메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages

Structural Characterization of the Complex of SecB and Metallothionein-Labeled proOmpA by Cryo-Electron Microscopy

Author keywords

[No Author keywords available]

Indexed keywords

METALLOTHIONEIN; PROOMPA PREPROTEIN; PROTEIN PRECURSOR; PROTEIN SECB; UNCLASSIFIED DRUG;

EID: 84867121268     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047015     Document Type: Article
Times cited : (5)

References (45)
  • 1
    • 0029128898 scopus 로고
    • Diffusion-Limited Interaction Between Unfolded Polypeptides and the Escherichia-Coli Chaperone SecB
    • Fekkes P, denBlaauwen T, Driessen AJM, (1995) Diffusion-Limited Interaction Between Unfolded Polypeptides and the Escherichia-Coli Chaperone SecB. Biochemistry 34: 10078-10085.
    • (1995) Biochemistry , vol.34 , pp. 10078-10085
    • Fekkes, P.1    denBlaauwen, T.2    Driessen, A.J.M.3
  • 3
    • 69249101589 scopus 로고    scopus 로고
    • Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands
    • Lilly AA, Crane JM, Randall LL, (2009) Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Sci 18: 1860-1868.
    • (2009) Protein Sci , vol.18 , pp. 1860-1868
    • Lilly, A.A.1    Crane, J.M.2    Randall, L.L.3
  • 4
    • 0031863439 scopus 로고    scopus 로고
    • Calorimetric analyses of the interaction between SecB and its ligands
    • Randall LL, Topping TB, Suciu D, Hardy SJS, (1998) Calorimetric analyses of the interaction between SecB and its ligands. Protein Sci 7: 1195-1200.
    • (1998) Protein Sci , vol.7 , pp. 1195-1200
    • Randall, L.L.1    Topping, T.B.2    Suciu, D.3    Hardy, S.J.S.4
  • 5
    • 0028831186 scopus 로고
    • High Selectivity with Low Specificity - How SecB Has Solved the Paradox of Chaperone Binding
    • Randall LL, Hardy SJS, (1995) High Selectivity with Low Specificity- How SecB Has Solved the Paradox of Chaperone Binding. Trends Biochem Sci 20: 65-70.
    • (1995) Trends Biochem Sci , vol.20 , pp. 65-70
    • Randall, L.L.1    Hardy, S.J.S.2
  • 6
    • 0026025966 scopus 로고
    • A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB
    • Hardy SJS, Randall LL, (1991) A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB. Science 251: 439-443.
    • (1991) Science , vol.251 , pp. 439-443
    • Hardy, S.J.S.1    Randall, L.L.2
  • 7
    • 0028875765 scopus 로고
    • Mapping of the Binding Frame for the Chaperone SecB Within A Natural Ligand, Galactose-Binding Protein
    • Khisty VJ, Munske GR, Randall LL, (1995) Mapping of the Binding Frame for the Chaperone SecB Within A Natural Ligand, Galactose-Binding Protein. J Biol Chem 270: 25920-25927.
    • (1995) J Biol Chem , vol.270 , pp. 25920-25927
    • Khisty, V.J.1    Munske, G.R.2    Randall, L.L.3
  • 8
    • 33750096803 scopus 로고    scopus 로고
    • Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein
    • Smith VF, Hardy SJS, Randall LL, (1997) Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein. FASEB J 11: A903-A903.
    • (1997) FASEB J , vol.11
    • Smith, V.F.1    Hardy, S.J.S.2    Randall, L.L.3
  • 9
    • 0028214003 scopus 로고
    • Determination of the Binding Frame Within A Physiological Ligand for the Chaperone SecB
    • Topping TB, Randall LL, (1994) Determination of the Binding Frame Within A Physiological Ligand for the Chaperone SecB. Protein Sci 3: 730-736.
    • (1994) Protein Sci , vol.3 , pp. 730-736
    • Topping, T.B.1    Randall, L.L.2
  • 10
    • 0026577035 scopus 로고
    • Biogenesis of Outer-Membrane Protein Phoe of Escherichia-Coli - Evidence for Multiple SecB-Binding Sites in the Mature Portion of the Phoe Protein
    • deCock H, Overeem W, Tommassen J, (1992) Biogenesis of Outer-Membrane Protein Phoe of Escherichia-Coli- Evidence for Multiple SecB-Binding Sites in the Mature Portion of the Phoe Protein. J Mol Biol 224: 369-379.
    • (1992) J Mol Biol , vol.224 , pp. 369-379
    • deCock, H.1    Overeem, W.2    Tommassen, J.3
  • 11
    • 0031656854 scopus 로고    scopus 로고
    • Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA
    • Fekkes P, de Wit JG, van der Wolk JPW, Kimsey HH, Kumamoto CA, et al. (1998) Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol Microbiol 29: 1179-1190.
    • (1998) Mol Microbiol , vol.29 , pp. 1179-1190
    • Fekkes, P.1    de Wit, J.G.2    van der Wolk, J.P.W.3    Kimsey, H.H.4    Kumamoto, C.A.5
  • 12
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • Fekkes P, van der Does C, Driessen AJM, (1997) The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J 16: 6105-6113.
    • (1997) EMBO J , vol.16 , pp. 6105-6113
    • Fekkes, P.1    van der Does, C.2    Driessen, A.J.M.3
  • 13
    • 0025036708 scopus 로고
    • The Binding Cascade of SecB to SecA to SecY/E Mediates Preprotein Targeting to the Escherichia-Coli Plasma-Membrane
    • Hartl FU, Lecker S, Schiebel E, Hendrick JP, Wickner W, (1990) The Binding Cascade of SecB to SecA to SecY/E Mediates Preprotein Targeting to the Escherichia-Coli Plasma-Membrane. Cell 63: 269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 14
    • 36749011854 scopus 로고    scopus 로고
    • Direct observation of chaperone-induced changes in a protein folding pathway
    • Bechtluft P, van Leeuwen RGH, Tyreman M, Tomkiewicz D, Nouwen N, et al. (2007) Direct observation of chaperone-induced changes in a protein folding pathway. Science 318: 1458-1461.
    • (2007) Science , vol.318 , pp. 1458-1461
    • Bechtluft, P.1    van Leeuwen, R.G.H.2    Tyreman, M.3    Tomkiewicz, D.4    Nouwen, N.5
  • 15
    • 0030798169 scopus 로고    scopus 로고
    • Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands
    • Topping TB, Randall LL, (1997) Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. J Biol Chem 272: 19314-19318.
    • (1997) J Biol Chem , vol.272 , pp. 19314-19318
    • Topping, T.B.1    Randall, L.L.2
  • 17
    • 39649107959 scopus 로고    scopus 로고
    • Kinetics and energetics of the translocation of maltose binding protein folding mutants
    • Tomikiewicz D, Nouwen N, Driessen AJM, (2008) Kinetics and energetics of the translocation of maltose binding protein folding mutants. J Mol Biol 377: 83-90.
    • (2008) J Mol Biol , vol.377 , pp. 83-90
    • Tomikiewicz, D.1    Nouwen, N.2    Driessen, A.J.M.3
  • 19
    • 77949486176 scopus 로고    scopus 로고
    • The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB
    • Tang Y, Pan XJ, Tai PC, Sui SF, (2010) The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB. Biochem Biophys Res Commun 393: 698-702.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 698-702
    • Tang, Y.1    Pan, X.J.2    Tai, P.C.3    Sui, S.F.4
  • 20
    • 0023946435 scopus 로고
    • Efficient Invitro Translocation Into Escherichia-Coli Membrane-Vesicles of A Protein Carrying An Uncleavable Signal Peptide - Characterization of the Translocation Process
    • Yamane K, Matsuyama S, Mizushima S, (1988) Efficient Invitro Translocation Into Escherichia-Coli Membrane-Vesicles of A Protein Carrying An Uncleavable Signal Peptide- Characterization of the Translocation Process. J Biol Chem 263: 5368-5372.
    • (1988) J Biol Chem , vol.263 , pp. 5368-5372
    • Yamane, K.1    Matsuyama, S.2    Mizushima, S.3
  • 21
    • 84855859923 scopus 로고    scopus 로고
    • Metallothionein as a clonable high-density marker for cryo-electron microscopy
    • Bouchet-Marquis C, Pagratis M, Kirmse R, Hoenger A, (2012) Metallothionein as a clonable high-density marker for cryo-electron microscopy. J Struct Biol 177: 119-127.
    • (2012) J Struct Biol , vol.177 , pp. 119-127
    • Bouchet-Marquis, C.1    Pagratis, M.2    Kirmse, R.3    Hoenger, A.4
  • 22
    • 59149094180 scopus 로고    scopus 로고
    • Visualization of proteins in intact cells with a clonable tag for electron microscopy
    • Diestra E, Fontana J, Guichard P, Marco S, Risco C, (2009) Visualization of proteins in intact cells with a clonable tag for electron microscopy. J Struct Biol 165: 157-168.
    • (2009) J Struct Biol , vol.165 , pp. 157-168
    • Diestra, E.1    Fontana, J.2    Guichard, P.3    Marco, S.4    Risco, C.5
  • 23
    • 34548627873 scopus 로고    scopus 로고
    • Concatenated metallothionein as a clonable gold label for electron microscopy
    • Mercogliano CP, DeRosier DJ, (2007) Concatenated metallothionein as a clonable gold label for electron microscopy. J Struct Biol 160: 70-82.
    • (2007) J Struct Biol , vol.160 , pp. 70-82
    • Mercogliano, C.P.1    DeRosier, D.J.2
  • 24
    • 35948943072 scopus 로고    scopus 로고
    • A genetically encoded metallothionein tag enabling efficient protein detection by electron microscopy
    • Nishino Y, Yasunaga T, Miyazawa A, (2007) A genetically encoded metallothionein tag enabling efficient protein detection by electron microscopy. J Electron Microsc 56: 93-101.
    • (2007) J Electron Microsc , vol.56 , pp. 93-101
    • Nishino, Y.1    Yasunaga, T.2    Miyazawa, A.3
  • 25
    • 84864976128 scopus 로고    scopus 로고
    • Enhanced detection efficiency of genetically encoded tag allows the visualization of monomeric proteins by electron microscopy
    • Fukunaga Y, Higashihara A, Nishino Y, Yasunaga T, Jin M, et al. (2012) Enhanced detection efficiency of genetically encoded tag allows the visualization of monomeric proteins by electron microscopy. J Electron Microsc 101093/jmicro/dfs043.
    • (2012) J Electron Microsc 101093/jmicro/dfs043.
    • Fukunaga, Y.1    Higashihara, A.2    Nishino, Y.3    Yasunaga, T.4    Jin, M.5
  • 27
    • 0029973546 scopus 로고    scopus 로고
    • A significant fraction of functional SecA is permanently embedded in the membrane - SecA cycling on and off the membrane is not essential during protein translocation
    • Chen XC, Xu HD, Tai PC, (1996) A significant fraction of functional SecA is permanently embedded in the membrane- SecA cycling on and off the membrane is not essential during protein translocation. J Biol Chem 271: 29698-29706.
    • (1996) J Biol Chem , vol.271 , pp. 29698-29706
    • Chen, X.C.1    Xu, H.D.2    Tai, P.C.3
  • 29
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • Nishiyama KI, Suzuki T, Tokuda H, (1996) Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell 85: 71-81.
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.I.1    Suzuki, T.2    Tokuda, H.3
  • 30
    • 0026601975 scopus 로고
    • A Streptavidin Metallothionein Chimera That Allows Specific Labeling of Biological-Materials with Many Different Heavy-Metal Ions
    • Sano T, Glazer AN, Cantor CR, (1992) A Streptavidin Metallothionein Chimera That Allows Specific Labeling of Biological-Materials with Many Different Heavy-Metal Ions. Proc Natl Acad Sci U S A 89: 1534-1538.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1534-1538
    • Sano, T.1    Glazer, A.N.2    Cantor, C.R.3
  • 31
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116: 190-199.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W, (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 34
    • 80855132610 scopus 로고    scopus 로고
    • Tilt-Pair Analysis of Images from a Range of Different Specimens in Single-Particle Electron Cryomicroscopy
    • Henderson R, Chen SX, Chen JZ, Grigorieff N, Passmore LA, et al. (2011) Tilt-Pair Analysis of Images from a Range of Different Specimens in Single-Particle Electron Cryomicroscopy. J Mol Biol 413: 1028-1046.
    • (2011) J Mol Biol , vol.413 , pp. 1028-1046
    • Henderson, R.1    Chen, S.X.2    Chen, J.Z.3    Grigorieff, N.4    Passmore, L.A.5
  • 35
    • 0019413905 scopus 로고
    • Escherichia-Coli Mutant Pleiotropically Defective in the Export of Secreted Proteins
    • Oliver DB, Beckwith J, (1981) Escherichia-Coli Mutant Pleiotropically Defective in the Export of Secreted Proteins. Cell 25: 765-772.
    • (1981) Cell , vol.25 , pp. 765-772
    • Oliver, D.B.1    Beckwith, J.2
  • 36
    • 0034161573 scopus 로고    scopus 로고
    • SecYEG assembles into a tetramer to form the active protein translocation channel
    • Manting EH, van der Does C, Remigy H, Engel A, Driessen AJM, (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J 19: 852-861.
    • (2000) EMBO J , vol.19 , pp. 852-861
    • Manting, E.H.1    van der Does, C.2    Remigy, H.3    Engel, A.4    Driessen, A.J.M.5
  • 37
    • 78649543432 scopus 로고    scopus 로고
    • Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimmer
    • Tang Y, Pan XJ, Tai PC, Sui SF, (2010) Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimmer. Sci China Life Sci 53: 1049-1056.
    • (2010) Sci China Life Sci , vol.53 , pp. 1049-1056
    • Tang, Y.1    Pan, X.J.2    Tai, P.C.3    Sui, S.F.4
  • 38
    • 0026073817 scopus 로고
    • Delta-Mu-H+ and Atp Function at Different Steps of the Catalytic Cycle of Preprotein Translocase
    • Schiebel E, Driessen AJM, Hartl FU, Wickner W, (1991) Delta-Mu-H+ and Atp Function at Different Steps of the Catalytic Cycle of Preprotein Translocase. Cell 64: 927-939.
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.M.2    Hartl, F.U.3    Wickner, W.4
  • 39
    • 0025005885 scopus 로고
    • Translocation of Proompa Possessing An Intramolecular Disulfide Bridge Into Membrane-Vesicles of Escherichia-Coli - Effect of Membrane Energization
    • Tani K, Tokuda H, Mizushima S, (1990) Translocation of Proompa Possessing An Intramolecular Disulfide Bridge Into Membrane-Vesicles of Escherichia-Coli- Effect of Membrane Energization. J Biol Chem 265: 17341-17347.
    • (1990) J Biol Chem , vol.265 , pp. 17341-17347
    • Tani, K.1    Tokuda, H.2    Mizushima, S.3
  • 40
    • 0025370548 scopus 로고
    • Proompa Contains Secondary and Tertiary Structure Prior to Translocation and Is Shielded from Aggregation by Association with SecB Protein
    • Lecker SH, Driessen AJM, Wickner W, (1990) Proompa Contains Secondary and Tertiary Structure Prior to Translocation and Is Shielded from Aggregation by Association with SecB Protein. EMBO J 9: 2309-2314.
    • (1990) EMBO J , vol.9 , pp. 2309-2314
    • Lecker, S.H.1    Driessen, A.J.M.2    Wickner, W.3
  • 41
    • 0032514646 scopus 로고    scopus 로고
    • SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state
    • Panse G, Udgaonkar B, (1998) Varadarajan (1998) SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state. Biochemistry 37: 14477-14483.
    • (1998) Biochemistry , vol.37 , pp. 14477-14483
    • Panse, G.1    Udgaonkar, B.2
  • 42
    • 33748795820 scopus 로고    scopus 로고
    • Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling
    • Crane M, Suo Y, Lilly A, Mao CF, Hubbell WL, et al. (2006) Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. J Mol Biol 363: 63-74.
    • (2006) J Mol Biol , vol.363 , pp. 63-74
    • Crane, M.1    Suo, Y.2    Lilly, A.3    Mao, C.F.4    Hubbell, W.L.5
  • 43
    • 0031734169 scopus 로고    scopus 로고
    • The interaction between the chaperone SecB and its ligands: Evidence for multiple subsites for binding
    • Randall LL, Hrdy SJS, Topping TB, Smith VF, Bruce JE, et al. (1998) The interaction between the chaperone SecB and its ligands: Evidence for multiple subsites for binding. Protein Sci 7: 2384-2390.
    • (1998) Protein Sci , vol.7 , pp. 2384-2390
    • Randall, L.L.1    Hrdy, S.J.S.2    Topping, T.B.3    Smith, V.F.4    Bruce, J.E.5
  • 44
    • 16244410498 scopus 로고    scopus 로고
    • Asymmetric binding between SecA and SecB two symmetric proteins: Implications for function in export
    • Randall LL, Crane JM, Lilly AA, Liu GP, Mao CF, et al. (2005) Asymmetric binding between SecA and SecB two symmetric proteins: Implications for function in export. J Mol Biol 348: 479-489.
    • (2005) J Mol Biol , vol.348 , pp. 479-489
    • Randall, L.L.1    Crane, J.M.2    Lilly, A.A.3    Liu, G.P.4    Mao, C.F.5
  • 45
    • 79551533114 scopus 로고    scopus 로고
    • Dimeric SecA Couples the Preprotein Translocation in an Asymmetric Manner
    • Tang Y, Pan XJ, Chen Y, Tai PC, Sui SF, (2011) Dimeric SecA Couples the Preprotein Translocation in an Asymmetric Manner. Plos One 6: e16498.
    • (2011) Plos One , vol.6
    • Tang, Y.1    Pan, X.J.2    Chen, Y.3    Tai, P.C.4    Sui, S.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.