메뉴 건너뛰기




Volumn 107, Issue 50, 2010, Pages 21412-21417

Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF

Author keywords

Colicin translocation; Intrinsically unstructured protein; Isothermal titration calorimetry; Protein protein interaction; Transmembrane signaling

Indexed keywords

COLICIN; EPITOPE; OUTER MEMBRANE PROTEIN F;

EID: 78650758264     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1010780107     Document Type: Article
Times cited : (78)

References (48)
  • 1
    • 77953293697 scopus 로고    scopus 로고
    • Molecular mechanisms in signal transduction at the membrane
    • Groves JT, Kuriyan J (2010) Molecular mechanisms in signal transduction at the membrane. Nat Struct Mol Biol 17:659-665.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 659-665
    • Groves, J.T.1    Kuriyan, J.2
  • 2
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 3
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ,Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 39049162291 scopus 로고    scopus 로고
    • Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1
    • Galea CA, et al. (2008) Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1. J Mol Biol 376:827-838.
    • (2008) J Mol Biol , vol.376 , pp. 827-838
    • Galea, C.A.1
  • 6
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM (2008) Tight regulation of unstructured proteins: From transcript synthesis to protein degradation. Science 322:1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 7
    • 2442442058 scopus 로고    scopus 로고
    • The molecular basis of fibronectin-mediated bacterial adherence to host cells
    • Schwarz-Linek U, Hook M, Potts JR (2004) The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol Microbiol 52:631-641.
    • (2004) Mol Microbiol , vol.52 , pp. 631-641
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 8
    • 33947368999 scopus 로고    scopus 로고
    • Colicin biology
    • Cascales E, et al. (2007) Colicin biology. Microbiol Mol Biol R 71:158-229.
    • (2007) Microbiol Mol Biol R , vol.71 , pp. 158-229
    • Cascales, E.1
  • 9
    • 0242490498 scopus 로고    scopus 로고
    • The structure of BtuB with bound colicin E3 R-domain implies a translocon
    • Kurisu G, et al. (2003) The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nat Struct Biol 10:948-954.
    • (2003) Nat Struct Biol , vol.10 , pp. 948-954
    • Kurisu, G.1
  • 10
    • 34249095469 scopus 로고    scopus 로고
    • Structure of colicin i receptor bound to the R-domain of colicin Ia: Implications for protein import
    • Buchanan SK, et al. (2007) Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import. EMBO J 26:2594-2604.
    • (2007) EMBO J , vol.26 , pp. 2594-2604
    • Buchanan, S.K.1
  • 11
    • 34548179597 scopus 로고    scopus 로고
    • Structure of the complex of the colicin E2 R-domain and its BtuB receptor. the outer membrane colicin translocon
    • Sharma O, et al. (2007) Structure of the complex of the colicin E2 R-domain and its BtuB receptor. The outer membrane colicin translocon. J Biol Chem 282:23163-23170.
    • (2007) J Biol Chem , vol.282 , pp. 23163-23170
    • Sharma, O.1
  • 12
    • 1842525243 scopus 로고    scopus 로고
    • Antibiotic-mediated antagonism leads to a bacterial game of rock-paper-scissors in vivo
    • Kirkup BC, RileyMA (2004) Antibiotic-mediated antagonism leads to a bacterial game of rock-paper-scissors in vivo. Nature 428:412-414.
    • (2004) Nature , vol.428 , pp. 412-414
    • Kirkup, B.C.1    Riley, M.A.2
  • 13
    • 0035478958 scopus 로고    scopus 로고
    • Immunity proteins: Enzyme inhibitors that avoid the active site
    • Kleanthous C, Walker D (2001) Immunity proteins: Enzyme inhibitors that avoid the active site. Trends Biochem Sci 26:624-631.
    • (2001) Trends Biochem Sci , vol.26 , pp. 624-631
    • Kleanthous, C.1    Walker, D.2
  • 14
    • 67650553422 scopus 로고    scopus 로고
    • Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation
    • Vankemmelbeke M, et al. (2009) Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation. J Biol Chem 284:18932-18941.
    • (2009) J Biol Chem , vol.284 , pp. 18932-18941
    • Vankemmelbeke, M.1
  • 15
    • 0015132507 scopus 로고
    • Inactivation of ribosomes in vitro by colicin e 3
    • Boon T (1971) Inactivation of ribosomes in vitro by colicin E 3. Proc Natl Acad Sci USA 68:2421-2425.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 2421-2425
    • Boon, T.1
  • 16
    • 77957790848 scopus 로고    scopus 로고
    • Structural basis for ribosomal 16S rRNA cleavage by the cytotoxic domain of colicin E3
    • in press
    • Ng L, et al. (2010) Structural basis for ribosomal 16S rRNA cleavage by the cytotoxic domain of colicin E3. Nat Struct Mol Biol, in press.
    • (2010) Nat Struct Mol Biol
    • Ng, L.1
  • 17
    • 0033605708 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease targeting specific transfer RNA anticodons
    • Ogawa T, et al. (1999) A cytotoxic ribonuclease targeting specific transfer RNA anticodons. Science 283:2097-2100.
    • (1999) Science , vol.283 , pp. 2097-2100
    • Ogawa, T.1
  • 18
    • 0033006298 scopus 로고    scopus 로고
    • Structural and mechanistic basis of immunity toward endonuclease colicins
    • Kleanthous C, et al. (1999) Structural and mechanistic basis of immunity toward endonuclease colicins. Nat Struct Biol 6:243-252.
    • (1999) Nat Struct Biol , vol.6 , pp. 243-252
    • Kleanthous, C.1
  • 19
    • 25444521558 scopus 로고    scopus 로고
    • Cell entry mechanism of enzymatic bacterial colicins: Porin recruitment and the thermodynamics of receptor binding
    • Housden NG, Loftus SR, Moore GR, James R, Kleanthous C (2005) Cell entry mechanism of enzymatic bacterial colicins: Porin recruitment and the thermodynamics of receptor binding. Proc Natl Acad Sci USA 102:13849-13854.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13849-13854
    • Housden, N.G.1    Loftus, S.R.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 20
    • 27144529152 scopus 로고    scopus 로고
    • Tol-Pal proteins are critical cell envelope components of Erwinia chrysanthemi affecting cell morphology and virulence
    • Dubuisson JF, Vianney A, Hugouvieux-Cotte-Pattat N, Lazzaroni JC (2005) Tol-Pal proteins are critical cell envelope components of Erwinia chrysanthemi affecting cell morphology and virulence. Microbiology 151:3337-3347.
    • (2005) Microbiology , vol.151 , pp. 3337-3347
    • Dubuisson, J.F.1    Vianney, A.2    Hugouvieux-Cotte-Pattat, N.3    Lazzaroni, J.C.4
  • 21
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: Going for Baroque?
    • Wiener MC (2005) TonB-dependent outer membrane transport: Going for Baroque? Curr Opin Struct Biol 15:394-400.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 394-400
    • Wiener, M.C.1
  • 22
    • 75149196290 scopus 로고    scopus 로고
    • The colicin Ia receptor, Cir, is also the translocator for colicin Ia
    • Jakes KS, Finkelstein A (2010) The colicin Ia receptor, Cir, is also the translocator for colicin Ia. Mol Microbiol 75:567-578.
    • (2010) Mol Microbiol , vol.75 , pp. 567-578
    • Jakes, K.S.1    Finkelstein, A.2
  • 23
    • 75149123914 scopus 로고    scopus 로고
    • Translocator hunt comes full Cir-Col
    • Kleanthous C (2010) Translocator hunt comes full Cir-Col. Mol Microbiol 75:529-533.
    • (2010) Mol Microbiol , vol.75 , pp. 529-533
    • Kleanthous, C.1
  • 24
    • 40049110400 scopus 로고    scopus 로고
    • Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F
    • Baboolal TG, et al. (2008) Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F. Structure 16:371-379.
    • (2008) Structure , vol.16 , pp. 371-379
    • Baboolal, T.G.1
  • 25
    • 10044257908 scopus 로고    scopus 로고
    • Colicin occlusion of OmpF and TolC channels: Outer membrane translocons for colicin import
    • Zakharov SD, et al. (2004) Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import. Biophys J 87:3901-3911.
    • (2004) Biophys J , vol.87 , pp. 3901-3911
    • Zakharov, S.D.1
  • 26
    • 49149127813 scopus 로고    scopus 로고
    • Crystal structures of the OmpF porin: Function in a colicin translocon
    • Yamashita E, Zhalnina MV, Zakharov SD, Sharma O, Cramer WA (2008) Crystal structures of the OmpF porin: Function in a colicin translocon. EMBO J 27:2171-2180.
    • (2008) EMBO J , vol.27 , pp. 2171-2180
    • Yamashita, E.1    Zhalnina, M.V.2    Zakharov, S.D.3    Sharma, O.4    Cramer, W.A.5
  • 27
    • 33747603486 scopus 로고    scopus 로고
    • Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9
    • Loftus SR, et al. (2006) Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. Proc Natl Acad Sci USA 103:12353-12358.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12353-12358
    • Loftus, S.R.1
  • 28
    • 70349205369 scopus 로고    scopus 로고
    • Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins
    • Bonsor DA, et al. (2009) Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins. EMBO J 28:2846-2857.
    • (2009) EMBO J , vol.28 , pp. 2846-2857
    • Bonsor, D.A.1
  • 29
    • 33748667290 scopus 로고    scopus 로고
    • The colicin E3 outer membrane translocon: Immunity protein release allows interaction of the cytotoxic domain with OmpF porin
    • Zakharov SD, Zhalnina MV, Sharma O, Cramer WA (2006) The colicin E3 outer membrane translocon: Immunity protein release allows interaction of the cytotoxic domain with OmpF porin. Biochemistry 45:10199-10207.
    • (2006) Biochemistry , vol.45 , pp. 10199-10207
    • Zakharov, S.D.1    Zhalnina, M.V.2    Sharma, O.3    Cramer, W.A.4
  • 30
    • 49149127813 scopus 로고    scopus 로고
    • Crystal structures of the OmpF porin: Function in a colicin translocon
    • Yamashita E, Zhalnina MV, Zakharov SD, Sharma O, Cramer WA (2008) Crystal structures of the OmpF porin: Function in a colicin translocon. EMBO J 27:2171-2180.
    • (2008) EMBO J , vol.27 , pp. 2171-2180
    • Yamashita, E.1    Zhalnina, M.V.2    Zakharov, S.D.3    Sharma, O.4    Cramer, W.A.5
  • 31
    • 33846220225 scopus 로고    scopus 로고
    • Minimum length requirement of the flexible N-terminal translocation subdomain of colicin E3
    • Sharma O, Cramer WA (2007) Minimum length requirement of the flexible N-terminal translocation subdomain of colicin E3. J Bacteriol 189:363-368.
    • (2007) J Bacteriol , vol.189 , pp. 363-368
    • Sharma, O.1    Cramer, W.A.2
  • 32
    • 0020267591 scopus 로고
    • The BtuB group col plasmids and homology between the colicins they encode
    • Mock M, Pugsley AP (1982) The BtuB group col plasmids and homology between the colicins they encode. J Bacteriol 150:1069-1076.
    • (1982) J Bacteriol , vol.150 , pp. 1069-1076
    • Mock, M.1    Pugsley, A.P.2
  • 33
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol R 67:593-656.
    • (2003) Microbiol Mol Biol R , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 34
    • 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 2:2006-0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 2006-0008
    • Baba, T.1
  • 35
    • 77954446192 scopus 로고    scopus 로고
    • Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide
    • Apetrei A, et al. (2010) Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide. J Bioenerg Biomembr 42:173-180.
    • (2010) J Bioenerg Biomembr , vol.42 , pp. 173-180
    • Apetrei, A.1
  • 36
    • 52249085709 scopus 로고    scopus 로고
    • The unfoldomics decade: An update on intrinsically disordered proteins
    • Dunker AK, et al. (2008) The unfoldomics decade: An update on intrinsically disordered proteins. BMC Genomics 9(Suppl 2):S1.
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 2
    • Dunker, A.K.1
  • 37
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15:35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 38
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • Radivojac P, et al. (2007) Intrinsic disorder and functional proteomics. Biophys J 92:1439-1456.
    • (2007) Biophys J , vol.92 , pp. 1439-1456
    • Radivojac, P.1
  • 39
    • 59849116258 scopus 로고    scopus 로고
    • Intrinsically unstructured phosphoprotein TSP9 regulates light harvesting in Arabidopsis thaliana
    • Fristedt R, et al. (2009) Intrinsically unstructured phosphoprotein TSP9 regulates light harvesting in Arabidopsis thaliana. Biochemistry 48:499-509.
    • (2009) Biochemistry , vol.48 , pp. 499-509
    • Fristedt, R.1
  • 40
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 42
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK (2008) Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu Rev Biophys 37:215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, MinorW(1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Crystallogr 30:1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 45
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 46
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 47
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375 383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1
  • 48
    • 16644397843 scopus 로고    scopus 로고
    • Developments in the CCP4 molecular-graphics project
    • Potterton L, et al. (2004) Developments in the CCP4 molecular-graphics project. Acta Crystallogr D 60:2288-2294.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2288-2294
    • Potterton, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.