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Volumn 5, Issue , 2014, Pages

Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes

Author keywords

[No Author keywords available]

Indexed keywords

AG43 PROTEIN; GOLD; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN TAMA; OUTER MEMBRANE PROTEIN TAMB; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; LIPID BILAYER; NANOPARTICLE;

EID: 84939171436     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6078     Document Type: Article
Times cited : (66)

References (45)
  • 1
    • 84869495206 scopus 로고    scopus 로고
    • Evolution of the beta-barrel assembly machinery
    • Webb, C. T., Heinz, E. & Lithgow, T. Evolution of the beta-barrel assembly machinery. Trends Microbiol. 20, 612-620 (2012).
    • (2012) Trends Microbiol. , vol.20 , pp. 612-620
    • Webb, C.T.1    Heinz, E.2    Lithgow, T.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
    • 84902327125 scopus 로고    scopus 로고
    • Assembly of beta-barrel proteins into bacterial outer membranes
    • Selkrig, J., and Leyton, D. L., Webb, C. T. & Lithgow, T. Assembly of beta-barrel proteins into bacterial outer membranes. Biochim. Biophys. Acta 1843, 1542-1550 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1542-1550
    • Selkrig, J.1    Leyton, D.L.2    Webb, C.T.3    Lithgow, T.4
  • 5
    • 84861451226 scopus 로고    scopus 로고
    • The bacterial outer membrane beta-barrel assembly machinery
    • Kim, K. H., Aulakh, S. & Paetzel, M. The bacterial outer membrane beta-barrel assembly machinery. Protein Sci. 21, 751-768 (2012).
    • (2012) Protein Sci. , vol.21 , pp. 751-768
    • Kim, K.H.1    Aulakh, S.2    Paetzel, M.3
  • 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, 385-390 (2013).
    • (2013) Nature , vol.501 , pp. 385-390
    • Noinaj, N.1
  • 7
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of skp in the biogenesis of outer membrane protein
    • De Cock, H. et al. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259, 96-103 (1999).
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • De Cock, H.1
  • 8
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein phoe with the periplasmic chaperone skp occurs at the cytoplasmic membrane
    • Harms, N. et al. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 276, 18804-18811 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18804-18811
    • Harms, N.1
  • 9
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schafer, U., Beck, K. & Muller, M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274, 24567-24574 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schafer, U.1    Beck, K.2    Muller, M.3
  • 10
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • Tamm, L. K., Hong, H. & Liang, B. Folding and assembly of beta-barrel membrane proteins. Biochim. Biophys. Acta 1666, 250-263 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 11
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J. E. & Otzen, D. E. Interactions between folding factors and bacterial outer membrane proteins. Mol. Microbiol. 57, 326-346 (2005).
    • (2005) Mol. Microbiol. , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 12
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, skp, and DegP in Escherichia coli
    • Sklar, J. G., Wu, T., Kahne, D. & Silhavy, T. J. Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 21, 2473-2484 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 13
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain
    • Ieva, R., Tian, P., Peterson, J. H. & Bernstein, H. D. Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. Proc. Natl Acad. Sci. USA 108, E383-E391 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. E383-E391
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.D.4
  • 14
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim, S. et al. Structure and function of an essential component of the outer membrane protein assembly machine. Science 317, 961-964 (2007).
    • (2007) Science , vol.317 , pp. 961-964
    • Kim, S.1
  • 15
    • 77956153485 scopus 로고    scopus 로고
    • Dissection of beta-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli
    • Bennion, D., and Charlson, E. S., Coon, E. & Misra, R. Dissection of beta-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli. Mol. Microbiol. 77, 1153-1171 (2010).
    • (2010) Mol. Microbiol. , vol.77 , pp. 1153-1171
    • Bennion, D.1    Charlson, E.S.2    Coon, E.3    Misra, R.4
  • 16
    • 77957678381 scopus 로고    scopus 로고
    • Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein
    • Ruiz-Perez, F., Henderson, I. R. & Nataro, J. P. Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein. Gut. Microbes 1, 339-344 (2010).
    • (2010) Gut. Microbes , vol.1 , pp. 339-344
    • Ruiz-Perez, F.1    Henderson, I.R.2    Nataro, J.P.3
  • 17
    • 84861172996 scopus 로고    scopus 로고
    • Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics
    • Denoncin, K., Schwalm, J., Vertommen, D., Silhavy, T. J. & Collet, J. F. Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics. Proteomics 12, 1391-1401 (2012).
    • (2012) Proteomics , vol.12 , pp. 1391-1401
    • Denoncin, K.1    Schwalm, J.2    Vertommen, D.3    Silhavy, T.J.4    Collet, J.F.5
  • 18
    • 27144431766 scopus 로고    scopus 로고
    • Protein complexes of the Escherichia coli cell envelope
    • Stenberg, F. et al. Protein complexes of the Escherichia coli cell envelope. J. Biol. Chem. 280, 34409-34419 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 34409-34419
    • Stenberg, F.1
  • 19
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T. et al. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121, 235-245 (2005).
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1
  • 20
    • 35948954841 scopus 로고    scopus 로고
    • First glimpse of the crystal structure of YaeT's POTRA domains
    • Misra, R. First glimpse of the crystal structure of YaeT's POTRA domains. ACS Chem. Biol. 2, 649-651 (2007).
    • (2007) ACS Chem. Biol. , vol.2 , pp. 649-651
    • Misra, R.1
  • 21
    • 84860719904 scopus 로고    scopus 로고
    • Discovery of an archetypal protein transport system in bacterial outer membranes
    • Selkrig, J. et al. Discovery of an archetypal protein transport system in bacterial outer membranes. Nat. Struct. Mol. Biol. 19, S1 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. S1
    • Selkrig, J.1
  • 22
    • 84905401566 scopus 로고    scopus 로고
    • A comprehensive analysis of the omp85/TpsB protein superfamily structural diversity
    • Heinz, E. & Lithgow, T. A comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity. Front. Microbiol. 5, 370 (2014).
    • (2014) Front. Microbiol. , vol.5 , pp. 370
    • Heinz, E.1    Lithgow, T.2
  • 23
    • 84887430811 scopus 로고    scopus 로고
    • The structural basis of autotransporter translocation by TamA
    • Gruss, F. et al. The structural basis of autotransporter translocation by TamA. Nat. Struct. Mol. Biol. 20, 1318-1320 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1318-1320
    • Gruss, F.1
  • 24
    • 77649289609 scopus 로고    scopus 로고
    • Complete genome sequence and comparative metabolic profiling of the prototypical enteroaggregative Escherichia coli strain 042
    • Chaudhuri, R. R. et al. Complete genome sequence and comparative metabolic profiling of the prototypical enteroaggregative Escherichia coli strain 042. PLoS ONE 5, e8801 (2010).
    • (2010) PLoS ONE , vol.5
    • Chaudhuri, R.R.1
  • 25
    • 81755177857 scopus 로고    scopus 로고
    • Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways
    • Babu, M. et al. Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways. PLoS Genet. 7, e1002377 (2011).
    • (2011) PLoS Genet. , vol.7
    • Babu, M.1
  • 26
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker, M. et al. Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc. Natl Acad. Sci. USA 103, 4918-4923 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4918-4923
    • Junker, M.1
  • 27
    • 69949171713 scopus 로고    scopus 로고
    • An ion-channel-containing model membrane: Structural determination by magnetic contrast neutron reflectometry
    • Holt, S. A. et al. An ion-channel-containing model membrane: structural determination by magnetic contrast neutron reflectometry. Soft Matter 5, 2576-2586 (2009).
    • (2009) Soft Matter , vol.5 , pp. 2576-2586
    • Holt, S.A.1
  • 28
    • 79951773699 scopus 로고    scopus 로고
    • The structural orientation of antibody layers bound to engineered biosensor surfaces
    • Le Brun, A. P., Holt, S. A., and Shah, D. S., Majkrzak, C. F. & Lakey, J. H. The structural orientation of antibody layers bound to engineered biosensor surfaces. Biomaterials 32, 3303-3311 (2011).
    • (2011) Biomaterials , vol.32 , pp. 3303-3311
    • Le Brun, A.P.1    Holt, S.A.2    Shah, D.S.3    Majkrzak, C.F.4    Lakey, J.H.5
  • 29
    • 69949138064 scopus 로고    scopus 로고
    • Neutrons for biologists: A beginner's guide, or why you should consider using neutrons
    • Lakey, J. H. Neutrons for biologists: a beginner's guide, or why you should consider using neutrons. J. R. Soc. Interface 5, 567-573 (2009).
    • (2009) J. R. Soc. Interface , vol.5 , pp. 567-573
    • Lakey, J.H.1
  • 30
    • 68349116231 scopus 로고    scopus 로고
    • Quartz crystal microbalance as a sensor to characterize macromolecular assembly dynamics
    • (2009)
    • Kanazawa, K. & Cho, N.-J. Quartz crystal microbalance as a sensor to characterize macromolecular assembly dynamics. J. Sensors 2009, 1-17 (2009).
    • (2009) J. Sensors , pp. 1-17
    • Kanazawa, K.1    Cho, N.-J.2
  • 31
    • 79955842226 scopus 로고    scopus 로고
    • QCM-D fingerprinting of membrane-active peptides
    • McCubbin, G. A. et al. QCM-D fingerprinting of membrane-active peptides. Eur. Biophys. J. 40, 437-446 (2011).
    • (2011) Eur. Biophys. J. , vol.40 , pp. 437-446
    • McCubbin, G.A.1
  • 32
    • 80052553079 scopus 로고    scopus 로고
    • The interaction of cubosomes with supported phospholipid bilayers using neutron reflectometry and QCM-D
    • Shen, H.-H.. et al. The interaction of cubosomes with supported phospholipid bilayers using neutron reflectometry and QCM-D. Soft Matter 7, 8041-8049 (2011).
    • (2011) Soft Matter , vol.7 , pp. 8041-8049
    • Shen, H.-H.1
  • 33
    • 77952400735 scopus 로고    scopus 로고
    • Destruction and solubilization of supported phospholipid bilayers on silica by the biosurfactant surfactin
    • Shen, H. H., and Thomas, R. K., Penfold, J. & Fragneto, G. Destruction and solubilization of supported phospholipid bilayers on silica by the biosurfactant surfactin. Langmuir 26, 7334-7342 (2010).
    • (2010) Langmuir , vol.26 , pp. 7334-7342
    • Shen, H.H.1    Thomas, R.K.2    Penfold, J.3    Fragneto, G.4
  • 35
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The keio collection
    • 2006.0008
    • Baba, T. et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol.. 2, 2006.0008 (2006).
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1
  • 36
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl Acad. Sci. USA 97, 6640-6645 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 37
    • 0025325983 scopus 로고
    • The 'megaprimer' method of site-directed mutagenesis
    • Sarkar, G. & Sommer, S. S. The 'megaprimer' method of site-directed mutagenesis. Biotechniques 8, 404-407 (1990).
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 38
    • 82755163015 scopus 로고    scopus 로고
    • Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins
    • Leyton, D. L. et al. Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins. J. Biol. Chem. 286, 42283-42291 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 42283-42291
    • Leyton, D.L.1
  • 39
    • 33748093283 scopus 로고    scopus 로고
    • Identification of tam41 maintaining integriy of the TIM23 protein translocator complex in mitochonidria
    • Tamura, Y. et al. Identification of Tam41 maintaining integriy of the TIM23 protein translocator complex in mitochonidria. J. Cell. Biol. 174, 631-637 (2006).
    • (2006) J. Cell. Biol. , vol.174 , pp. 631-637
    • Tamura, Y.1
  • 40
    • 84865523255 scopus 로고    scopus 로고
    • Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC
    • Webb, C. T. et al. Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC. J. Mol. Biol. 422, 545-555 (2012).
    • (2012) J. Mol. Biol. , vol.422 , pp. 545-555
    • Webb, C.T.1
  • 41
    • 34447287606 scopus 로고    scopus 로고
    • Functional analysis of antigen 43 in uropathogenic Escherichia coli reveals a role in long-term persistence in the urinary tract
    • Ulett, G. C. et al. Functional analysis of antigen 43 in uropathogenic Escherichia coli reveals a role in long-term persistence in the urinary tract. Infect. Immun. 75, 3233-3244 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 3233-3244
    • Ulett, G.C.1
  • 42
    • 10344265554 scopus 로고    scopus 로고
    • Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy
    • Ataka, K. et al. Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy. J. Am. Chem. Soc. 126, 16199-16206 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16199-16206
    • Ataka, K.1
  • 43
    • 13944267055 scopus 로고    scopus 로고
    • Controlling protein orientation at interfaces using histidine tags: An alternative to ni/NTA
    • Johnson, D. L. & Martin, L. L. Controlling protein orientation at interfaces using histidine tags: an alternative to Ni/NTA. J. Am. Chem. Soc. 127, 2018-2019 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2018-2019
    • Johnson, D.L.1    Martin, L.L.2
  • 44
    • 3342914945 scopus 로고    scopus 로고
    • Neutron reflection from liquid interfaces
    • Thomas, R. K. Neutron reflection from liquid interfaces. Annu. Rev. Phys. Chem. 55, 391-426 (2004).
    • (2004) Annu. Rev. Phys. Chem. , vol.55 , pp. 391-426
    • Thomas, R.K.1
  • 45
    • 79953759979 scopus 로고    scopus 로고
    • Motofit-integrating neutron reflectometry acquisition, reduction and analysis into one, easy to use, package
    • Nelson, A. Motofit-integrating neutron reflectometry acquisition, reduction and analysis into one, easy to use, package. J. Phys. Conf. Ser. 251, 012094 (2010).
    • (2010) J. Phys. Conf. Ser. , vol.251
    • Nelson, A.1


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