메뉴 건너뛰기




Volumn 179, Issue 4, 1997, Pages 1400-1403

Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; POLYMER; POLYSIALIC ACID;

EID: 0031039494     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.4.1400-1403.1997     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0025284388 scopus 로고
    • Energy coupling in bacterial periplasmic permeases
    • Ames, G. F.-L., and A. K. Joshi. 1990. Energy coupling in bacterial periplasmic permeases. J. Bacteriol. 172:4133-4137.
    • (1990) J. Bacteriol. , vol.172 , pp. 4133-4137
    • Ames, G.F.-L.1    Joshi, A.K.2
  • 2
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G. F.-L., C. S. Mimura, S. R. Holbrook, and V. Shyamala. 1992. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. 65:1-47.
    • (1992) Adv. Enzymol. , vol.65 , pp. 1-47
    • Ames, G.F.-L.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 3
    • 0027475808 scopus 로고
    • The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface
    • Baichwal, V., D. Liu, and G. F.-L. Ames. 1993. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proc. Natl. Acad. Sci. USA 90:620-624.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 620-624
    • Baichwal, V.1    Liu, D.2    Ames, G.F.-L.3
  • 4
    • 0029766843 scopus 로고    scopus 로고
    • Coating the surface: A model for expression of capsular polysialic acid in Escherichia coli K1
    • Bliss, J. M., and R. P. Silver. 1996. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1. Mol. Microbiol. 21:221-231.
    • (1996) Mol. Microbiol. , vol.21 , pp. 221-231
    • Bliss, J.M.1    Silver, R.P.2
  • 5
    • 0029657972 scopus 로고    scopus 로고
    • Polysialic acid export in Escherichia coli K1: The role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation
    • Bliss, J. M., C. F. Garon, and R. P. Silver. 1996. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation. Glycobiology 6:445-452.
    • (1996) Glycobiology , vol.6 , pp. 445-452
    • Bliss, J.M.1    Garon, C.F.2    Silver, R.P.3
  • 6
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and W. Wickner. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78:835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 7
    • 0029561762 scopus 로고
    • SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
    • Economou, A., J. A. Pogliano, J. Beckwith, D. B. Oliver, and W. Wickner. 1995. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell 83:1171-1181.
    • (1995) Cell , vol.83 , pp. 1171-1181
    • Economou, A.1    Pogliano, J.A.2    Beckwith, J.3    Oliver, D.B.4    Wickner, W.5
  • 8
    • 0025362726 scopus 로고
    • The role of ATP in binding-protein-dependent transport systems
    • Higgins, C. F. 1990. The role of ATP in binding-protein-dependent transport systems. Res. Microbiol. 141:353-360.
    • (1990) Res. Microbiol. , vol.141 , pp. 353-360
    • Higgins, C.F.1
  • 9
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 10
    • 77957010716 scopus 로고
    • Bacterial membranes
    • Kaback, H. R. 1971. Bacterial membranes. Methods Enzymol. 22:99-120.
    • (1971) Methods Enzymol. , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 11
    • 0026786329 scopus 로고
    • Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease: Comparison with other members of the family
    • Kerppola, R. E., and G. F.-L. Ames. 1992. Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease: comparison with other members of the family. J. Biol. Chem. 267:2329-2336.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2329-2336
    • Kerppola, R.E.1    Ames, G.F.-L.2
  • 12
    • 0025874251 scopus 로고
    • The membrane-bound proteins of periplasmic permeases form a complex: Identification of the histidine permease HisQMP complex
    • Kerppola, R. E., V. K. Shyamala, P. Klebba, and G. F.-L. Ames. 1991. The membrane-bound proteins of periplasmic permeases form a complex: identification of the histidine permease HisQMP complex. J. Biol. Chem. 266:9857-9865.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9857-9865
    • Kerppola, R.E.1    Shyamala, V.K.2    Klebba, P.3    Ames, G.F.-L.4
  • 13
    • 0027956170 scopus 로고
    • SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state
    • Kim, Y. J., T. Rajapandi, and D. Oliver. 1994. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell 78:845-853.
    • (1994) Cell , vol.78 , pp. 845-853
    • Kim, Y.J.1    Rajapandi, T.2    Oliver, D.3
  • 14
    • 0027488666 scopus 로고
    • Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
    • Mitchell, C., and D. Oliver. 1993. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol. Microbiol. 10:483-497.
    • (1993) Mol. Microbiol. , vol.10 , pp. 483-497
    • Mitchell, C.1    Oliver, D.2
  • 15
    • 0025152680 scopus 로고
    • The role of bacterial polysaccharide capsules as virulence factors
    • Moxon, E. R., and J. S. Kroll. 1990. The role of bacterial polysaccharide capsules as virulence factors. Curr. Top. Microbiol. Immunol. 150:65-85.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.150 , pp. 65-85
    • Moxon, E.R.1    Kroll, J.S.2
  • 16
    • 0025885026 scopus 로고
    • Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1
    • Pavelka, M. S., Jr., L. F. Wright, and R. P. Silver. 1991. Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1. J. Bacteriol. 173:4603-4610.
    • (1991) J. Bacteriol. , vol.173 , pp. 4603-4610
    • Pavelka Jr., M.S.1    Wright, L.F.2    Silver, R.P.3
  • 17
    • 0027931373 scopus 로고
    • Characterization of KpsT, the ATP-binding component of the ABC-transporter involved with the export of capsular polysialic acid in Escherichia coli K1
    • Pavelka, M. S., Jr., S. F. Hayes, and R. P. Silver. 1994. Characterization of KpsT, the ATP-binding component of the ABC-transporter involved with the export of capsular polysialic acid in Escherichia coli K1. J. Biol. Chem. 269:20149-20158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20149-20158
    • Pavelka Jr., M.S.1    Hayes, S.F.2    Silver, R.P.3
  • 18
    • 0024604620 scopus 로고
    • Reconstitution of the histidine periplasmic transport system in membrane vesicles: Energy coupling and interaction between the binding protein and the membrane complex
    • Prossnitz, E., A. Gee, and G. F.-L. Ames. 1989. Reconstitution of the histidine periplasmic transport system in membrane vesicles: energy coupling and interaction between the binding protein and the membrane complex. J. Biol. Chem. 264:5006-5014.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5006-5014
    • Prossnitz, E.1    Gee, A.2    Ames, G.F.-L.3
  • 19
    • 0028799110 scopus 로고
    • Bacterial polysaccharides in sickness and in health
    • Roberts, I. S. 1995. Bacterial polysaccharides in sickness and in health. Microbiology 141:2023-2031.
    • (1995) Microbiology , vol.141 , pp. 2023-2031
    • Roberts, I.S.1
  • 20
    • 0029092262 scopus 로고
    • The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane
    • Schneider, E., S. Hunke, and S. Tebbe. 1995. The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane. J. Bacteriol. 177:5364-5367.
    • (1995) J. Bacteriol. , vol.177 , pp. 5364-5367
    • Schneider, E.1    Hunke, S.2    Tebbe, S.3
  • 21
    • 0025084040 scopus 로고
    • Molecular analysis of the Escherichia coli K5 kps locus: Identification and characterization of an inner-membrane capsular polysaccharide transport system
    • Smith, A. N., G. J. Boulnois, and I. S. Roberts. 1990. Molecular analysis of the Escherichia coli K5 kps locus: identification and characterization of an inner-membrane capsular polysaccharide transport system. Mol. Microbiol. 4:1863-1869.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1863-1869
    • Smith, A.N.1    Boulnois, G.J.2    Roberts, I.S.3
  • 22
    • 0018287494 scopus 로고
    • Role of a membranous sialyltransferase complex in the synthesis of surface polymers containing polysialic acid in Escherichia coli
    • Troy, F. A., and M. A. McCloskey. 1979. Role of a membranous sialyltransferase complex in the synthesis of surface polymers containing polysialic acid in Escherichia coli. J. Biol. Chem. 254:7377-7387.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7377-7387
    • Troy, F.A.1    McCloskey, M.A.2
  • 23
    • 0029589562 scopus 로고
    • Biosynthesis of the polysialic acid capsule in Escherichia coli K1
    • Vimr, E., S. Steenbergen, and M. Cieslewicz. 1995. Biosynthesis of the polysialic acid capsule in Escherichia coli K1. J. Industr. Microbiol. 15:352-360.
    • (1995) J. Industr. Microbiol. , vol.15 , pp. 352-360
    • Vimr, E.1    Steenbergen, S.2    Cieslewicz, M.3
  • 24
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- And β- subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β- subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 8:945-951.
    • (1982) EMBO J. , vol.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 25
    • 0025012599 scopus 로고
    • Biosynthesis of the polysialic acid capsule in Escherichia coli K1 : The endogenous acceptor of polysialic acid is a membrane protein of 20 kDa
    • Weisgerber, C., and F. A. Troy. 1990. Biosynthesis of the polysialic acid capsule in Escherichia coli K1 : the endogenous acceptor of polysialic acid is a membrane protein of 20 kDa. J. Biol. Chem. 265:1578-1587.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1578-1587
    • Weisgerber, C.1    Troy, F.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.