메뉴 건너뛰기




Volumn 2, Issue 6, 2011, Pages

Erratum to Unbalanced charge distribution as a determinant for dependence of a subset of Escherichia coli membrane proteins on the membrane insertase YidC (mBio (2011) 2, 6, 10.1128/mBio.00238-11);Unbalanced charge distribution as a determinant for dependence of a subset of Escherichia coli membrane proteins on the membrane insertase YidC

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; YIDC PROTEIN;

EID: 84855239343     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00500-12     Document Type: Erratum
Times cited : (22)

References (46)
  • 1
    • 0031892162 scopus 로고    scopus 로고
    • How many membrane proteins are there?
    • Boyd D, Schierle C, Beckwith J. 1998. How many membrane proteins are there? Protein Sci. 7:201-205.
    • (1998) Protein Sci , vol.7 , pp. 201-205
    • Boyd, D.1    Schierle, C.2    Beckwith, J.3
  • 2
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K, Dalbey RE. 2008. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat. Rev. Microbiol. 6:234-244.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 3
    • 57649119791 scopus 로고    scopus 로고
    • Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes
    • Kol S, Nouwen N, Driessen AJ. 2008. Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes. J. Biol. Chem. 283:31269-31273.
    • (2008) J. Biol. Chem , vol.283 , pp. 31269-31273
    • Kol, S.1    Nouwen, N.2    Driessen, A.J.3
  • 4
    • 18844444516 scopus 로고    scopus 로고
    • Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review)
    • Yi L, Dalbey RE. 2005. Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review). Mol. Membr. Biol. 22:101-111.
    • (2005) Mol. Membr. Biol , vol.22 , pp. 101-111
    • Yi, L.1    Dalbey, R.E.2
  • 5
    • 33845761509 scopus 로고    scopus 로고
    • The mechanosensi-tive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli
    • Facey SJ, Neugebauer SA, Krauss S, Kuhn A. 2007. The mechanosensi-tive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli. J. Mol. Biol. 365:995-1004.
    • (2007) J. Mol. Biol , vol.365 , pp. 995-1004
    • Facey, S.J.1    Neugebauer, S.A.2    Krauss, S.3    Kuhn, A.4
  • 6
    • 4544234959 scopus 로고    scopus 로고
    • Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase
    • Yi L, Celebi N, Chen M, Dalbey RE. 2004. Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase. J. Biol. Chem. 279:39260-39267.
    • (2004) J. Biol. Chem , vol.279 , pp. 39260-39267
    • Yi, L.1    Celebi, N.2    Chen, M.3    Dalbey, R.E.4
  • 7
    • 0034632819 scopus 로고    scopus 로고
    • YidC mediates membrane protein insertion in bacteria
    • Samuelson JC, et al. 2000. YidC mediates membrane protein insertion in bacteria. Nature 406:637-641.
    • (2000) Nature , vol.406 , pp. 637-641
    • Samuelson, J.C.1
  • 8
    • 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
  • 9
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxa1 family of protein translocases
    • Yen MR, Harley KT, Tseng YH, Saier MH. 2001. Phylogenetic and structural analyses of the oxa1 family of protein translocases. FEMS Mi-crobiol. Lett. 204:223-231.
    • (2001) FEMS Mi-crobiol. Lett , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier, M.H.4
  • 10
    • 47249121296 scopus 로고    scopus 로고
    • A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels
    • Camp AH, Losick R. 2008. A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels. Mol. Microbiol. 69:402-417.
    • (2008) Mol. Microbiol , vol.69 , pp. 402-417
    • Camp, A.H.1    Losick, R.2
  • 11
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: Membrane-localized chaperones facilitating membrane protein insertion?
    • Kuhn A, Stuart R, Henry R, Dalbey RE. 2003. The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein 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.E.4
  • 12
    • 0034651753 scopus 로고    scopus 로고
    • YidC, the Escherichia coli homologue of mitochon-drial Oxa1p, is a component of the Sec translocase
    • Scotti PA, et al. 2000. YidC, the Escherichia coli homologue of mitochon-drial Oxa1p, is a component of the Sec translocase. EMBO J. 19:542-549.
    • (2000) EMBO J , vol.19 , pp. 542-549
    • Scotti, P.A.1
  • 13
    • 0034859711 scopus 로고    scopus 로고
    • YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translo-con and lipids
    • Beck K, et al. 2001. YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translo-con and lipids. EMBO Rep. 2:709-714.
    • (2001) EMBO Rep , vol.2 , pp. 709-714
    • Beck, K.1
  • 14
    • 55249119546 scopus 로고    scopus 로고
    • YidC is involved in the biogenesis of anaerobic respiratory complexes in the inner membrane of Escherichia coli
    • Price CE, Driessen AJ. 2008. YidC is involved in the biogenesis of anaerobic respiratory complexes in the inner membrane of Escherichia coli. J. Biol. Chem. 283:26921-26927.
    • (2008) J. Biol. Chem , vol.283 , pp. 26921-26927
    • Price, C.E.1    Driessen, A.J.2
  • 15
    • 0037947833 scopus 로고    scopus 로고
    • A conserved function of YidC in the biogenesis of respiratory chain complexes
    • van der Laan M, et al. 2003. A conserved function of YidC in the biogenesis of respiratory chain complexes. Proc. Natl. Acad. Sci. U. S. A. 100: 5801-5806.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 5801-5806
    • van der Laan, M.1
  • 16
    • 49649117794 scopus 로고    scopus 로고
    • Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC
    • Wagner S, et al. 2008. Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. J. Biol. Chem. 283: 17881-17890.
    • (2008) J. Biol. Chem , vol.283 , pp. 17881-17890
    • Wagner, S.1
  • 17
    • 0345505686 scopus 로고    scopus 로고
    • Versatility of inner membrane protein biogenesis in Escherichia coli
    • Fröderberg L, et al. 2003. Versatility of inner membrane protein biogenesis in Escherichia coli. Mol. Microbiol. 47:1015-1027.
    • (2003) Mol. Microbiol , vol.47 , pp. 1015-1027
    • Fröderberg, L.1
  • 18
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • Nagamori S, Smirnova IN, Kaback HR. 2004. Role of YidC in folding of polytopic membrane proteins. J. Cell Biol. 165:53-62.
    • (2004) J. Cell Biol , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 19
    • 77956555964 scopus 로고    scopus 로고
    • Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions
    • Price CE, et al. 2010. Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions. Proteomics 10:3235-3247.
    • (2010) Proteomics , vol.10 , pp. 3235-3247
    • Price, C.E.1
  • 20
    • 79955914078 scopus 로고    scopus 로고
    • Characterization of the consequences of YidC depletion on the inner membrane proteome of E. coli using 2D blue native/SDS-PAGE
    • Wickström D, et al. 2011. Characterization of the consequences of YidC depletion on the inner membrane proteome of E. coli using 2D blue native/SDS-PAGE. J. Mol. Biol. 409:124-135.
    • (2011) J. Mol. Biol , vol.409 , pp. 124-135
    • Wickström, D.1
  • 21
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa M, et al. 2005. Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12:291-299.
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1
  • 22
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll L, Krogh A, Sonnhammer EL. 2004. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338: 1027-1036.
    • (2004) J. Mol. Biol , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 23
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley DO, et al. 2005. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308:1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1
  • 25
    • 0041315927 scopus 로고    scopus 로고
    • YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase
    • Yi L, et al. 2003. YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase. Biochemistry 42:10537-10544.
    • (2003) Biochemistry , vol.42 , pp. 10537-10544
    • Yi, L.1
  • 26
    • 0015132002 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100
    • Schnaitman CA. 1971. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J. Bacteriol. 108:545-552.
    • (1971) J. Bacteriol , vol.108 , pp. 545-552
    • Schnaitman, C.A.1
  • 27
    • 20144387770 scopus 로고    scopus 로고
    • The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential
    • van Bloois E, et al. 2005. The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential. J. Biol. Chem. 280: 12996-13003.
    • (2005) J. Biol. Chem , vol.280 , pp. 12996-13003
    • van Bloois, E.1
  • 28
    • 1642540997 scopus 로고    scopus 로고
    • A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli
    • Schmidt KL, et al. 2004. A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli. J. Bacteriol. 186:785-793.
    • (2004) J. Bacteriol , vol.186 , pp. 785-793
    • Schmidt, K.L.1
  • 29
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apoli-poprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon C, Vidal-Ingigliardi D, Pugsley AP. 2005. Depletion of apoli-poprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 280:974 -983.
    • (2005) J. Biol. Chem , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 30
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T, Bork-Jensen J, Gerdes K. 2005. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55:78-89.
    • (2005) Mol. Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 31
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba T, et al. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006-2008.
    • (2006) Mol. Syst. Biol , vol.2 , pp. 2006-2008
    • Baba, T.1
  • 32
    • 19944431737 scopus 로고    scopus 로고
    • Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome
    • Hashimoto M, et al. 2005. Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome. Mol. Microbiol. 55: 137-149.
    • (2005) Mol. Microbiol , vol.55 , pp. 137-149
    • Hashimoto, M.1
  • 33
    • 0141504252 scopus 로고    scopus 로고
    • Experimental determination and system level analysis of essential genes in Escherichia coli MG1655
    • Gerdes SY, et al. 2003. Experimental determination and system level analysis of essential genes in Escherichia coli MG1655. J. Bacteriol. 185: 5673-5684.
    • (2003) J. Bacteriol , vol.185 , pp. 5673-5684
    • Gerdes, S.Y.1
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 0024372724 scopus 로고
    • Positively charged amino acid residues can act as topogenic determinants in membrane proteins
    • Boyd D, Beckwith J. 1989. Positively charged amino acid residues can act as topogenic determinants in membrane proteins. Proc. Natl. Acad. Sci. U. S. A. 86:9446-9450.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 9446-9450
    • Boyd, D.1    Beckwith, J.2
  • 36
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne G. 1986. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:3021-3027.
    • (1986) EMBO J , vol.5 , pp. 3021-3027
    • von Heijne, G.1
  • 37
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund H, Elofsson A. 2008. OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24:1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 39
    • 80052782538 scopus 로고    scopus 로고
    • Membrane localization of small proteins in Escherichia coli
    • Fontaine F, Fuchs RT, Storz G. 2011. Membrane localization of small proteins in Escherichia coli. J. Biol. Chem. 286:32464-32474.
    • (2011) J. Biol. Chem , vol.286 , pp. 32464-32474
    • Fontaine, F.1    Fuchs, R.T.2    Storz, G.3
  • 40
    • 0028175016 scopus 로고
    • Topological "frustration" in multispan-ning E. coli inner membrane proteins
    • Gafvelin G, von Heijne G. 1994. Topological "frustration" in multispan-ning E. coli inner membrane proteins. Cell 77:401-412.
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    von Heijne, G.2
  • 42
    • 0036015653 scopus 로고    scopus 로고
    • SecDFyajC forms a heterotetrameric complex with YidC
    • Nouwen N, Driessen AJ. 2002. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 44:1397-1405.
    • (2002) Mol. Microbiol , vol.44 , pp. 1397-1405
    • Nouwen, N.1    Driessen, A.J.2
  • 43
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • Van den Berg B, et al. 2004. X-ray structure of a protein-conducting channel. Nature 427:36-44.
    • (2004) Nature , vol.427 , pp. 36-44
    • van den Berg, B.1
  • 44
    • 37349111755 scopus 로고    scopus 로고
    • Projection structure of yidC: A conserved mediator of membrane protein assembly
    • Lotz M, Haase W, Kühlbrandt W, Collinson I. 2008. Projection structure of yidC: a conserved mediator of membrane protein assembly. J. Mol. Biol. 375:901-907.
    • (2008) J. Mol. Biol , vol.375 , pp. 901-907
    • Lotz, M.1    Haase, W.2    Kühlbrandt, W.3    Collinson, I.4
  • 45
    • 0034958117 scopus 로고    scopus 로고
    • Sec-dependent membrane protein insertion: Sequential interaction of nascent FtsQ with SecY and YidC
    • Urbanus ML, et al. 2001. Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC. EMBO Rep. 2:524-529.
    • (2001) EMBO Rep , vol.2 , pp. 524-529
    • Urbanus, M.L.1
  • 46
    • 77950510571 scopus 로고    scopus 로고
    • Conserved negative charges in the trans-membrane segments of subunit K of the NADH: Ubiquinone oxidoreduc-tase determine its dependence on YidC for membrane insertion
    • Price CE, Driessen AJ. 2010. Conserved negative charges in the trans-membrane segments of subunit K of the NADH: ubiquinone oxidoreduc-tase determine its dependence on YidC for membrane insertion. J. Biol. Chem. 285:3575-3581.
    • (2010) J. Biol. Chem , vol.285 , pp. 3575-3581
    • Price, C.E.1    Driessen, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.