메뉴 건너뛰기




Volumn 181, Issue 7, 1999, Pages 2267-2272

Structure-function study of MalF protein by random mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; MALTODEXTRIN; MALTOSE;

EID: 0032963083     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.7.2267-2272.1999     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • Boos, W., and H. Shuman. 1998. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62: 204-229.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, A.H.2
  • 2
    • 0022911351 scopus 로고
    • Mutagenesis by random linker insertion into the lamB gene of E. coli K12
    • Boulain, J. C., A. Charbit, and M. Hofnung. 1986. Mutagenesis by random linker insertion into the lamB gene of E. coli K12. Mol. Gen. Genet. 205:339-348.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 339-348
    • Boulain, J.C.1    Charbit, A.2    Hofnung, M.3
  • 3
    • 0024372724 scopus 로고
    • Positively charged amino acid residues can act as topogenic determinants in membrane proteins
    • Boyd, D., and J. Beckwith. 1989. Positively charged amino acid residues can act as topogenic determinants in membrane proteins. Proc. Natl. Acad. Sci. USA 86:9446-9450.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9446-9450
    • Boyd, D.1    Beckwith, A.J.2
  • 4
    • 0028347539 scopus 로고
    • Mutations that alter the transmembrane signalling 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 signalling 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
  • 5
    • 0024712936 scopus 로고
    • Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: A potential new regulatory site in the interoperonic region
    • Dahl, M. K., E. Francoz, W. Saurin, W. Boos, M. D. Manson, and M. Hofnung. 1989. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Mol. Gen. Genet. 218:199-207.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 199-207
    • Dahl, M.K.1    Francoz, E.2    Saurin, W.3    Boos, W.4    Manson, M.D.5    Hofnung, M.6
  • 6
    • 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
  • 7
    • 0022125681 scopus 로고
    • Sequence of malG gene in E. coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and M. Hofnung. 1985. Sequence of malG gene 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
  • 8
    • 0017519960 scopus 로고
    • Outer membrane proteins of Escherichia coli. V. Evidence that protein 1 and bacteriophage-directed protein 2 are different polypeptides
    • Diedrich, D. L., A. O. Summers, and C. A. Schnaitman. 1977. Outer membrane proteins of Escherichia coli. V. Evidence that protein 1 and bacteriophage-directed protein 2 are different polypeptides. J. Bacteriol. 131:598-607.
    • (1977) J. Bacteriol. , vol.131 , pp. 598-607
    • Diedrich, D.L.1    Summers, A.O.2    Schnaitman, C.A.3
  • 9
    • 0023274512 scopus 로고
    • Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose
    • Duplay, P., S. Szmelcman, H. Bedouelle, and M. Hofnung. 1987. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose. J. Mol. Biol. 194:563-673.
    • (1987) J. Mol. Biol. , vol.194 , pp. 563-673
    • Duplay, P.1    Szmelcman, S.2    Bedouelle, H.3    Hofnung, M.4
  • 10
    • 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
  • 11
    • 0025947624 scopus 로고
    • Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal
    • Ehrmann, M., and J. Beckwith. 1991. Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J. Biol. Chem. 266:16530-16533.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16530-16533
    • Ehrmann, M.1    Beckwith, J.2
  • 12
    • 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
  • 13
    • 0021161867 scopus 로고
    • Nucleotide sequence of the gene for malf protein, an inner membrane component of the maltose transport system
    • Froshauer, S., and J. Beckwith. 1984. Nucleotide sequence of the gene for MalF protein, an inner membrane component of the maltose transport system. J. Biol. Chem. 259:10896-10903.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10896-10903
    • Froshauer, S.1    Beckwith, A.J.2
  • 14
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of E. coli
    • Froshauer, S., G. N. Green, D. Boyd, K. McGovern, and J. Beckwith. 1988. Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of E. coli. J. Mol. Biol. 200:501-511.
    • (1988) J. Mol. Biol. , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 15
    • 0025252193 scopus 로고
    • Solubilization of native membrane proteins
    • Hjelmeland, L. M. 1990. Solubilization of native membrane proteins. Methods Enzymol. 182:253-264.
    • (1990) Methods Enzymol. , vol.182 , pp. 253-264
    • Hjelmeland, L.M.1
  • 16
    • 0027490784 scopus 로고
    • Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli - Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK(2) membrane transport complex
    • Hor, L. I., and H. A. Shuman. 1993. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli - each lobe of maltose-binding protein interacts with a different subunit of the MalFGK(2) membrane transport complex. J. Mol. Biol. 233:659-670.
    • (1993) J. Mol. Biol. , vol.233 , pp. 659-670
    • Hor, L.I.1    Shuman, H.A.2
  • 17
    • 0031888811 scopus 로고    scopus 로고
    • Archaeal binding protein-dependent ABC transporter: Molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Horlacher, R., K. B. Xavier, H. Santos, J. DiRuggiero, M. Kossmann, and W. Boos. 1998. Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180:680-689.
    • (1998) J. Bacteriol. , vol.180 , pp. 680-689
    • Horlacher, R.1    Xavier, K.B.2    Santos, H.3    Diruggiero, J.4    Kossmann, M.5    Boos, W.6
  • 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
    • 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
  • 20
    • 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. 16:2066-2077.
    • (1997) EMBO J. , vol.16 , pp. 2066-2077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 21
    • 0030695203 scopus 로고    scopus 로고
    • Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli
    • Mourez, M., S. Skouloubris, J. M. Betton, and E. Dassa. 1997 Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli. Mol. Microbiol. 26:821-831.
    • (1997) Mol. Microbiol. , vol.26 , pp. 821-831
    • Mourez, M.1    Skouloubris, S.2    Betton, J.M.3    Dassa, E.4
  • 22
    • 0031968765 scopus 로고    scopus 로고
    • Exploring the role of integral membrane proteins in ATP-binding cassette transporters: Analysis of a collection of MalG insertion mutants
    • Nelson, B. D., and B. Traxler. 1998. Exploring the role of integral membrane proteins in ATP-binding cassette transporters: analysis of a collection of MalG insertion mutants. J. Bacteriol. 180:2507-2514.
    • (1998) J. Bacteriol. , vol.180 , pp. 2507-2514
    • Nelson, B.D.1    Traxler, B.2
  • 23
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg, M. F., R. Callaghan, R. C. Ford, and C. F. Higgins. 1997. Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J. Biol. Chem. 272: 10685-10694.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 24
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., P. Fariselli, and R. Casadio. 1996. Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci. 7:1704-1718.
    • (1996) Protein Sci. , vol.7 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 26
    • 0026544212 scopus 로고
    • Completion of the nucleotide sequence of the maltose B region in Salmonella typhimurium - The high conservation of the malM gene suggests a selected physiological role for its product
    • Schneider, E., E. Francoz, and E. Dassa. 1992. Completion of the nucleotide sequence of the maltose B region in Salmonella typhimurium - the high conservation of the malM gene suggests a selected physiological role for its product. Biochim. Biophys. Acta 1129:223-227.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 223-227
    • Schneider, E.1    Francoz, E.2    Dassa, E.3
  • 27
    • 0024023812 scopus 로고
    • Truncated forms of Escherichia coli lactose permease: Models for study of biosynthesis and membrane insertion
    • Stochaj, U., H. J. Fritz, C. Heibach, M. Markgraf, A. von Schaewen, U. Sonnewald, and R. Ehring. 1988. Truncated forms of Escherichia coli lactose permease: models for study of biosynthesis and membrane insertion. J. Bacteriol. 170:2639-2645.
    • (1988) J. Bacteriol. , vol.170 , pp. 2639-2645
    • Stochaj, U.1    Fritz, H.J.2    Heibach, C.3    Markgraf, M.4    Von Schaewen, A.5    Sonnewald, U.6    Ehring, R.7
  • 28
    • 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
  • 29
    • 0026688543 scopus 로고
    • The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli
    • Traxler, B., C. Lee, D. Boyd, and J. Beckwith. 1992. The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli. J. Biol. Chem. 267:5339-5345.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5339-5345
    • Traxler, B.1    Lee, C.2    Boyd, D.3    Beckwith, J.4
  • 30
    • 15844393588 scopus 로고    scopus 로고
    • Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery
    • Traxler, B., and C. Murphy. 1996. Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery. J. Biol. Chem. 271:12394-12400.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12394-12400
    • Traxler, B.1    Murphy, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.