메뉴 건너뛰기




Volumn 46, Issue 23, 2007, Pages 6766-6773

An optimized purification and reconstitution method for the MscS channel: Strategies for spectroscopical analysis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASMIC; MECHANOSENSITIVE CHANNEL OF SMALL CONDUCTANCE (MSCS);

EID: 34250214534     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700322k     Document Type: Article
Times cited : (37)

References (47)
  • 1
    • 0001849178 scopus 로고    scopus 로고
    • Channel gate! Tension, leak and disclosure
    • Batiza, A. F., Rayment, I., and Kung, C. (1999) Channel gate! Tension, leak and disclosure, Structure 7, R99-R103.
    • (1999) Structure , vol.7
    • Batiza, A.F.1    Rayment, I.2    Kung, C.3
  • 2
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill, O. P., and Martinac, B. (2001) Molecular basis of mechanotransduction in living cells, Physiol. Rev. 81, 685-740.
    • (2001) Physiol. Rev , vol.81 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 3
    • 0035085703 scopus 로고    scopus 로고
    • Mechanosensitive channels in prokaryotes
    • Martinac, B. (2001) Mechanosensitive channels in prokaryotes, Cell. Physiol. Biochem. 11, 61-76.
    • (2001) Cell. Physiol. Biochem , vol.11 , pp. 61-76
    • Martinac, B.1
  • 4
    • 0037421991 scopus 로고    scopus 로고
    • Molecular mechanisms of mechanosensation: Big lessons from small cells
    • Blount, P. (2003) Molecular mechanisms of mechanosensation: Big lessons from small cells, Neuron 37, 731-734.
    • (2003) Neuron , vol.37 , pp. 731-734
    • Blount, P.1
  • 5
    • 3042853029 scopus 로고    scopus 로고
    • Mechanosensitive ion channels: Molecules of mechanotransduction
    • Martinac, B. (2004) Mechanosensitive ion channels: Molecules of mechanotransduction, J. Cell Sci. 117, 2449-2460.
    • (2004) J. Cell Sci , vol.117 , pp. 2449-2460
    • Martinac, B.1
  • 6
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • Kung, C. (2005) A possible unifying principle for mechanosensation, Nature 436, 647-654.
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 7
    • 33244458728 scopus 로고    scopus 로고
    • Gating prokaryotic mechanosensitive channels
    • Perozo, E. (2006) Gating prokaryotic mechanosensitive channels, Nat. Rev. Mol. Cell Biol. 7, 109-119.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 109-119
    • Perozo, E.1
  • 9
    • 0033578649 scopus 로고    scopus 로고
    • Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel
    • Maingret, F., Patel, A. J., Lesage, F., Lazdunski, M., and Honore, E. (1999) Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel, J. Biol. Chem. 274, 26691-26696.
    • (1999) J. Biol. Chem , vol.274 , pp. 26691-26696
    • Maingret, F.1    Patel, A.J.2    Lesage, F.3    Lazdunski, M.4    Honore, E.5
  • 10
    • 0036307827 scopus 로고    scopus 로고
    • Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure
    • Kellenberger, S., and Schild, L. (2002) Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure, Physiol. Rev. 82, 735-767.
    • (2002) Physiol. Rev , vol.82 , pp. 735-767
    • Kellenberger, S.1    Schild, L.2
  • 11
    • 0041520528 scopus 로고    scopus 로고
    • New TRP channels in hearing and mechanosensation
    • Corey, D. P. (2003) New TRP channels in hearing and mechanosensation, Neuron 39, 585-588.
    • (2003) Neuron , vol.39 , pp. 585-588
    • Corey, D.P.1
  • 12
    • 0029885811 scopus 로고    scopus 로고
    • Multiple mechanosensitive ion channels from Escherichia coli, activated at different thresholds of applied pressure
    • Berrier, C., Besnard, M., Ajouz, B., Coulombe, A., and Ghazi, A. (1996) Multiple mechanosensitive ion channels from Escherichia coli, activated at different thresholds of applied pressure, J. Membr. Biol. 151, 175-187.
    • (1996) J. Membr. Biol , vol.151 , pp. 175-187
    • Berrier, C.1    Besnard, M.2    Ajouz, B.3    Coulombe, A.4    Ghazi, A.5
  • 13
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina, N., Totemeyer, S., Stokes, N. R., Louis, P., Jones, M. A., and Booth, I. R. (1999) Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity, EMBO J. 18, 1730-1737.
    • (1999) EMBO J , vol.18 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 16
    • 0027181625 scopus 로고
    • Two types of mechanosensitive channels in the Escherichia coli cell envelope: Solubilization and functional reconstitution
    • Sukharev, S. I., Martinac, B., Arshavsky, V. Y., and Kung, C. (1993) Two types of mechanosensitive channels in the Escherichia coli cell envelope: Solubilization and functional reconstitution, Biophys. J. 65, 177-183.
    • (1993) Biophys. J , vol.65 , pp. 177-183
    • Sukharev, S.I.1    Martinac, B.2    Arshavsky, V.Y.3    Kung, C.4
  • 17
    • 0032145657 scopus 로고    scopus 로고
    • Voltage-independent adaptation of mechanosensitive channels in Escherichia coli protoplasts
    • Koprowski, P., and Kubalski, A. (1998) Voltage-independent adaptation of mechanosensitive channels in Escherichia coli protoplasts, J. Membr. Biol. 164, 253-262.
    • (1998) J. Membr. Biol , vol.164 , pp. 253-262
    • Koprowski, P.1    Kubalski, A.2
  • 18
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • Perozo, E., Cortes, D. M., Sompornpisut, P., Kloda, A., and Martinac, B. (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels, Nature 418, 942-948.
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 19
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., Spencer, R. H., Lee, A. T., Barclay, M. T., and Rees, D. C. (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel, Science 282, 2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 20
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass, R. B., Strop, P., Barclay, M., and Rees, D. C. (2002) Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel, Science 298, 1582-1587.
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 22
    • 0003074951 scopus 로고    scopus 로고
    • Common evolutionary origins of mechanosensitive ion channels in Archaea, Bacteria and cell-walled Eukarya
    • Kloda, A., and Martinac, B. (2002) Common evolutionary origins of mechanosensitive ion channels in Archaea, Bacteria and cell-walled Eukarya, Archaea 1, 35-44.
    • (2002) Archaea , vol.1 , pp. 35-44
    • Kloda, A.1    Martinac, B.2
  • 23
    • 30044442533 scopus 로고    scopus 로고
    • MscS-like proteins control plastid size and shape in Arabidopsis thaliana
    • Haswell, E. S., and Meyerowitz, E. M. (2006) MscS-like proteins control plastid size and shape in Arabidopsis thaliana, Curr. Biol. 16, 1-11.
    • (2006) Curr. Biol , vol.16 , pp. 1-11
    • Haswell, E.S.1    Meyerowitz, E.M.2
  • 24
    • 0027367442 scopus 로고
    • Calcium channel currents recorded from isolated myocytes of rat basilar artery are stretch sensitive
    • Langton, P. D. (1993) Calcium channel currents recorded from isolated myocytes of rat basilar artery are stretch sensitive, J. Physiol. 471, 1-11.
    • (1993) J. Physiol , vol.471 , pp. 1-11
    • Langton, P.D.1
  • 25
    • 0032715203 scopus 로고    scopus 로고
    • Cholesterol inhibits spontaneous action potentials and calcium currents in guinea pig gallbladder smooth muscle
    • Jennings, L. J., Xu, Q. W., Firth, T. A., Nelson, M. T., and Mawe, G. M. (1999) Cholesterol inhibits spontaneous action potentials and calcium currents in guinea pig gallbladder smooth muscle, Am. J. Physiol. 277, G1017-G1026.
    • (1999) Am. J. Physiol , vol.277
    • Jennings, L.J.1    Xu, Q.W.2    Firth, T.A.3    Nelson, M.T.4    Mawe, G.M.5
  • 26
    • 0036840333 scopus 로고    scopus 로고
    • Mechanosensitivity of N-type calcium channel currents
    • Calabrese, B., Tabarean, I. V., Juranka, P., and Morris, C. E. (2002) Mechanosensitivity of N-type calcium channel currents, Biophys. J. 83, 2560-2574.
    • (2002) Biophys. J , vol.83 , pp. 2560-2574
    • Calabrese, B.1    Tabarean, I.V.2    Juranka, P.3    Morris, C.E.4
  • 27
    • 33744474549 scopus 로고    scopus 로고
    • Membrane stretch slows the concerted step prior to opening in a Kv channel
    • Laitko, U., Juranka, P. F., and Morris, C. E. (2006) Membrane stretch slows the concerted step prior to opening in a Kv channel, J. Gen. Physiol. 127, 687-701.
    • (2006) J. Gen. Physiol , vol.127 , pp. 687-701
    • Laitko, U.1    Juranka, P.F.2    Morris, C.E.3
  • 28
    • 0030745896 scopus 로고    scopus 로고
    • + channel (SKCl): Oligomeric stoichiometry and stability
    • + channel (SKCl): Oligomeric stoichiometry and stability, Biochemistry 36, 10343-10352.
    • (1997) Biochemistry , vol.36 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.2
  • 30
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D. M., Cuello, L. G., and Perozo, E. (2001) Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating, J. Gen. Physiol. 117, 165-180.
    • (2001) J. Gen. Physiol , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 31
    • 0036280794 scopus 로고    scopus 로고
    • Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes
    • Sukharev, S. (2002) Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes, Biophys. J. 83, 290-298.
    • (2002) Biophys. J , vol.83 , pp. 290-298
    • Sukharev, S.1
  • 32
    • 33846828514 scopus 로고    scopus 로고
    • Ion Conduction through MscS as Determined by Electrophysiology and Simulation
    • Sotomayor, M., Vasquez, V., Perozo, E., and Schulten, K. (2007) Ion Conduction through MscS as Determined by Electrophysiology and Simulation, Biophys. J. 92, 886-902.
    • (2007) Biophys. J , vol.92 , pp. 886-902
    • Sotomayor, M.1    Vasquez, V.2    Perozo, E.3    Schulten, K.4
  • 34
  • 35
    • 0042858140 scopus 로고    scopus 로고
    • The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants
    • Miller, S., Edwards, M. D., Ozdemir, C., and Booth, I. R. (2003) The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants, J. Biol. Chem. 278, 32246-32250.
    • (2003) J. Biol. Chem , vol.278 , pp. 32246-32250
    • Miller, S.1    Edwards, M.D.2    Ozdemir, C.3    Booth, I.R.4
  • 36
    • 4143072661 scopus 로고    scopus 로고
    • The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity
    • Schumann, U., Edwards, M. D., Li, C., and Booth, I. R. (2004) The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity, FEBS Lett. 572, 233-237.
    • (2004) FEBS Lett , vol.572 , pp. 233-237
    • Schumann, U.1    Edwards, M.D.2    Li, C.3    Booth, I.R.4
  • 37
    • 23644444909 scopus 로고    scopus 로고
    • Refractive index-based determination of detergent concentration and its application to the study of membrane proteins
    • Strop, P., and Brunger, A. T. (2005) Refractive index-based determination of detergent concentration and its application to the study of membrane proteins, Protein Sci. 14, 2207-2211.
    • (2005) Protein Sci , vol.14 , pp. 2207-2211
    • Strop, P.1    Brunger, A.T.2
  • 38
    • 13544268703 scopus 로고    scopus 로고
    • The "dashpot" mechanism of stretch-dependent gating in MscS
    • Akitake, B., Anishkin, A., and Sukharev, S. (2005) The "dashpot" mechanism of stretch-dependent gating in MscS, J. Gen. Physiol. 125, 143-154.
    • (2005) J. Gen. Physiol , vol.125 , pp. 143-154
    • Akitake, B.1    Anishkin, A.2    Sukharev, S.3
  • 39
    • 24944476565 scopus 로고    scopus 로고
    • The influence of a membrane environment on the structure and stability of a prokaryotic potassium channel, KcsA
    • Encinar, J. A., Molina, M. L., Poveda, J. A., Barrera, F. N., Renart, M. L., Fernandez, A. M., and Gonzalez-Ros, J. M. (2005) The influence of a membrane environment on the structure and stability of a prokaryotic potassium channel, KcsA, FEBS Lett. 579, 5199-5204.
    • (2005) FEBS Lett , vol.579 , pp. 5199-5204
    • Encinar, J.A.1    Molina, M.L.2    Poveda, J.A.3    Barrera, F.N.4    Renart, M.L.5    Fernandez, A.M.6    Gonzalez-Ros, J.M.7
  • 40
    • 0027016905 scopus 로고
    • Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin
    • Farahbakhsh, Z. T., Altenbach, C., and Hubbell, W. L. (1992) Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin, Photochem. Photobiol. 56, 1019-1033.
    • (1992) Photochem. Photobiol , vol.56 , pp. 1019-1033
    • Farahbakhsh, Z.T.1    Altenbach, C.2    Hubbell, W.L.3
  • 41
    • 0028243155 scopus 로고
    • Binding and state of aggregation of spin-labeled cecropin AD in phospholipid bilayers: Effects of surface charge and fatty acyl chain length
    • McHaourab, H. S., Hyde, J. S., and Feix, J. B. (1994) Binding and state of aggregation of spin-labeled cecropin AD in phospholipid bilayers: Effects of surface charge and fatty acyl chain length, Biochemists 33, 6691-6699.
    • (1994) Biochemists , vol.33 , pp. 6691-6699
    • McHaourab, H.S.1    Hyde, J.S.2    Feix, J.B.3
  • 42
    • 0034884665 scopus 로고    scopus 로고
    • Site-directed spin-labeling analysis of reconstituted Mscl in the closed state
    • Perozo, E., Kloda, A., Cortes, D. M., and Martinac, B. (2001) Site-directed spin-labeling analysis of reconstituted Mscl in the closed state, J. Gen. Physiol. 118, 193-206.
    • (2001) J. Gen. Physiol , vol.118 , pp. 193-206
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 43
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., Kloda, A., Cortes, D. M., and Martinac, B. (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating, Nat. Struct. Biol. 9, 696-703.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 45
    • 34147178808 scopus 로고    scopus 로고
    • Akitake, B., Spelbrink, R. E., Anishkin, A., Killian, J. A., de Kruijff, B., and Sukharev, S. (2007) 2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensitive channel MscS, Biophys. J. (in press).
    • Akitake, B., Spelbrink, R. E., Anishkin, A., Killian, J. A., de Kruijff, B., and Sukharev, S. (2007) 2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensitive channel MscS, Biophys. J. (in press).
  • 47
    • 0025114667 scopus 로고
    • Mechanosensitive ion channels of E. coli activated by amphipaths
    • Martinac, B., Adler, J., and Kung, C. (1990) Mechanosensitive ion channels of E. coli activated by amphipaths, Nature 348, 261-263.
    • (1990) Nature , vol.348 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.