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Volumn 5, Issue , 2015, Pages

Lipids assist the membrane insertion of a BAM-independent outer membrane protein

Author keywords

[No Author keywords available]

Indexed keywords

BAMA PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; LIPID BILAYER; OUTER MEMBRANE PROTEIN;

EID: 84944699383     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep15068     Document Type: Article
Times cited : (11)

References (60)
  • 1
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67, 593-656 (2003).
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 2
    • 84870912403 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel integral proteins of bacterial outer membrane
    • Solov'eva, T. F., Novikova, O. D. & Portnyagina, O. Y. Biogenesis of beta-barrel integral proteins of bacterial outer membrane. Biochemistry (Mosc) 77, 1221-36 (2012).
    • (2012) Biochemistry (Mosc) , Issue.77 , pp. 1221-1236
    • Solov'Eva, T.F.1    Novikova, O.D.2    Portnyagina, O.Y.3
  • 3
    • 79959468179 scopus 로고    scopus 로고
    • Beta-Barrel membrane protein assembly by the Bam complex
    • Hagan, C. L., Silhavy, T. J. & Kahne, D. Beta-Barrel membrane protein assembly by the Bam complex. Annu Rev Biochem 80, 189-210 (2011).
    • (2011) Annu Rev Biochem , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 4
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen, A. J. & Nouwen, N. Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 77, 643-67 (2008).
    • (2008) Annu Rev Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 5
    • 84899126341 scopus 로고    scopus 로고
    • Outer membrane beta-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA
    • Gessmann, D. et al. Outer membrane beta-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA. Proc Natl Acad Sci USA 111, 5878-83 (2014).
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 5878-5883
    • Gessmann, D.1
  • 6
    • 84884419175 scopus 로고    scopus 로고
    • Structural insight into the biogenesis of beta-barrel membrane proteins
    • Noinaj, N. et al. Structural insight into the biogenesis of beta-barrel membrane proteins. Nature 501, 385-90 (2013).
    • (2013) Nature , vol.501 , pp. 385-390
    • Noinaj, N.1
  • 7
    • 84878935527 scopus 로고    scopus 로고
    • The lipid bilayer-inserted membrane protein BamA of Escherichia coli facilitates insertion and folding of outer membrane protein A from its complex with Skp
    • Patel, G. J. & Kleinschmidt, J. H. The lipid bilayer-inserted membrane protein BamA of Escherichia coli facilitates insertion and folding of outer membrane protein A from its complex with Skp. Biochemistry 52, 3974-86 (2013).
    • (2013) Biochemistry , vol.52 , pp. 3974-3986
    • Patel, G.J.1    Kleinschmidt, J.H.2
  • 8
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M. & Tommassen, J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299, 262-5 (2003).
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 9
    • 84939131090 scopus 로고    scopus 로고
    • Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA
    • Dunstan, R. A. et al. Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA. Mol Microbiol 97, 616-29 (2015).
    • (2015) Mol Microbiol , vol.97 , pp. 616-629
    • Dunstan, R.A.1
  • 10
    • 84855218868 scopus 로고    scopus 로고
    • Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries
    • Hoang, H. H. et al. Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries. MBio 2, e00246-11 (2011).
    • (2011) MBio 2 , pp. e00246-e00311
    • Hoang, H.H.1
  • 11
    • 84922031735 scopus 로고    scopus 로고
    • TtOmp85, a beta-barrel assembly protein, functions by barrel augmentation
    • Estrada Mallarino, L. et al. TtOmp85, a beta-barrel assembly protein, functions by barrel augmentation. Biochemistry 54, 844-52 (2015).
    • (2015) Biochemistry , vol.54 , pp. 844-852
    • Estrada Mallarino, L.1
  • 12
    • 84924962448 scopus 로고    scopus 로고
    • The beta-barrel membrane protein insertase machinery from Gram-negative bacteria
    • Noinaj, N., Rollauer, S. E. & Buchanan, S. K. The beta-barrel membrane protein insertase machinery from Gram-negative bacteria. Curr Opin Struct Biol 31, 35-42 (2015).
    • (2015) Curr Opin Struct Biol , vol.31 , pp. 35-42
    • Noinaj, N.1    Rollauer, S.E.2    Buchanan, S.K.3
  • 13
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: Dynamic channels for protein transport across membranes
    • Korotkov, K. V., Gonen, T. & Hol, W. G. Secretins: dynamic channels for protein transport across membranes. Trends Biochem Sci 36, 433-43 (2011).
    • (2011) Trends Biochem Sci , vol.36 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.3
  • 14
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel, M. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J Mol Biol 279, 485-99 (1998).
    • (1998) J Mol Biol , vol.279 , pp. 485-499
    • Russel, M.1
  • 15
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami, M. et al. Structural insights into the secretin PulD and its trypsin-resistant core. J Biol Chem 280, 37732-41 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 37732-37741
    • Chami, M.1
  • 16
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov, K. V., Pardon, E., Steyaert, J. & Hol, W. G. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17, 255-65 (2009).
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 17
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S. & Boucher, C. A. A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol Gen Genet 243, 112-8 (1994).
    • (1994) Mol Gen Genet , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 18
    • 0030965150 scopus 로고    scopus 로고
    • The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function
    • Daefler, S., Guilvout, I., Hardie, K. R., Pugsley, A. P. & Russel, M. The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function. Mol Microbiol 24, 465-75 (1997).
    • (1997) Mol Microbiol , vol.24 , pp. 465-475
    • Daefler, S.1    Guilvout, I.2    Hardie, K.R.3    Pugsley, A.P.4    Russel, M.5
  • 19
    • 80655144742 scopus 로고    scopus 로고
    • Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone
    • Nickerson, N. N. et al. Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone. J Biol Chem 286, 38833-43 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 38833-38843
    • Nickerson, N.N.1
  • 20
    • 79955027962 scopus 로고    scopus 로고
    • Sorting of an integral outer membrane protein via the lipoproteinspecific Lol pathway and a dedicated lipoprotein pilotin
    • Collin, S., Guilvout, I., Nickerson, N. N. & Pugsley, A. P. Sorting of an integral outer membrane protein via the lipoproteinspecific Lol pathway and a dedicated lipoprotein pilotin. Mol Microbiol 80, 655-65 (2011).
    • (2011) Mol Microbiol , vol.80 , pp. 655-665
    • Collin, S.1    Guilvout, I.2    Nickerson, N.N.3    Pugsley, A.P.4
  • 21
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout, I., Chami, M., Engel, A., Pugsley, A. P. & Bayan, N. Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. Embo J 25, 5241-9 (2006).
    • (2006) Embo J , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 22
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K. R., Lory, S. & Pugsley, A. P. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. Embo J 15, 978-88 (1996).
    • (1996) Embo J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 23
    • 34249825232 scopus 로고    scopus 로고
    • YaeT-independent multimerization and outer membrane association of secretin PulD
    • Collin, S., Guilvout, I., Chami, M. & Pugsley, A. P. YaeT-independent multimerization and outer membrane association of secretin PulD. Mol Microbiol 64, 1350-7 (2007).
    • (2007) Mol Microbiol , vol.64 , pp. 1350-1357
    • Collin, S.1    Guilvout, I.2    Chami, M.3    Pugsley, A.P.4
  • 24
    • 55549120907 scopus 로고    scopus 로고
    • Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • Burgess, N. K., Dao, T. P., Stanley, A. M. & Fleming, K. G. Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. J Biol Chem 283, 26748-58 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 26748-26758
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4
  • 25
    • 49349091518 scopus 로고    scopus 로고
    • In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD
    • Guilvout, I. et al. In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD. J Mol Biol 382, 13-23 (2008).
    • (2008) J Mol Biol , vol.382 , pp. 13-23
    • Guilvout, I.1
  • 26
    • 84862557282 scopus 로고    scopus 로고
    • The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation
    • Entzminger, K. C., Chang, C., Myhre, R. O., McCallum, K. C. & Maynard, J. A. The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation. Biochemistry 51, 4822-34 (2012).
    • (2012) Biochemistry , vol.51 , pp. 4822-4834
    • Entzminger, K.C.1    Chang, C.2    Myhre, R.O.3    McCallum, K.C.4    Maynard, J.A.5
  • 27
    • 84881669853 scopus 로고    scopus 로고
    • Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP
    • McMorran, L. M., Bartlett, A. I., Huysmans, G. H., Radford, S. E. & Brockwell, D. J. Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J Mol Biol 425, 3178-91 (2013).
    • (2013) J Mol Biol , vol.425 , pp. 3178-3191
    • McMorran, L.M.1    Bartlett, A.I.2    Huysmans, G.H.3    Radford, S.E.4    Brockwell, D.J.5
  • 28
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • Patel, G. J., Behrens-Kneip, S., Holst, O. & Kleinschmidt, J. H. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 48, 10235-45 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10235-10245
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 29
    • 84886912356 scopus 로고    scopus 로고
    • Sequential steps in the assembly of the multimeric outer membrane secretin PulD
    • Huysmans, G. H., Guilvout, I. & Pugsley, A. P. Sequential steps in the assembly of the multimeric outer membrane secretin PulD. J Biol Chem 288, 30700-7 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 30700-30707
    • Huysmans, G.H.1    Guilvout, I.2    Pugsley, A.P.3
  • 30
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: Separation of proteolytic protection and piloting functions
    • Hardie, K. R., Seydel, A., Guilvout, I. & Pugsley, A. P. The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol Microbiol 22, 967-76 (1996).
    • (1996) Mol Microbiol , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsley, A.P.4
  • 31
    • 83355177984 scopus 로고    scopus 로고
    • Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca
    • Tosi, T. et al. Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca. Mol Microbiol 82, 1422-32 (2011).
    • (2011) Mol Microbiol , vol.82 , pp. 1422-1432
    • Tosi, T.1
  • 32
    • 79952105841 scopus 로고    scopus 로고
    • Multimerization-defective variants of dodecameric secretin PulD
    • Guilvout, I., Nickerson, N. N., Chami, M. & Pugsley, A. P. Multimerization-defective variants of dodecameric secretin PulD. Res Microbiol 162, 180-90 (2011).
    • (2011) Res Microbiol , vol.162 , pp. 180-190
    • Guilvout, I.1    Nickerson, N.N.2    Chami, M.3    Pugsley, A.P.4
  • 33
    • 0021764821 scopus 로고
    • Bacterial membranes and lipid packing theory
    • Goldfine, H. Bacterial membranes and lipid packing theory. J Lipid Res 25, 1501-7 (1984).
    • (1984) J Lipid Res , vol.25 , pp. 1501-1507
    • Goldfine, H.1
  • 35
    • 84881301987 scopus 로고    scopus 로고
    • Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin
    • Rehman, S., Gu, S., Shevchik, V. E. & Pickersgill, R. W. Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin. Acta Crystallogr D Biol Crystallogr 69, 1381-6 (2013).
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 1381-1386
    • Rehman, S.1    Gu, S.2    Shevchik, V.E.3    Pickersgill, R.W.4
  • 36
    • 84860904270 scopus 로고    scopus 로고
    • Structural and functional insights into the pilotin-secretin complex of the type II secretion system
    • Gu, S., Rehman, S., Wang, X., Shevchik, V. E. & Pickersgill, R. W. Structural and functional insights into the pilotin-secretin complex of the type II secretion system. PLoS Pathog 8, e1002531 (2012).
    • (2012) PLoS Pathog , vol.8 , pp. e1002531
    • Gu, S.1    Rehman, S.2    Wang, X.3    Shevchik, V.E.4    Pickersgill, R.W.5
  • 37
    • 0031736546 scopus 로고    scopus 로고
    • Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system
    • Shevchik, V. E. & Condemine, G. Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system. Microbiology 144 (Pt 11), 3219-28 (1998).
    • (1998) Microbiology , vol.144 , pp. 3219-3228
    • Shevchik, V.E.1    Condemine, G.2
  • 38
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert, C., Ryter, A. & Pugsley, A. P. Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J 6, 3531-8 (1987).
    • (1987) EMBO J , vol.6 , pp. 3531-3538
    • D'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 39
    • 84898437564 scopus 로고    scopus 로고
    • Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins
    • Guilvout, I. et al. Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structure 22, 582-9 (2014).
    • (2014) Structure , vol.22 , pp. 582-589
    • Guilvout, I.1
  • 40
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta 1612, 1-40 (2003).
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 41
    • 0017174518 scopus 로고
    • Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12
    • Lugtenberg, E. J. & Peters, R. Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12. Biochim Biophys Acta 441, 38-47 (1976).
    • (1976) Biochim Biophys Acta , vol.441 , pp. 38-47
    • Lugtenberg, E.J.1    Peters, R.2
  • 42
    • 0032740652 scopus 로고    scopus 로고
    • Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids
    • Huang, C. & Li, S. Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids. Biochim Biophys Acta 1422, 273-307 (1999).
    • (1999) Biochim Biophys Acta , vol.1422 , pp. 273-307
    • Huang, C.1    Li, S.2
  • 43
    • 7044232102 scopus 로고    scopus 로고
    • Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
    • van den Brink-van der Laan, E., Killian, J. A. & de Kruijff, B. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim Biophys Acta 1666, 275-88 (2004).
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 275-288
    • Van Den Brink-Van Der Laan, E.1    Killian, J.A.2    De Kruijff, B.3
  • 44
    • 0029975929 scopus 로고    scopus 로고
    • Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures
    • Morein, S., Andersson, A., Rilfors, L. & Lindblom, G. Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures. J Biol Chem 271, 6801-9 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.2    Rilfors, L.3    Lindblom, G.4
  • 45
    • 0025860802 scopus 로고
    • Acyl chain unsaturation modulates distribution of lecithin molecular species between mixed micelles and vesicles in model bile. Implications for particle structure and metastable cholesterol solubilities
    • Cohen, D. E. & Carey, M. C. Acyl chain unsaturation modulates distribution of lecithin molecular species between mixed micelles and vesicles in model bile. Implications for particle structure and metastable cholesterol solubilities. J Lipid Res 32, 1291-302 (1991).
    • (1991) J Lipid Res , vol.32 , pp. 1291-1302
    • Cohen, D.E.1    Carey, M.C.2
  • 46
    • 84878626414 scopus 로고    scopus 로고
    • The targeting, docking and anti-proteolysis functions of the secretin chaperone PulS
    • Collin, S., Krehenbrink, M., Guilvout, I. & Pugsley, A. P. The targeting, docking and anti-proteolysis functions of the secretin chaperone PulS. Res Microbiol 164, 390-6 (2013).
    • (2013) Res Microbiol , vol.164 , pp. 390-396
    • Collin, S.1    Krehenbrink, M.2    Guilvout, I.3    Pugsley, A.P.4
  • 47
    • 84875065984 scopus 로고    scopus 로고
    • Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS
    • Dunstan, R. A. et al. Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS. PLoS Pathog 9, e1003117 (2013).
    • (2013) PLoS Pathog , vol.9 , pp. e1003117
    • Dunstan, R.A.1
  • 48
    • 55749114256 scopus 로고    scopus 로고
    • PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin
    • Koo, J. et al. PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin. J Bacteriol 190, 6961-9 (2008).
    • (2008) J Bacteriol , vol.190 , pp. 6961-6969
    • Koo, J.1
  • 49
    • 12344272637 scopus 로고    scopus 로고
    • Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function
    • Carbonnelle, E., Helaine, S., Prouvensier, L., Nassif, X. & Pelicic, V. Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function. Mol Microbiol 55, 54-64 (2005).
    • (2005) Mol Microbiol , vol.55 , pp. 54-64
    • Carbonnelle, E.1    Helaine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 50
    • 71749120639 scopus 로고    scopus 로고
    • HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
    • Viarre, V. et al. HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J Biol Chem 284, 33815-23 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 33815-33823
    • Viarre, V.1
  • 51
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S. M. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc Natl Acad Sci USA 82, 3665-9 (1985).
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 52
    • 33751253139 scopus 로고    scopus 로고
    • Influence of lipid chemistry on membrane fluidity: Tail and headgroup interactions
    • Seu, K. J., Cambrea, L. R., Everly, R. M. & Hovis, J. S. Influence of lipid chemistry on membrane fluidity: tail and headgroup interactions. Biophys J 91, 3727-35 (2006).
    • (2006) Biophys J , vol.91 , pp. 3727-3735
    • Seu, K.J.1    Cambrea, L.R.2    Everly, R.M.3    Hovis, J.S.4
  • 53
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., Olbrich, K. C., McIntosh, T., Needham, D. & Evans, E. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys J 79, 328-39 (2000).
    • (2000) Biophys J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 54
    • 84921858909 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG
    • Goyal, P. et al. Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516, 250-3 (2014).
    • (2014) Nature , vol.516 , pp. 250-253
    • Goyal, P.1
  • 55
    • 79959235705 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza
    • Sathiyamoorthy, K., Mills, E., Franzmann, T. M., Rosenshine, I. & Saper, M. A. The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza. Biochemistry 50, 5465-76 (2011).
    • (2011) Biochemistry , vol.50 , pp. 5465-5476
    • Sathiyamoorthy, K.1    Mills, E.2    Franzmann, T.M.3    Rosenshine, I.4    Saper, M.A.5
  • 56
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • Guilvout, I., Hardie, K. R., Sauvonnet, N. & Pugsley, A. P. Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J Bacteriol 181, 7212-20 (1999).
    • (1999) J Bacteriol , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 57
    • 0024341985 scopus 로고
    • Protein secretion by gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12
    • d'Enfert, C., Reyss, I., Wandersman, C. & Pugsley, A. P. Protein secretion by gram-negative bacteria. Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12. J Biol Chem 264, 17462-8 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 17462-17468
    • D'Enfert, C.1    Reyss, I.2    Wandersman, C.3    Pugsley, A.P.4
  • 58
    • 0344915159 scopus 로고    scopus 로고
    • Membrane association and multimerization of secreton component pulC
    • Possot, O. M., Gerard-Vincent, M. & Pugsley, A. P. Membrane association and multimerization of secreton component pulC. J Bacteriol 181, 4004-11 (1999).
    • (1999) J Bacteriol , vol.181 , pp. 4004-4011
    • Possot, O.M.1    Gerard-Vincent, M.2    Pugsley, A.P.3
  • 59
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., Chapon, C., D'Enfert, C., Pugsley, A. P. & Schwartz, M. Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. J Bacteriol 164, 633-8 (1985).
    • (1985) J Bacteriol , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 60
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157, 38-46 (2007).
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1


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