메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Real Time Observation of Single Membrane Protein Insertion Events by the Escherichia coli Insertase YidC

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COAT PROTEIN; MEMBRANE PROTEIN; PF3 PROTEIN; UNCLASSIFIED DRUG; YIDC PROTEIN;

EID: 84875118916     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0059023     Document Type: Article
Times cited : (31)

References (27)
  • 1
    • 0035899986 scopus 로고    scopus 로고
    • Fluorescence energy transfer shows a close helix-helix distance in the transmembrane M13 procoat protein
    • Eisenhawer M, Cattarinussi S, Kuhn A, Vogel H, (2001) Fluorescence energy transfer shows a close helix-helix distance in the transmembrane M13 procoat protein. Biochem 40: 12321-12328.
    • (2001) Biochem , vol.40 , pp. 12321-12328
    • Eisenhawer, M.1    Cattarinussi, S.2    Kuhn, A.3    Vogel, H.4
  • 2
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial membrane proteins
    • Dalbey R, Wang P, Kuhn A, (2011) Assembly of bacterial membrane proteins. Ann Rev Biochem 80: 161-187.
    • (2011) Ann Rev Biochem , vol.80 , pp. 161-187
    • Dalbey, R.1    Wang, P.2    Kuhn, A.3
  • 3
    • 34047151280 scopus 로고    scopus 로고
    • YidC as an essential and multifunctional component in membrane protein assembly
    • Kiefer D, Kuhn A, (2007) YidC as an essential and multifunctional component in membrane protein assembly. Int Rev Cytol 259: 113-138.
    • (2007) Int Rev Cytol , vol.259 , pp. 113-138
    • Kiefer, D.1    Kuhn, A.2
  • 4
    • 33747346787 scopus 로고    scopus 로고
    • The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast
    • Gaisne M, Bonnefoy N, (2006) The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast. FEMS Yeast Res 6: 869-882.
    • (2006) FEMS Yeast Res , vol.6 , pp. 869-882
    • Gaisne, M.1    Bonnefoy, N.2
  • 5
    • 71249147710 scopus 로고    scopus 로고
    • Alb4 of Arabidopsis promotes assembly and stabilisation of a none chlorophyll-binding photosynthetic complex, the CF1CF0-ATP synthase
    • Benz M, Bals T, Gügel IL, Piotrowski M, Kuhn A, et al. (2010) Alb4 of Arabidopsis promotes assembly and stabilisation of a none chlorophyll-binding photosynthetic complex, the CF1CF0-ATP synthase. Mol Plant 2: 1410-1424.
    • (2010) Mol Plant , vol.2 , pp. 1410-1424
    • Benz, M.1    Bals, T.2    Gügel, I.L.3    Piotrowski, M.4    Kuhn, A.5
  • 6
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • van der Laan M, Bechtluft P, Kol S, Nouwen N, Driessen AJ, (2004) F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis. J Cell Biol 165: 213-222.
    • (2004) J Cell Biol , vol.165 , pp. 213-222
    • van der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 7
    • 1542350817 scopus 로고    scopus 로고
    • Escherichia coli YidC is a membrane insertase for Sec-independent proteins
    • Serek J, Bauer-Manz G, Struhalla G, Vandenberg L, Kiefer D, et al. (2004) Escherichia coli YidC is a membrane insertase for Sec-independent proteins. EMBO J 23: 294-301.
    • (2004) EMBO J , vol.23 , pp. 294-301
    • Serek, J.1    Bauer-Manz, G.2    Struhalla, G.3    Vandenberg, L.4    Kiefer, D.5
  • 8
    • 84885866691 scopus 로고    scopus 로고
    • Substrate-dependent conformational dynamics of the E. coli insertase YidC
    • Imhof N, Kuhn A, Gerken U, (2011) Substrate-dependent conformational dynamics of the E. coli insertase YidC. Biochemistry 50: 229-239.
    • (2011) Biochemistry , vol.50 , pp. 229-239
    • Imhof, N.1    Kuhn, A.2    Gerken, U.3
  • 9
    • 84856719849 scopus 로고    scopus 로고
    • Dynamic disulfide scanning of the membrane-inserting Pf3 coat protein reveals multiple YidC substrate contacts
    • Klenner C, Kuhn A, (2012) Dynamic disulfide scanning of the membrane-inserting Pf3 coat protein reveals multiple YidC substrate contacts. J Biol Chem 287: 3769-3776.
    • (2012) J Biol Chem , vol.287 , pp. 3769-3776
    • Klenner, C.1    Kuhn, A.2
  • 10
    • 56649088137 scopus 로고    scopus 로고
    • The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis
    • Klenner C, Yuan J, Dalbey RE, Kuhn A, (2008) The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis. FEBS Lett 582: 3967-3972.
    • (2008) FEBS Lett , vol.582 , pp. 3967-3972
    • Klenner, C.1    Yuan, J.2    Dalbey, R.E.3    Kuhn, A.4
  • 11
    • 80052033226 scopus 로고    scopus 로고
    • YidC-driven membrane insertion of single fluorescent Pf3 coat proteins
    • Ernst S, Schönbauer AK, Bär G, Börsch M, Kuhn A, (2011) YidC-driven membrane insertion of single fluorescent Pf3 coat proteins. J Mol Biol 412: 165-175.
    • (2011) J Mol Biol , vol.412 , pp. 165-175
    • Ernst, S.1    Schönbauer, A.K.2    Bär, G.3    Börsch, M.4    Kuhn, A.5
  • 12
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster T, (1949) Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann Physik 2: 55-75.
    • (1949) Ann Physik , vol.2 , pp. 55-75
    • Förster, T.1
  • 13
    • 0343886397 scopus 로고
    • Classical aspects of energy transfer in molecular systems
    • Kuhn H, (1970) Classical aspects of energy transfer in molecular systems. J Chem Phys 53: 101-108.
    • (1970) J Chem Phys , vol.53 , pp. 101-108
    • Kuhn, H.1
  • 14
    • 0033977852 scopus 로고    scopus 로고
    • Real-time swelling-series method improves the accuracy of lamellar neutron-diffraction data
    • Darkes MJ, Bradshaw JP, (2000) Real-time swelling-series method improves the accuracy of lamellar neutron-diffraction data. Acta Crystallogr D Biol Crystallogr 56: 48-54.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 48-54
    • Darkes, M.J.1    Bradshaw, J.P.2
  • 15
    • 37349063087 scopus 로고    scopus 로고
    • Features of transmembrane segments that promote the lateral release from the translocase into the lipid phase
    • Xie K, Hessa T, Seppalä S, Rapp M, von Heijne G, et al. (2007) Features of transmembrane segments that promote the lateral release from the translocase into the lipid phase. Biochemistry 46: 15153-15161.
    • (2007) Biochemistry , vol.46 , pp. 15153-15161
    • Xie, K.1    Hessa, T.2    Seppalä, S.3    Rapp, M.4    von Heijne, G.5
  • 16
    • 67650489237 scopus 로고    scopus 로고
    • Substrate-induced conformational change of the Escherichia coli membrane insertase YidC
    • Winterfeld S, Imhof N, Roos T, Bär G, Kuhn A, et al. (2009) Substrate-induced conformational change of the Escherichia coli membrane insertase YidC. Biochemistry 48: 6684-6691.
    • (2009) Biochemistry , vol.48 , pp. 6684-6691
    • Winterfeld, S.1    Imhof, N.2    Roos, T.3    Bär, G.4    Kuhn, A.5
  • 17
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane insertion
    • Kuhn A, Stuart R, Henry R, Dalbey R, (2003) The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane insertion? Trends Cell Biol 13: 510-516.
    • (2003) Trends Cell Biol , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.4
  • 18
    • 0037040894 scopus 로고    scopus 로고
    • Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane insertion
    • Chen M, Samuelson J, Jiang F, Müller M, Kuhn A, et al. (2002) Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane insertion. J Biol Chem 277: 7670-7675.
    • (2002) J Biol Chem , vol.277 , pp. 7670-7675
    • Chen, M.1    Samuelson, J.2    Jiang, F.3    Müller, M.4    Kuhn, A.5
  • 19
    • 0033571246 scopus 로고    scopus 로고
    • Hydrophobic forces drive the spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control
    • Kiefer D, Kuhn A, (1999) Hydrophobic forces drive the spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control. EMBO J 18: 6299-6306.
    • (1999) EMBO J , vol.18 , pp. 6299-6306
    • Kiefer, D.1    Kuhn, A.2
  • 20
    • 33845761509 scopus 로고    scopus 로고
    • The mechanosensitive channel protein MscL is targeted by SRP to the novel YidC membrane insertion pathway of E. coli
    • Facey S, Neugebauer S, Krauss S, Kuhn A, (2007) The mechanosensitive channel protein MscL is targeted by SRP to the novel YidC membrane insertion pathway of E. coli. J Mol Biol 385: 995-1004.
    • (2007) J Mol Biol , vol.385 , pp. 995-1004
    • Facey, S.1    Neugebauer, S.2    Krauss, S.3    Kuhn, A.4
  • 21
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman DM, Steitz TA, Goldman A, (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Ann Rev Biophys Biochem Chem 15: 321-353.
    • (1986) Ann Rev Biophys Biochem Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 22
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White SH, Wimley WC, (1999) Membrane protein folding and stability: physical principles. Ann Rev Biophys Biomol Struct 28: 319-365.
    • (1999) Ann Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 23
    • 0026680833 scopus 로고
    • Dissection of IncP conjugative plasmid transfer: definition of the transfer region Tra2 by mobilization of the Tra1 region in trans
    • Lessl M, Balzer D, Lurz R, Waters V, Guiney DG, et al. (1992) Dissection of IncP conjugative plasmid transfer: definition of the transfer region Tra2 by mobilization of the Tra1 region in trans. J Bacteriol 174: 2493-2500.
    • (1992) J Bacteriol , vol.174 , pp. 2493-2500
    • Lessl, M.1    Balzer, D.2    Lurz, R.3    Waters, V.4    Guiney, D.G.5
  • 24
    • 44449150447 scopus 로고    scopus 로고
    • Initial binding process of the membrane insertase YidC with its substrate Pf3 coat protein is reversible
    • Gerken U, Erhardt D, Bär G, Gosh R, Kuhn A, (2008) Initial binding process of the membrane insertase YidC with its substrate Pf3 coat protein is reversible. Biochemistry 47: 6052-6058.
    • (2008) Biochemistry , vol.47 , pp. 6052-6058
    • Gerken, U.1    Erhardt, D.2    Bär, G.3    Gosh, R.4    Kuhn, A.5
  • 25
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames BN, Dubin DT, (1960) The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem 235: 769-775.
    • (1960) J Biol Chem , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 26
    • 84855476209 scopus 로고    scopus 로고
    • Ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy
    • Verhalen B, Ernst S, Börsch M, Wilkens S, (2012) Ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy. J Biol Chem 287: 1112-1127.
    • (2012) J Biol Chem , vol.287 , pp. 1112-1127
    • Verhalen, B.1    Ernst, S.2    Börsch, M.3    Wilkens, S.4
  • 27
    • 70349216367 scopus 로고    scopus 로고
    • 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase
    • Düser MG, Zarrabi N, Cipriano DJ, Ernst S, Glick GD, et al. (2009) 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase. EMBO J 28: 2689-2696.
    • (2009) EMBO J , vol.28 , pp. 2689-2696
    • Düser, M.G.1    Zarrabi, N.2    Cipriano, D.J.3    Ernst, S.4    Glick, G.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.