropoulos I.C., Liakopoulos T.D., Bagos P.G., and Hamodrakas S.J. TMRPres2D: high quality visual representation of transmembrane protein models Bioinformatics 20 2004 3258 3260 (Pubitemid 39619221)
    • (2004) Bioinformatics , vol.20 , Issue.17 , pp. 3258-3260
    • Spyropoulos, I.C.1    Liakopoulos, T.D.2    Bagos, P.G.3    Hamodrakas, S.J.4
  • 49
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton, Oxford University Press USA
    • Pace C., and Scholtz J. Measuring the conformational stability of a protein T.E. Creighton, Protein Structure. A Practical Approach 1997 Oxford University Press USA 299 321
    • (1997) Protein Structure. A Practical Approach , pp. 299-321
    • Pace, C.1    Scholtz, J.2
  • 51
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 52
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280 (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.