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Volumn 159, Issue 1, 2011, Pages 33-40

Stability, denaturation and refolding of Mycobacterium tuberculosis MfpA, a DNA mimicking protein that confers antibiotic resistance

Author keywords

Antibiotic resistance; CD; Fluorescence; MfpA; Pentapeptide repeat protein; Protein folding

Indexed keywords

BACTERIAL PROTEIN; PROTEIN MFPA; QUINOLINE DERIVED ANTIINFECTIVE AGENT; UNCLASSIFIED DRUG;

EID: 80052311657     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.04.015     Document Type: Conference Paper
Times cited : (7)

References (40)
  • 1
    • 20344367084 scopus 로고    scopus 로고
    • Biochemistry: A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA
    • DOI 10.1126/science.1110699
    • S. Hegde, M. Vetting, S. Roderick, L. Mitchenall, A. Maxwell, H. Takiff, and S. Blanchard A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA Science 308 2005 1480 1483 (Pubitemid 40791304)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1480-1483
    • Hegde, S.S.1    Vetting, M.W.2    Roderick, S.L.3    Mitchenall, L.A.4    Maxwell, A.5    Takiff, H.E.6    Blanchard, J.S.7
  • 3
    • 0031105464 scopus 로고    scopus 로고
    • Gyrase as a drug target
    • A. Maxwell Gyrase as a drug target Trends Microbiol. 5 1997 102 109
    • (1997) Trends Microbiol. , vol.5 , pp. 102-109
    • Maxwell, A.1
  • 5
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • J.C. Wang Cellular roles of DNA topoisomerases: a molecular perspective Nat. Rev. Mol. Cell Biol. 3 2002
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3
    • Wang, J.C.1
  • 6
    • 61349143151 scopus 로고    scopus 로고
    • Solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA
    • S. Khrapunov, H. Cheng, S. Hegde, J. Blanchard, and M. Brenowitz Solution structure and refolding of the Mycobacterium tuberculosis pentapeptide repeat protein MfpA J. Biol. Chem. 283 2008 36290 36299
    • (2008) J. Biol. Chem. , vol.283 , pp. 36290-36299
    • Khrapunov, S.1    Cheng, H.2    Hegde, S.3    Blanchard, J.4    Brenowitz, M.5
  • 7
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C. Dobson Protein misfolding, functional amiloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 8
    • 0032832463 scopus 로고    scopus 로고
    • Isolation inclusion bodies from bacteria
    • G. Georgiu, and P. Valax Isolation inclusion bodies from bacteria Methods Enzymol. 309 1999 48 58
    • (1999) Methods Enzymol. , vol.309 , pp. 48-58
    • Georgiu, G.1    Valax, P.2
  • 9
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 13 1986 266 280 (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 11
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • DOI 10.1126/science.1060438
    • D. Shortle, and M. Ackerman Persistence of native-like topology in a denatured protein in 8 M urea Science 293 2001 487 489 (Pubitemid 32679075)
    • (2001) Science , vol.293 , Issue.5529 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 12
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • O. Ptytsyn Molten globule and protein folding Adv. Protein Chem. 47 1995 83 229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptytsyn, O.1
  • 15
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • J.M. Sanchez-Ruiz Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry Biophys. J. 61 1992 921 935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 16
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • M.R. Eftink The use of fluorescence methods to monitor unfolding transitions in proteins Biophys. J. 66 1994 482 501 (Pubitemid 24058467)
    • (1994) Biophysical Journal , vol.66 , Issue.2 , pp. 482-501
    • Eftink, M.R.1
  • 18
    • 33845428343 scopus 로고    scopus 로고
    • An unfolding story of helical transmembrane proteins
    • DOI 10.1021/bi0620454
    • R. Renthal An unfolding story of helical transmembrane proteins Biochemistry 45 2006 14559 14566 (Pubitemid 44906972)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14559-14566
    • Renthal, R.1
  • 20
    • 0033578401 scopus 로고    scopus 로고
    • Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: Circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor
    • N. Sreerama, M.C. Manning, M.E. Powers, J.X. Zhang, D.P. Goldenberg, and R.W. Woody Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor Biochemistry 38 1999 10814 10822
    • (1999) Biochemistry , vol.38 , pp. 10814-10822
    • Sreerama, N.1    Manning, M.C.2    Powers, M.E.3    Zhang, J.X.4    Goldenberg, D.P.5    Woody, R.W.6
  • 21
    • 1642546383 scopus 로고    scopus 로고
    • Computation and Analysis of Protein Circular Dichroism Spectra
    • DOI 10.1016/S0076-6879(04)83013-1
    • N. Sreerama, and R. Woody 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
  • 23
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • C.N. Pace, and K.L. Shaw Linear extrapolation method of analyzing solvent denaturation curves Proteins 4 2000 1 7
    • (2000) Proteins , vol.4 , pp. 1-7
    • Pace, C.N.1    Shaw, K.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
    • M.M. Santoro, and D.W. Bolen Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants Biochemistry 27 1988 8063 8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 25
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • DOI 10.1021/bi963095j
    • F. Lau, and J. Bowie A method for assessing the stability of a membrane protein Biochemistry 36 1997 5884 5892 (Pubitemid 27214941)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 26
    • 34547558209 scopus 로고    scopus 로고
    • Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system
    • DOI 10.1016/j.bpc.2007.06.005, PII S0301462207001585
    • H.L. Bagger, S.V. Hoffmann, C.C. Fuglsang, and P. Westh Glycoprotein-surfactant interactions: a calorimetric and spectroscopic investigation of the phytase-SDS system Biophys. Chem. 129 2007 251 258 (Pubitemid 47198379)
    • (2007) Biophysical Chemistry , vol.129 , Issue.2-3 , pp. 251-258
    • Bagger, H.L.1    Hoffmann, S.V.2    Fuglsang, C.C.3    Westh, P.4
  • 27
    • 0015207709 scopus 로고
    • Elastase. 11. Optical properties and the effects of sodium dodecyl sulfate
    • L. Visseri, and E.R. Bloutj Elastase. 11. Optical properties and the effects of sodium dodecyl sulfate Biochemistry 10 1971 743 752
    • (1971) Biochemistry , vol.10 , pp. 743-752
    • Visseri, L.1    Bloutj, E.R.2
  • 28
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • DOI 10.1021/bi963095j
    • F.W. Lau, and J.U. Bowie A method for assessing the stability of a membrane protein Biochemistry 36 1997 5884 5892 (Pubitemid 27214941)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 29
    • 33846411081 scopus 로고    scopus 로고
    • Extensive unfolding of the C-LytA choline-binding module by submicellar concentrations of sodium dodecyl sulphate
    • DOI 10.1016/j.febslet.2006.12.042, PII S0014579306015067
    • B. Maestro, and J.M. Sanz Extensive unfolding of the C-LytA choline-binding module by submicellar concentrations of sodium dodecyl sulphate FEBS Lett. 581 2007 375 381 (Pubitemid 46149605)
    • (2007) FEBS Letters , vol.581 , Issue.3 , pp. 375-381
    • Maestro, B.1    Sanz, J.M.2
  • 30
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • I. Kim, W. Xu, and J.C. Reed Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities Nat. Rev. Mol. Cell Biol. 7 2008 1013 1030
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 32
  • 35
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • R. Lumry, and H. Eyring Conformation changes of proteins J. Phys. Chem. 58 1954 110 120
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 36
    • 25444474165 scopus 로고    scopus 로고
    • Using micellar mole fractions to assess membrane protein stability in mixed micelles
    • DOI 10.1016/j.bbamem.2005.08.006, PII S0005273605002580
    • P. Sehgal, J.E. Mogensen, and D.E. Otzen Using micellar mole fractions to assess membrane protein stability in mixed micelles Biochim. Biophys. Acta 1716 2005 59 68 (Pubitemid 41377150)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1716 , Issue.1 , pp. 59-68
    • Sehgal, P.1    Mogensen, J.E.2    Otzen, D.E.3
  • 39
    • 67349104401 scopus 로고    scopus 로고
    • Circular dichroism spectroscopy has intrinsic limitations for protein secondary structure analysis
    • S. Khrapunov Circular dichroism spectroscopy has intrinsic limitations for protein secondary structure analysis Anal. Biochem. 389 2009 174 176
    • (2009) Anal. Biochem. , vol.389 , pp. 174-176
    • Khrapunov, S.1
  • 40
    • 4644285228 scopus 로고    scopus 로고
    • Protein folding in the cell: Reshaping the folding funnel
    • DOI 10.1016/j.tibs.2004.08.008, PII S0968000404002099
    • P.L. Clark Protein folding in the cell: reshaping the folding funnel Trends Biochem. Sci. 29 2004 527 534 (Pubitemid 39265169)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.10 , pp. 527-534
    • Clark, P.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.