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Volumn 62, Issue 4, 2006, Pages 1064-1075

A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; DETERGENT; ESCHERICHIA COLI PROTEIN; LIPOPROTEIN; MAGNESIUM; MUTANT PROTEIN; PROTEIN LOLCDE; UNCLASSIFIED DRUG;

EID: 33750454808     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05378.x     Document Type: Article
Times cited : (39)

References (49)
  • 1
    • 0029045244 scopus 로고
    • Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli
    • Bouveret, E., Derouiche, R., Rigal, A., Lloubes, R., Lazdunski, C., and Benedetti, H. (1995) Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli. J Biol Chem 270: 11071-11077.
    • (1995) J Biol Chem , vol.270 , pp. 11071-11077
    • Bouveret, E.1    Derouiche, R.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Benedetti, H.6
  • 2
    • 0016748566 scopus 로고
    • Covalent lipoprotein from the outer membrane of Escherichia coli
    • Braun, V. (1975) Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim Biophys Acta 415: 335-377.
    • (1975) Biochim Biophys Acta , vol.415 , pp. 335-377
    • Braun, V.1
  • 3
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., Lu, G., Lin, J., Davidson, A.L., and Quiocho, F.A. (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 12: 651-661.
    • (2003) Mol Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 4
    • 0023874147 scopus 로고
    • A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: Application to lens ATPases
    • Chifflet, S., Torriglia, A., Chiesa, R., and Tolosa, S. (1988) A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases. Anal Biochem 168: 1-4.
    • (1988) Anal Biochem , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 5
    • 33645215647 scopus 로고    scopus 로고
    • ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter
    • Daus, M.L., Landmesser, H., Schlosser, A., Muller, P., Herrmann, A., and Schneider, E. (2006) ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter. J Biol Chem 281: 3856-3865.
    • (2006) J Biol Chem , vol.281 , pp. 3856-3865
    • Daus, M.L.1    Landmesser, H.2    Schlosser, A.3    Muller, P.4    Herrmann, A.5    Schneider, E.6
  • 6
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A.L., and Chen, J. (2004) ATP-binding cassette transporters in bacteria. Annu Rev Biochem 73: 241-268.
    • (2004) Annu Rev Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 7
    • 0037044719 scopus 로고    scopus 로고
    • Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals
    • Fukuda, A., Matsuyama, S., Hara, T., Nakayama, J., Nagasawa, H., and Tokuda, H. (2002) Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals. J Biol Chem 277: 43512-43518.
    • (2002) J Biol Chem , vol.277 , pp. 43512-43518
    • Fukuda, A.1    Matsuyama, S.2    Hara, T.3    Nakayama, J.4    Nagasawa, H.5    Tokuda, H.6
  • 8
    • 0141890241 scopus 로고    scopus 로고
    • Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals
    • Hara, T., Matsuyama, S., and Tokuda, H. (2003) Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals. J Biol Chem 278: 40408-40414.
    • (2003) J Biol Chem , vol.278 , pp. 40408-40414
    • Hara, T.1    Matsuyama, S.2    Tokuda, H.3
  • 9
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins, C.F., and Linton, K.J. (2004) The ATP switch model for ABC transporters. Nat Struct Mol Biol 11: 918-926.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 10
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I.B., and Blight, M.A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J Mol Biol 293: 381-399.
    • (1999) J Mol Biol , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 11
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K.P., Karcher, A., Shin, D.S., Craig, L., Arthur, L.M., Carney, J.P., and Tainer, J.A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101: 789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 12
    • 0034700252 scopus 로고    scopus 로고
    • Non-equivalence of the nucleotide-binding subunits of an ABC transporter, the histidine permease, and conformational changes in the membrane complex
    • Kreimer, D.I., Chai, K.P., and Ames, G.F.-L. (2000) Non-equivalence of the nucleotide-binding subunits of an ABC transporter, the histidine permease, and conformational changes in the membrane complex. Biochemistry 39: 14183-14195.
    • (2000) Biochemistry , vol.39 , pp. 14183-14195
    • Kreimer, D.I.1    Chai, K.P.2    Ames, G.F.-L.3
  • 13
    • 0035831524 scopus 로고    scopus 로고
    • Walker a lysine mutations of TAP1 and TAP2 interfere with peptide translocation but not peptide binding
    • Lapinski, P.E., Neubig, R.R., and Raghavan, M. (2001) Walker A lysine mutations of TAP1 and TAP2 interfere with peptide translocation but not peptide binding. J Biol Chem 276: 7526-7533.
    • (2001) J Biol Chem , vol.276 , pp. 7526-7533
    • Lapinski, P.E.1    Neubig, R.R.2    Raghavan, M.3
  • 14
    • 0037474237 scopus 로고    scopus 로고
    • Intermediate structural states involved in MRP1-mediated drug transport. Role of glutathione
    • Manciu, L., Chang, X.B., Buyse, F., Hou, Y.X., Gustot, A., Riordan, J.R., and Ruysschaert, J.M. (2003) Intermediate structural states involved in MRP1-mediated drug transport. Role of glutathione. J Biol Chem 278: 3347-3356.
    • (2003) J Biol Chem , vol.278 , pp. 3347-3356
    • Manciu, L.1    Chang, X.B.2    Buyse, F.3    Hou, Y.X.4    Gustot, A.5    Riordan, J.R.6    Ruysschaert, J.M.7
  • 15
    • 0035853856 scopus 로고    scopus 로고
    • Demonstration of conformational changes associated with activation of the maltose transport complex
    • Mannering, D.E., Sharma, S., and Davidson, A.L. (2001) Demonstration of conformational changes associated with activation of the maltose transport complex. J Biol Chem 276: 12362-12368.
    • (2001) J Biol Chem , vol.276 , pp. 12362-12368
    • Mannering, D.E.1    Sharma, S.2    Davidson, A.L.3
  • 17
    • 0035951073 scopus 로고    scopus 로고
    • The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein
    • Martin, C., Higgins, C.F., and Callaghan, R. (2001) The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein. Biochemistry 40: 15733-15742.
    • (2001) Biochemistry , vol.40 , pp. 15733-15742
    • Martin, C.1    Higgins, C.F.2    Callaghan, R.3
  • 18
    • 0037188471 scopus 로고    scopus 로고
    • Elucidation of the function of lipoprotein-sorting signals that determine membrane localization
    • Masuda, K., Matsuyama, S., and Tokuda, H. (2002) Elucidation of the function of lipoprotein-sorting signals that determine membrane localization. Proc Natl Acad Sci USA 99: 7390-7395.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7390-7395
    • Masuda, K.1    Matsuyama, S.2    Tokuda, H.3
  • 19
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama, S., Tajima, T., and Tokuda, H. (1995) A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J 14: 3365-3372.
    • (1995) EMBO J , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 20
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama, S., Yokota, N., and Tokuda, H. (1997) A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J 16: 6947-6955.
    • (1997) EMBO J , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 21
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in the quality control of Escherichia coli periplasm
    • Miyadai, H., Tanaka-Masuda, K., Matsuyama, S., and Tokuda, H. (2004) Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in the quality control of Escherichia coli periplasm. J Biol Chem 279: 39807-39813.
    • (2004) J Biol Chem , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.3    Tokuda, H.4
  • 22
    • 0037174123 scopus 로고    scopus 로고
    • Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE
    • Miyamoto, A., Matsuyama, S., and Tokuda, H. (2002) Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE. FEBS Lett 528: 193-196.
    • (2002) FEBS Lett , vol.528 , pp. 193-196
    • Miyamoto, A.1    Matsuyama, S.2    Tokuda, H.3
  • 23
    • 0021307433 scopus 로고
    • Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli
    • Mizushima, S. (1984) Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli. Mol Cell Biochem 60: 5-15.
    • (1984) Mol Cell Biochem , vol.60 , pp. 5-15
    • Mizushima, S.1
  • 24
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J.E., Millen, L., Binns, D., Hunt, J.F., and Thomas, P.J. (2002) Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J Biol Chem 277: 21111-21114.
    • (2002) J Biol Chem , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 25
    • 0030026629 scopus 로고    scopus 로고
    • Altered drug-stimulated ATPase activity in mutants of the human multidrug resistance protein
    • Müller, M., Bakos, E., Welker, E., Varadi, A., Germann, U.A., Gottesman, M.M., et al. (1996) Altered drug-stimulated ATPase activity in mutants of the human multidrug resistance protein. J Biol Chem 271: 1877-1883.
    • (1996) J Biol Chem , vol.271 , pp. 1877-1883
    • Müller, M.1    Bakos, E.2    Welker, E.3    Varadi, A.4    Germann, U.A.5    Gottesman, M.M.6
  • 26
    • 0036175948 scopus 로고    scopus 로고
    • Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane
    • Narita, S., Tanaka, K., Matsuyama, S., and Tokuda, H. (2002) Disruption of lolCDE, encoding an ATP-binding cassette transporter, is lethal for Escherichia coli and prevents release of lipoproteins from the inner membrane. J Bacteriol 184: 1417-1422.
    • (2002) J Bacteriol , vol.184 , pp. 1417-1422
    • Narita, S.1    Tanaka, K.2    Matsuyama, S.3    Tokuda, H.4
  • 27
    • 0029416964 scopus 로고
    • Preferential interaction of Sec-G with Sec-E stabilizes an unstable Sec-E derivative in the Escherichia coli cytoplasmic membrane
    • Nishiyama, K., Mizushima, S., and Tokuda, H. (1995) Preferential interaction of Sec-G with Sec-E stabilizes an unstable Sec-E derivative in the Escherichia coli cytoplasmic membrane. Biochem Biophys Res Commun 217: 217-223.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 217-223
    • Nishiyama, K.1    Mizushima, S.2    Tokuda, H.3
  • 28
    • 0141755312 scopus 로고    scopus 로고
    • Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)
    • Payen, L.F., Gao, M., Westlake, C.J., Cole, S.P., and Deeley, R.G. (2003) Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1). J Biol Chem 278: 38537-38547.
    • (2003) J Biol Chem , vol.278 , pp. 38537-38547
    • Payen, L.F.1    Gao, M.2    Westlake, C.J.3    Cole, S.P.4    Deeley, R.G.5
  • 29
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu, Q., Russell, P.L., and Sharom, F.J. (2003) Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle. Biochemistry 42: 1170-1177.
    • (2003) Biochemistry , vol.42 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 30
    • 17944370228 scopus 로고    scopus 로고
    • Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle
    • Rosenberg, M.F., Velarde, G., Ford, R.C., Martin, C., Berridge, G., Kerr, I.D., et al. (2001) Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle. EMBO J 20: 5615-5625.
    • (2001) EMBO J , vol.20 , pp. 5615-5625
    • Rosenberg, M.F.1    Velarde, G.2    Ford, R.C.3    Martin, C.4    Berridge, G.5    Kerr, I.D.6
  • 31
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., and Wu, H.C. (1994) Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J Biol Chem 269: 19701-19706.
    • (1994) J Biol Chem , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 32
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • Seydel, A., Gounon, P., and Pugsley, A.P. (1999) Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection. Mol Microbiol 34: 810-821.
    • (1999) Mol Microbiol , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 33
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P.C., Karpowich, N., Millen, L., Moody, J.E., Rosen, J., Thomas, P.J., and Hunt, J.F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10: 139-149.
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 34
    • 0033580854 scopus 로고    scopus 로고
    • Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis
    • Sonveaux, N., Vigano, C., Shapiro, A.B., Ling, V., and Ruysschaert, J.M. (1999) Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein. A tryptophan fluorescence quenching analysis. J Biol Chem 274: 17649-17654.
    • (1999) J Biol Chem , vol.274 , pp. 17649-17654
    • Sonveaux, N.1    Vigano, C.2    Shapiro, A.B.3    Ling, V.4    Ruysschaert, J.M.5
  • 35
    • 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., and Miki, K. (2003) Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J 22: 3199-3209.
    • (2003) EMBO J , vol.22 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4    Tokuda, H.5    Miki, K.6
  • 36
    • 27144449975 scopus 로고    scopus 로고
    • Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed β-barrel structures
    • Taniguchi, N., Matsuyama, S., and Tokuda, H. (2005) Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed β-barrel structures. J Biol Chem 280: 34481-34488.
    • (2005) J Biol Chem , vol.280 , pp. 34481-34488
    • Taniguchi, N.1    Matsuyama, S.2    Tokuda, H.3
  • 37
    • 0035861554 scopus 로고    scopus 로고
    • Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli
    • Terada, M., Kuroda, T., Matsuyama, S., and Tokuda, H. (2001) Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli. J Biol Chem 276: 47690-47694.
    • (2001) J Biol Chem , vol.276 , pp. 47690-47694
    • Terada, M.1    Kuroda, T.2    Matsuyama, S.3    Tokuda, H.4
  • 38
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • Tikhonova, E.B., and Zgurskaya, H.I. (2004) AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex. J Biol Chem 279: 32116-32124.
    • (2004) J Biol Chem , vol.279 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 39
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda, H., and Matsuyama, S. (2004) Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 1693: 5-13.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 40
    • 0025074071 scopus 로고
    • Reconstitution of translocation activity for secretory proteins from solubilized components of Escherichia coli
    • Tokuda, H., Shiozuka, K., and Mizushima, S. (1990) Reconstitution of translocation activity for secretory proteins from solubilized components of Escherichia coli. Eur J Biochem 192: 583-589.
    • (1990) Eur J Biochem , vol.192 , pp. 583-589
    • Tokuda, H.1    Shiozuka, K.2    Mizushima, S.3
  • 41
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • Verdon, G., Albers, S.V., Dijkstra, B.W., Driessen, A.J.M., and Thunnissen, A.-M.M.H. (2003) Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J Mol Biol 330: 343-358.
    • (2003) J Mol Biol , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.M.4    Thunnissen, A.-M.M.H.5
  • 42
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis
    • Vigano, C., Margolles, A., van Veen, H.W., Konings, W.N., and Ruysschaert, J.M. (2000) Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis. J Biol Chem 275: 10962-10967.
    • (2000) J Biol Chem , vol.275 , pp. 10962-10967
    • Vigano, C.1    Margolles, A.2    Van Veen, H.W.3    Konings, W.N.4    Ruysschaert, J.M.5
  • 43
    • 4344592803 scopus 로고    scopus 로고
    • Dynamics of ATP-binding cassette contribute to allosteric control, nucleotide binding and energy transduction in ABC transporters
    • Wang, C., Karpowich, N., Hunt, J.F., Rance, M., and Palmer, A.G. (2004) Dynamics of ATP-binding cassette contribute to allosteric control, nucleotide binding and energy transduction in ABC transporters. J Mol Biol 342: 525-537.
    • (2004) J Mol Biol , vol.342 , pp. 525-537
    • Wang, C.1    Karpowich, N.2    Hunt, J.F.3    Rance, M.4    Palmer, A.G.5
  • 44
    • 0032484007 scopus 로고    scopus 로고
    • LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate
    • Yakushi, T., Yokota, N., Matsuyama, S., and Tokuda, H. (1998) LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate. J Biol Chem 273: 32576-32581.
    • (1998) J Biol Chem , vol.273 , pp. 32576-32581
    • Yakushi, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 45
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi, T., Masuda, K., Narita, S., Matsuyama, S., and Tokuda, H. (2000) A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2: 212-218.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 46
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K., Yu, F., and Inouye, M. (1988) A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell 53: 423-432.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 47
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 48
    • 0032742815 scopus 로고    scopus 로고
    • Characterization of the LolA-LolB system as the general lipoprotein localization mechanism of Escherichia coli
    • Yokota, N., Kuroda, T., Matsuyama, S., and Tokuda, H. (1999) Characterization of the LolA-LolB system as the general lipoprotein localization mechanism of Escherichia coli. J Biol Chem 274: 30995-30999.
    • (1999) J Biol Chem , vol.274 , pp. 30995-30999
    • Yokota, N.1    Kuroda, T.2    Matsuyama, S.3    Tokuda, H.4
  • 49
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • Yuan, Y.R., Blecker, S., Martsinkevich, O., Millen, L., Thomas, P.J., and Hunt, J.F. (2001) The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. J Biol Chem 276: 32313-32321.
    • (2001) J Biol Chem , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6


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