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Volumn 581, Issue 18, 2007, Pages 3371-3376

Urea denaturation of α-hemolysin pore inserted in planar lipid bilayer detected by single nanopore recording: Loss of structural asymmetry

Author keywords

Hemolysin; Current asymmetry; Pore denaturation; Pore forming toxins; Protein denaturation

Indexed keywords

ALPHA HEMOLYSIN; HEMOLYSIN; MONOMER; UNCLASSIFIED DRUG; UREA;

EID: 34447280420     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.06.036     Document Type: Article
Times cited : (38)

References (36)
  • 2
    • 0037427958 scopus 로고    scopus 로고
    • [beta]-Barrel membrane protein folding and structure viewed through the lens of [alpha]-hemolysin
    • Montoya M., and Gouaux E. [beta]-Barrel membrane protein folding and structure viewed through the lens of [alpha]-hemolysin. Biochim. Biophys. Acta (BBA) - Biomembr. 1609 (2003) 19-27
    • (2003) Biochim. Biophys. Acta (BBA) - Biomembr. , vol.1609 , pp. 19-27
    • Montoya, M.1    Gouaux, E.2
  • 3
    • 0031877366 scopus 로고    scopus 로고
    • alpha-Hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channel-forming toxins
    • Gouaux E. alpha-Hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channel-forming toxins. J. Struct. Biol. 121 (1998) 110-122
    • (1998) J. Struct. Biol. , vol.121 , pp. 110-122
    • Gouaux, E.1
  • 4
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., and Gouaux J.E. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274 (1996) 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 5
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina G. Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90 (1986) 177-190
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 6
    • 0030710585 scopus 로고    scopus 로고
    • The charge state of an ion channel controls neutral polymer entry into its pore
    • Bezrukov S.M., and Kasianowicz J.J. The charge state of an ion channel controls neutral polymer entry into its pore. Eur. Biophys. J. 26 (1997) 471-476
    • (1997) Eur. Biophys. J. , vol.26 , pp. 471-476
    • Bezrukov, S.M.1    Kasianowicz, J.J.2
  • 7
    • 0242301631 scopus 로고    scopus 로고
    • Electrostatic influence on ion transport through the aHL channel
    • Misakian M., and Kasianowicz J.J. Electrostatic influence on ion transport through the aHL channel. J. Membr. Biol. 195 (2003) 137-146
    • (2003) J. Membr. Biol. , vol.195 , pp. 137-146
    • Misakian, M.1    Kasianowicz, J.J.2
  • 8
    • 16244372752 scopus 로고    scopus 로고
    • Single protein pores containing molecular adapters at high temperatures
    • Kang X.F., Gu L.Q., Cheley S., and Bayley H. Single protein pores containing molecular adapters at high temperatures. Angew. Chem., Int. Ed. Engl. 44 (2005) 1495-1499
    • (2005) Angew. Chem., Int. Ed. Engl. , vol.44 , pp. 1495-1499
    • Kang, X.F.1    Gu, L.Q.2    Cheley, S.3    Bayley, H.4
  • 9
    • 33845196984 scopus 로고    scopus 로고
    • Temperature-responsive protein pores
    • Jung Y., Bayley H., and Movileanu L. Temperature-responsive protein pores. J. Am. Chem. Soc. 128 (2006) 15332-15340
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15332-15340
    • Jung, Y.1    Bayley, H.2    Movileanu, L.3
  • 10
    • 22244445788 scopus 로고    scopus 로고
    • Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map
    • Aksimentiev A., and Schulten K. Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map. Biophys. J. 88 (2005) 3745-3761
    • (2005) Biophys. J. , vol.88 , pp. 3745-3761
    • Aksimentiev, A.1    Schulten, K.2
  • 11
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz J.J., Brandin E., Branton D., and Deamer D.W. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA 93 (1996) 13770-13773
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 12
    • 0032762996 scopus 로고    scopus 로고
    • Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules
    • Akeson M., Branton D., Kasianowicz J.J., Brandin E., and Deamer D.W. Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules. Biophys. J. 77 (1999) 3227-3233
    • (1999) Biophys. J. , vol.77 , pp. 3227-3233
    • Akeson, M.1    Branton, D.2    Kasianowicz, J.J.3    Brandin, E.4    Deamer, D.W.5
  • 13
    • 0030384264 scopus 로고    scopus 로고
    • Dynamics and free energy of polymers partitioning into a nanoscale pore
    • Bezrukov S.M., Vodyanoy I., Brutyan R.A., and Kasianowicz J.J. Dynamics and free energy of polymers partitioning into a nanoscale pore. Macromolecules 29 (1996) 8517-8522
    • (1996) Macromolecules , vol.29 , pp. 8517-8522
    • Bezrukov, S.M.1    Vodyanoy, I.2    Brutyan, R.A.3    Kasianowicz, J.J.4
  • 14
    • 34447256823 scopus 로고    scopus 로고
    • Oukhaled, G., Amiel, C., Bacri, L., Raphael, E., Sikorav, J.L. and Auvray, L. Transport of Single Neutral and Charged Macromolecules through Proteinic Nanopores. Paris, 4-9 july 2004. In: Proceedings of the 40th International IUPAC Symposium on Macromolecules. e-Polymers 2005, No. E_002, L1188.
  • 16
    • 33746590221 scopus 로고    scopus 로고
    • Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores
    • Stefureac R., Long Y.T., Kraatz H.B., Howard P., and Lee J.S. Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores. Biochemistry 45 (2006) 9172-9179
    • (2006) Biochemistry , vol.45 , pp. 9172-9179
    • Stefureac, R.1    Long, Y.T.2    Kraatz, H.B.3    Howard, P.4    Lee, J.S.5
  • 18
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley H., and Cremer P.S. Stochastic sensors inspired by biology. Nature 413 (2001) 226-230
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 19
    • 14844318136 scopus 로고    scopus 로고
    • Nanopore unzipping of individual DNA hairpin molecules
    • Mathe J., Visram H., Viasnoff V., Rabin Y., and Meller A. Nanopore unzipping of individual DNA hairpin molecules. Biophys. J. 87 (2004) 3205-3212
    • (2004) Biophys. J. , vol.87 , pp. 3205-3212
    • Mathe, J.1    Visram, H.2    Viasnoff, V.3    Rabin, Y.4    Meller, A.5
  • 21
    • 0032832241 scopus 로고    scopus 로고
    • A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus
    • Bortoleto R.K., and Ward R.J. A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus. FEBS Lett. 459 (1999) 438-442
    • (1999) FEBS Lett. , vol.459 , pp. 438-442
    • Bortoleto, R.K.1    Ward, R.J.2
  • 22
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal M., and Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA 69 (1972) 3561-3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 24
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: from structure to function
    • Parker M.W., and Feil S.C. Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88 (2005) 91-142
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 25
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley S.J., and Saibil H.R. The mechanism of pore formation by bacterial toxins. Curr. Opin. Struct. Biol. 16 (2006) 230-236
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 26
    • 0141866851 scopus 로고    scopus 로고
    • Unfolding of Vibrio cholerae hemolysin induces oligomerization of the toxin monomer
    • Chattopadhyay K., and Banerjee K.K. Unfolding of Vibrio cholerae hemolysin induces oligomerization of the toxin monomer. J. Biol. Chem. 278 (2003) 38470-38475
    • (2003) J. Biol. Chem. , vol.278 , pp. 38470-38475
    • Chattopadhyay, K.1    Banerjee, K.K.2
  • 28
    • 1942455221 scopus 로고    scopus 로고
    • Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes
    • Micelli S., Meleleo D., Picciarelli V., and Gallucci E. Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes. Biophys. J. 86 (2004) 2231-2237
    • (2004) Biophys. J. , vol.86 , pp. 2231-2237
    • Micelli, S.1    Meleleo, D.2    Picciarelli, V.3    Gallucci, E.4
  • 29
    • 0029841640 scopus 로고    scopus 로고
    • Self-catalyzed insertion of proteins into phospholipid membranes
    • Xu X., and Colombini M. Self-catalyzed insertion of proteins into phospholipid membranes. J. Biol. Chem. 271 (1996) 23675-23682
    • (1996) J. Biol. Chem. , vol.271 , pp. 23675-23682
    • Xu, X.1    Colombini, M.2
  • 30
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti C.A., and Remeta D.P. Energetics of membrane protein folding and stability. Arch. Biochem. Biophys. 453 (2006) 32-53
    • (2006) Arch. Biochem. Biophys. , vol.453 , pp. 32-53
    • Minetti, C.A.1    Remeta, D.P.2
  • 31
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White S.H., and Wimley W.C. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta 1376 (1998) 339-352
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 32
    • 33748746162 scopus 로고    scopus 로고
    • Formation of soluble oligomers and amyloid fibrils with physical properties of the scrapie isoform of the prion protein from the C-terminal domain of recombinant murine prion protein mPrP-(121-231)
    • Martins S.M., Frosoni D.J., Martinez A.M., De Felice F.G., and Ferreira S.T. Formation of soluble oligomers and amyloid fibrils with physical properties of the scrapie isoform of the prion protein from the C-terminal domain of recombinant murine prion protein mPrP-(121-231). J. Biol. Chem. 281 (2006) 26121-26128
    • (2006) J. Biol. Chem. , vol.281 , pp. 26121-26128
    • Martins, S.M.1    Frosoni, D.J.2    Martinez, A.M.3    De Felice, F.G.4    Ferreira, S.T.5
  • 34
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology
    • Lin H., Bhatia R., and Lal R. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 15 (2001) 2433-2444
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 35
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel H.A., and Lansbury Jr. P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?. Q. Rev. Biophys. 39 (2006) 167-201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2


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