메뉴 건너뛰기




Volumn 5, Issue AUGUST, 2016, Pages

Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; HYDROLASE; MEMBRANE LIPID; PERIPLASMIC BINDING PROTEIN; PHOSPHOLIPID; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; MLAB PROTEIN, E COLI; MLAD PROTEIN, E COLI;

EID: 84987704895     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.19042     Document Type: Article
Times cited : (87)

References (48)
  • 1
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain - A link between anion transporters and antisigma-factor antagonists
    • Aravind L, Koonin EV. 2000. The STAS domain - a link between anion transporters and antisigma-factor antagonists. Current Biology 10:R53-R55. doi: 10.1016/S0960-9822(00)00335-3
    • (2000) Current Biology , vol.10 , pp. R53-R55
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 33746096540 scopus 로고    scopus 로고
    • A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking
    • Awai K, Xu C, Tamot B, Benning C. 2006. A phosphatidic acid-binding protein of the chloroplast inner envelope membrane involved in lipid trafficking. PNAS 103:10817-10822. doi: 10.1073/pnas.0602754103
    • (2006) PNAS , vol.103 , pp. 10817-10822
    • Awai, K.1    Xu, C.2    Tamot, B.3    Benning, C.4
  • 4
    • 70350236482 scopus 로고    scopus 로고
    • Mechanisms of lipid transport involved in organelle biogenesis in plant cells
    • Benning C. 2009. Mechanisms of lipid transport involved in organelle biogenesis in plant cells. Annual Review of Cell and Developmental Biology 25:71-91. doi: 10.1146/annurev.cellbio.042308.113414
    • (2009) Annual Review of Cell and Developmental Biology , vol.25 , pp. 71-91
    • Benning, C.1
  • 5
    • 23744436588 scopus 로고    scopus 로고
    • The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis
    • Bishop RE. 2005. The lipid A palmitoyltransferase PagP: molecular mechanisms and role in bacterial pathogenesis. Molecular Microbiology 57:900-912. doi: 10.1111/j.1365-2958.2005.04711.x
    • (2005) Molecular Microbiology , vol.57 , pp. 900-912
    • Bishop, R.E.1
  • 7
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban MJ. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. Journal of Molecular Biology 104:541-555. doi: 10.1016/0022-2836(76)90119-4
    • (1976) Journal of Molecular Biology , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 8
    • 33847775356 scopus 로고    scopus 로고
    • A phylogenomic analysis of the Actinomycetales mce operons
    • Casali N, Riley LW. 2007. A phylogenomic analysis of the Actinomycetales mce operons. BMC Genomics 8:60. doi: 10.1186/1471-2164-8-60
    • (2007) BMC Genomics , vol.8 , pp. 60
    • Casali, N.1    Riley, L.W.2
  • 9
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen J, Sharma S, Quiocho FA, Davidson AL. 2001. Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. PNAS 98:1525-1530. doi: 10.1073/pnas.041542498
    • (2001) PNAS , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 10
    • 77953084208 scopus 로고    scopus 로고
    • Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • Chng SS, Gronenberg LS, Kahne D. 2010a. Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 49:4565-4567. doi: 10.1021/bi100493e
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S.S.1    Gronenberg, L.S.2    Kahne, D.3
  • 11
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • Chng SS, Ruiz N, Chimalakonda G, Silhavy TJ, Kahne D. 2010b. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. PNAS 107:5363-5368. doi: 10.1073/pnas.0912872107
    • (2010) PNAS , vol.107 , pp. 5363-5368
    • Chng, S.S.1    Ruiz, N.2    Chimalakonda, G.3    Silhavy, T.J.4    Kahne, D.5
  • 12
    • 84983166440 scopus 로고    scopus 로고
    • Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli
    • Chong ZS, Woo WF, Chng SS. 2015. Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli. Molecular Microbiology 98:1133-1146. doi: 10.1111/mmi.13202
    • (2015) Molecular Microbiology , vol.98 , pp. 1133-1146
    • Chong, Z.S.1    Woo, W.F.2    Chng, S.S.3
  • 13
    • 84893511071 scopus 로고    scopus 로고
    • PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane
    • Dalebroux ZD, Matamouros S, Whittington D, Bishop RE, Miller SI. 2014. PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane. PNAS 111:1963-1968. doi: 10.1073/pnas.1316901111
    • (2014) PNAS , vol.111 , pp. 1963-1968
    • Dalebroux, Z.D.1    Matamouros, S.2    Whittington, D.3    Bishop, R.E.4    Miller, S.I.5
  • 14
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. PNAS 97:6640-6645. doi: 10.1073/pnas.120163297
    • (2000) PNAS , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 16
    • 0033951375 scopus 로고    scopus 로고
    • Outer-membrane phospholipase A: Known structure, unknown biological function
    • Dekker N. 2000. Outer-membrane phospholipase A: known structure, unknown biological function. Molecular Microbiology 35:711-717. doi: 10.1046/j.1365-2958.2000.01775.x
    • (2000) Molecular Microbiology , vol.35 , pp. 711-717
    • Dekker, N.1
  • 20
    • 84862548484 scopus 로고    scopus 로고
    • Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export
    • Freinkman E, Okuda S, Ruiz N, Kahne D. 2012. Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export. Biochemistry 51:4800-4806. doi: 10.1021/bi300592c
    • (2012) Biochemistry , vol.51 , pp. 4800-4806
    • Freinkman, E.1    Okuda, S.2    Ruiz, N.3    Kahne, D.4
  • 21
    • 0016785971 scopus 로고
    • Biogenesis of membrane lipids: Mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase
    • Hawrot E, Kennedy EP. 1975. Biogenesis of membrane lipids: mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase. PNAS 72:1112-1116. doi: 10.1073/pnas.72.3.1112
    • (1975) PNAS , vol.72 , pp. 1112-1116
    • Hawrot, E.1    Kennedy, E.P.2
  • 23
    • 0017188213 scopus 로고
    • Outer membrane of Salmonella typhimurium: Accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium
    • Kamio Y, Nikaido H. 1976. Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium. Biochemistry 15:2561-2570. doi: 10.1021/bi00657a012
    • (1976) Biochemistry , vol.15 , pp. 2561-2570
    • Kamio, Y.1    Nikaido, H.2
  • 24
    • 0141737560 scopus 로고    scopus 로고
    • NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities
    • Kiianitsa K, Solinger JA, Heyer WD. 2003. NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities. Analytical Biochemistry 321:266-271. doi: 10.1016/S0003-2697(03)00461-5
    • (2003) Analytical Biochemistry , vol.321 , pp. 266-271
    • Kiianitsa, K.1    Solinger, J.A.2    Heyer, W.D.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. doi: 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
    • Liu CE, Liu PQ, Ames GF. 1997. Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). Journal of Biological Chemistry 272:21883-21891. doi: 10.1074/jbc.272.35.21883
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.Q.2    Ames, G.F.3
  • 27
    • 0018742678 scopus 로고
    • Phosphorus NMR analysis of phospholipids in detergents
    • London E, Feigenson GW. 1979. Phosphorus NMR analysis of phospholipids in detergents. Journal of Lipid Research 20:408-412.
    • (1979) Journal of Lipid Research , vol.20 , pp. 408-412
    • London, E.1    Feigenson, G.W.2
  • 28
    • 0017174518 scopus 로고
    • Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12
    • Lugtenberg EJ, Peters R. 1976. Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12. Biochimica Et Biophysica Acta 441:38-47. doi: 10.1016/0005-2760(76)90279-4
    • (1976) Biochimica Et Biophysica Acta , vol.441 , pp. 38-47
    • Lugtenberg, E.J.1    Peters, R.2
  • 29
    • 79960976768 scopus 로고    scopus 로고
    • UniProt Knowledgebase: A hub of integrated protein data
    • UniProt Consortium
    • Magrane M., UniProt Consortium. 2011. UniProt Knowledgebase: a hub of integrated protein data. Database 2011:bar009. doi: 10.1093/database/bar009
    • (2011) Database , vol.2011 , pp. 9
    • Magrane, M.1
  • 30
    • 66049121818 scopus 로고    scopus 로고
    • An ABC transport system that maintains lipid asymmetry in the gram-negative outer membrane
    • Malinverni JC, Silhavy TJ. 2009. An ABC transport system that maintains lipid asymmetry in the gram-negative outer membrane. PNAS 106:8009-8014. doi: 10.1073/pnas.0903229106
    • (2009) PNAS , vol.106 , pp. 8009-8014
    • Malinverni, J.C.1    Silhavy, T.J.2
  • 31
    • 0029904582 scopus 로고    scopus 로고
    • The SpoIIAA protein of Bacillus subtilis has GTP-binding properties
    • Najafi SM, Harris DA, Yudkin MD. 1996. The SpoIIAA protein of Bacillus subtilis has GTP-binding properties. Journal of Bacteriology 178:6632-6634.
    • (1996) Journal of Bacteriology , vol.178 , pp. 6632-6634
    • Najafi, S.M.1    Harris, D.A.2    Yudkin, M.D.3
  • 32
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiology and Molecular Biology Reviews 67:593-656. doi: 10.1128/MMBR.67.4.593-656.2003
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 33
    • 0023809599 scopus 로고
    • Coupled assay of Na+, K+-ATPase activity
    • Nørby JG. 1988. Coupled assay of Na+, K+-ATPase activity. Methods in Enzymology 156:116-119. doi: 10.1016/0076-6879(88)56014-7
    • (1988) Methods in Enzymology , vol.156 , pp. 116-119
    • Nørby, J.G.1
  • 34
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn MJ, Gander JE, Parisi E, Carson J. 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. The Journal of Biological Chemistry 247:3962-3972.
    • (1972) The Journal of Biological Chemistry , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 35
    • 41949119272 scopus 로고    scopus 로고
    • Mycobacterial persistence requires the utilization of host cholesterol
    • Pandey AK, Sassetti CM. 2008. Mycobacterial persistence requires the utilization of host cholesterol. PNAS 105:4376-4380. doi: 10.1073/pnas.0711159105
    • (2008) PNAS , vol.105 , pp. 4376-4380
    • Pandey, A.K.1    Sassetti, C.M.2
  • 36
    • 60549094781 scopus 로고    scopus 로고
    • Detergent binding explains anomalous SDS-PAGE migration of membrane proteins
    • Rath A, Glibowicka M, Nadeau VG, Chen G, Deber CM. 2009. Detergent binding explains anomalous SDS-PAGE migration of membrane proteins. PNAS 106:1760-1765. doi: 10.1073/pnas.0813167106
    • (2009) PNAS , vol.106 , pp. 1760-1765
    • Rath, A.1    Glibowicka, M.2    Nadeau, V.G.3    Chen, G.4    Deber, C.M.5
  • 37
    • 0033973103 scopus 로고    scopus 로고
    • The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
    • Reich-Slotky R, Panagiotidis C, Reyes M, Shuman HA. 2000. The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil. Journal of Bacteriology 182:993-1000. doi: 10.1128/JB. 182.4.993-1000.2000
    • (2000) Journal of Bacteriology , vol.182 , pp. 993-1000
    • Reich-Slotky, R.1    Panagiotidis, C.2    Reyes, M.3    Shuman, H.A.4
  • 38
    • 79957611908 scopus 로고    scopus 로고
    • Arabidopsis chloroplast lipid transport protein TGD2 disrupts membranes and is part of a large complex
    • Roston R, Gao J, Xu C, Benning C. 2011. Arabidopsis chloroplast lipid transport protein TGD2 disrupts membranes and is part of a large complex. The Plant Journal 66:759-769. doi: 10.1111/j.1365-313X.2011. 04536.x
    • (2011) The Plant Journal , vol.66 , pp. 759-769
    • Roston, R.1    Gao, J.2    Xu, C.3    Benning, C.4
  • 39
    • 84862299409 scopus 로고    scopus 로고
    • TGD1, -2, and -3 proteins involved in lipid trafficking form ATP-binding cassette (ABC) transporter with multiple substrate-binding proteins
    • Roston RL, Gao J, Murcha MW, Whelan J, Benning C. 2012. TGD1, -2, and -3 proteins involved in lipid trafficking form ATP-binding cassette (ABC) transporter with multiple substrate-binding proteins. Journal of Biological Chemistry 287:21406-21415. doi: 10.1074/jbc.M112.370213
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 21406-21415
    • Roston, R.L.1    Gao, J.2    Murcha, M.W.3    Whelan, J.4    Benning, C.5
  • 40
    • 18144406818 scopus 로고    scopus 로고
    • Structural and functional analysis of the C-terminal STAS (sulfate transporter and anti-sigma antagonist) domain of the Arabidopsis thaliana sulfate transporter SULTR1.2
    • Rouached H, Berthomieu P, El Kassis E, Cathala N, Catherinot V, Labesse G, Davidian JC, Fourcroy P. 2005. Structural and functional analysis of the C-terminal STAS (sulfate transporter and anti-sigma antagonist) domain of the Arabidopsis thaliana sulfate transporter SULTR1.2. Journal of Biological Chemistry 280:15976-15983. doi: 10.1074/jbc.M501635200
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 15976-15983
    • Rouached, H.1    Berthomieu, P.2    El Kassis, E.3    Cathala, N.4    Catherinot, V.5    Labesse, G.6    Davidian, J.C.7    Fourcroy, P.8
  • 41
    • 33747357532 scopus 로고    scopus 로고
    • The role of the STAS domain in the function and biogenesis of a sulfate transporter as probed by random mutagenesis
    • Shibagaki N, Grossman AR. 2006. The role of the STAS domain in the function and biogenesis of a sulfate transporter as probed by random mutagenesis. Journal of Biological Chemistry 281:22964-22973. doi: 10.1074/jbc.M603462200
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 22964-22973
    • Shibagaki, N.1    Grossman, A.R.2
  • 43
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom DJ, Duurkens RH, Olieman K, Erkens GB. 2008. Static light scattering to characterize membrane proteins in detergent solution. Methods 46:73-82. doi: 10.1016/j.ymeth.2008.06.012
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 45
    • 0038602740 scopus 로고    scopus 로고
    • Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
    • Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K. 2003. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. The EMBO Journal 22:3199-3209. doi: 10.1093/emboj/cdg324
    • (2003) The EMBO Journal , vol.22 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4    Tokuda, H.5    Miki, K.6
  • 46
    • 84875833653 scopus 로고    scopus 로고
    • A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization
    • Tal N, Ovcharenko E, Lewinson O. 2013. A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization. PNAS 110:5434-5439. doi: 10.1073/pnas. 1209644110
    • (2013) PNAS , vol.110 , pp. 5434-5439
    • Tal, N.1    Ovcharenko, E.2    Lewinson, O.3
  • 47
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. The EMBO Journal 1:945-951.
    • (1982) The EMBO Journal , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 48
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. PNAS 103:11754-11759. doi: 10.1073/pnas.0604744103
    • (2006) PNAS , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.