메뉴 건너뛰기




Volumn 180, Issue 9, 1998, Pages 2507-2514

Exploring the role of integral membrane proteins in ATP-binding cassette transporters: Analysis of a collection of MAlG insertion mutants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; MALTOSE BINDING PROTEIN; MEMBRANE PROTEIN;

EID: 0031968765     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.9.2507-2514.1998     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0029868045 scopus 로고    scopus 로고
    • Conserved domains in the N-and C-terminal domains of integral membrane transporter FhuB define sites important for intra- and intermolecular interactions
    • Böhm, B., H. Boschert, and W. Köster. 1996. Conserved domains in the N-and C-terminal domains of integral membrane transporter FhuB define sites important for intra-and intermolecular interactions. Mol. Microbiol. 20:223-232.
    • (1996) Mol. Microbiol. , vol.20 , pp. 223-232
    • Böhm, B.1    Boschert, H.2    Köster, W.3
  • 4
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, R. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.) ASM Press, Washington, D.C.
    • Boos, W., and J. M. Lucht. 1996. Periplasmic binding protein-dependent ABC transporters, p. 1175-1209. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, R. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 6
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd, D., B. Traxler, and J. Beckwith. 1993. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol. 175:553-556.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 7
    • 0028347539 scopus 로고
    • Mutations that alter the transmembrane signaling pathway in an ATP binding cassette (ABC) transporter
    • Covitz, K.-M. Y., C. H. Panagiotidis, L.-I. Hor, M. Reyes, N. A. Treptow, and H. A. Shuman. 1994. Mutations that alter the transmembrane signaling pathway in an ATP binding cassette (ABC) transporter. EMBO J. 13:1752-1759.
    • (1994) EMBO J. , vol.13 , pp. 1752-1759
    • Covitz, K.-M.Y.1    Panagiotidis, C.H.2    Hor, L.-I.3    Reyes, M.4    Treptow, N.A.5    Shuman, H.A.6
  • 8
    • 0027510078 scopus 로고
    • Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli
    • Dassa, E. 1993. Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli. Mol. Microbiol. 7:39-47.
    • (1993) Mol. Microbiol. , vol.7 , pp. 39-47
    • Dassa, E.1
  • 9
    • 0022125681 scopus 로고
    • Sequence of gene malG in E. coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and M. Hofnung. 1985. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 4:2287-2293.
    • (1985) EMBO J. , vol.4 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 10
    • 0027396907 scopus 로고
    • Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli
    • Dassa, E., and S. Muir. 1993. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7:29-38.
    • (1993) Mol. Microbiol. , vol.7 , pp. 29-38
    • Dassa, E.1    Muir, S.2
  • 11
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from E. coli
    • Davidson, A., and H. Nikaido. 1991. Purification and characterization of the membrane-associated components of the maltose transport system from E. coli. J. Biol. Chem. 266:8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.1    Nikaido, H.2
  • 12
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A. L., H. A. Shuman, and H. Nikaido. 1992. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. USA 89:2360-2364.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 13
    • 0029975122 scopus 로고    scopus 로고
    • Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis
    • Ehrle, R., C. Pick, R. Ulrich, E. Hofmann, and M. Ehrmann. 1996. Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis. J. Bacteriol. 178:2255-2262.
    • (1996) J. Bacteriol. , vol.178 , pp. 2255-2262
    • Ehrle, R.1    Pick, C.2    Ulrich, R.3    Hofmann, E.4    Ehrmann, M.5
  • 14
    • 0025052350 scopus 로고
    • Genetic analysis of membrane protein topology by a sandwich gene fusion approach
    • Ehrmann, M., D. Boyd, and J. Beckwith. 1990. Genetic analysis of membrane protein topology by a sandwich gene fusion approach. Proc. Natl. Acad. Sci. USA 87:7574-7578.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7574-7578
    • Ehrmann, M.1    Boyd, D.2    Beckwith, J.3
  • 15
    • 0029164287 scopus 로고
    • The ABC of channel regulation
    • Higgins, C. F. 1995. The ABC of channel regulation. Cell 82:693-696.
    • (1995) Cell , vol.82 , pp. 693-696
    • Higgins, C.F.1
  • 17
    • 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. 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.2
  • 18
    • 0031039347 scopus 로고    scopus 로고
    • MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants
    • Lippincott, J., and B. Traxler. 1997. MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants. J. Bacteriol. 179:1337-1343.
    • (1997) J. Bacteriol. , vol.179 , pp. 1337-1343
    • Lippincott, J.1    Traxler, B.2
  • 19
    • 0031588907 scopus 로고    scopus 로고
    • A simple screen for permissive sites in proteins. Analysis of Escherichia coli lac permease
    • Manoil, C., and J. Bailey. 1997. A simple screen for permissive sites in proteins. Analysis of Escherichia coli lac permease. J. Mol. Biol. 267:250-263.
    • (1997) J. Mol. Biol. , vol.267 , pp. 250-263
    • Manoil, C.1    Bailey, J.2
  • 20
    • 0029610258 scopus 로고
    • Membrane protein assembly: Genetic, evolutionary and medical perspectives
    • Manoil, C., and B. Traxler. 1995. Membrane protein assembly: genetic, evolutionary and medical perspectives. Annu. Rev. Genet. 29:131-150.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 131-150
    • Manoil, C.1    Traxler, B.2
  • 21
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 22
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., M. Hofnung, and E. Dassa. 1997. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16:3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 24
    • 0030945611 scopus 로고    scopus 로고
    • Insertion mutagenesis of the lac repressor and its implications for structure-function analysis
    • Nelson, B. D., C. Manoil, and B. Traxler. 1997. Insertion mutagenesis of the lac repressor and its implications for structure-function analysis. J. Bacteriol. 179:3721-3728.
    • (1997) J. Bacteriol. , vol.179 , pp. 3721-3728
    • Nelson, B.D.1    Manoil, C.2    Traxler, B.3
  • 25
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido, H. 1994. Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett. 346:55-58.
    • (1994) FEBS Lett. , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 26
    • 0027375813 scopus 로고
    • Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter
    • Panagiotidis, C. H., M. Reyes, A. Sievertsen, W. Boos, and H. A. Shuman. 1993. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. J. Biol. Chem. 268:23685-23696.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23685-23696
    • Panagiotidis, C.H.1    Reyes, M.2    Sievertsen, A.3    Boos, W.4    Shuman, H.A.5
  • 27
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J.-L., and D. M. Engelman. 1990. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 29
    • 0028240216 scopus 로고
    • Bacterial binding protein-dependent permeases: Characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins
    • Saurin, W., W. Köster, and E. Dassa. 1994. Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins. Mol. Microbiol. 12:993-1004.
    • (1994) Mol. Microbiol. , vol.12 , pp. 993-1004
    • Saurin, W.1    Köster, W.2    Dassa, E.3
  • 30
    • 0029883155 scopus 로고    scopus 로고
    • Characterization and analysis of conserved motifs in a peroxisomal ATP-binding cassette transporter
    • Shani, N., A. Sapag, and D. Valle. 1996. Characterization and analysis of conserved motifs in a peroxisomal ATP-binding cassette transporter. J. Biol. Chem. 271:8725-8730.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8725-8730
    • Shani, N.1    Sapag, A.2    Valle, D.3
  • 31
    • 0027763278 scopus 로고
    • Tinkering with transporters: Periplasmic binding protein-dependent maltose transport in E. coli
    • Shuman, H. A. and C. H. Panagiotidis. 1993. Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli. J. Bioenerg. Biomembr. 25:613-620.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 613-620
    • Shuman, H.A.1    Panagiotidis, C.H.2
  • 32
    • 0026469992 scopus 로고
    • Assembly of a hetero-oligomeric membrane protein complex
    • Traxler, B., and J. Beckwith. 1992. Assembly of a hetero-oligomeric membrane protein complex. Proc. Natl. Acad. Sci. USA 89:10852-10856.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10852-10856
    • Traxler, B.1    Beckwith, J.2
  • 33
    • 0022259474 scopus 로고
    • Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system
    • Treptow, N. A., and H. A. Shuman. 1985. Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J. Bacteriol. 163:654-660.
    • (1985) J. Bacteriol. , vol.163 , pp. 654-660
    • Treptow, N.A.1    Shuman, H.A.2
  • 34
    • 0023787957 scopus 로고
    • Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system
    • Treptow, N. A., and H. A. Shuman. 1988. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J. Mol. Biol. 202:809-822.
    • (1988) J. Mol. Biol. , vol.202 , pp. 809-822
    • Treptow, N.A.1    Shuman, H.A.2
  • 35
    • 0030988015 scopus 로고    scopus 로고
    • Biophysical aspects of P-glycoprotein-mediated multidrug resistance
    • Wadkins, R. M., and P. D. Roepe. 1997. Biophysical aspects of P-glycoprotein-mediated multidrug resistance. Int. Rev. Cytol. 171:121-165.
    • (1997) Int. Rev. Cytol. , vol.171 , pp. 121-165
    • Wadkins, R.M.1    Roepe, P.D.2
  • 36
    • 0029616734 scopus 로고
    • Cystic fibrosis: Genotypic and phenotypic variations
    • Zielenski, J., and L. C. Tsui. 1995. Cystic fibrosis: genotypic and phenotypic variations. Annu. Rev. Genet. 29:777-807.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 777-807
    • Zielenski, J.1    Tsui, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.