메뉴 건너뛰기




Volumn 266, Issue 2, 1999, Pages 420-430

Functional consequences of mutations in the conserved 'signature sequence' of the ATP-binding-cassette protein MalK

Author keywords

ABC transport systems; MalFGK2; MalK; Maltose transport

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; BACTERIAL PROTEIN; LINK PROTEIN; LIPOSOME; MALTOSE; MALTOSE BINDING PROTEIN; MUTANT PROTEIN; TRYPSIN; MALK PROTEIN, BACTERIA; MALK PROTEIN, SALMONELLA TYPHIMURIUM; PROTEIN; RECOMBINANT PROTEIN;

EID: 0033485380     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00871.x     Document Type: Article
Times cited : (73)

References (47)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganism to man
    • 1. Higgins, C.F. (1992) ABC transporters: from microorganism to man. Annu. Rev. Cell Biol. 8, 67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 4
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding-protein-dependent ABC transporters, in Escherichia coli and Salmonella
    • Neidhardt, F.C. et al., eds. American Society for Microbiology, Washington, DC
    • 4. Boos, W. & Lucht, J.M. (1996) Periplasmic binding-protein-dependent ABC transporters, in Escherichia coli and Salmonella. In Cellular and Molecular Biology (Neidhardt, F.C. et al., eds), pp. 1175-1209. American Society for Microbiology, Washington, DC.
    • (1996) Cellular and Molecular Biology , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 5
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • 5. Schneider, E. & Hunke, S. (1998) ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol. Rev. 22, 1-20.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 6
    • 0026638255 scopus 로고
    • ATP-dependent bacterial transporters and cystic fibrosis: Analogy between channels and transporters
    • 6. Ames, G.F.-L. & Lecar, H. (1992) ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. FASEB J. 6, 2660-2666.
    • (1992) FASEB J. , vol.6 , pp. 2660-2666
    • Ames, G.F.-L.1    Lecar, H.2
  • 7
    • 0026094617 scopus 로고
    • Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP-binding cassette (ABC) protein superfamily
    • 7. Berkower, C. & Michaelis, S. (1991) Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP-binding cassette (ABC) protein superfamily. EMBO J. 10, 3777-3785.
    • (1991) EMBO J. , vol.10 , pp. 3777-3785
    • Berkower, C.1    Michaelis, S.2
  • 8
    • 0028033550 scopus 로고
    • Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1
    • 8. Hoof, T., Demmer, A., Hadam, M.R., Riordan, J.R. & Tümmler, B. (1994) Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1. J. Biol Chem. 269, 20575-20583.
    • (1994) J. Biol Chem. , vol.269 , pp. 20575-20583
    • Hoof, T.1    Demmer, A.2    Hadam, M.R.3    Riordan, J.R.4    Tümmler, B.5
  • 9
    • 0028915106 scopus 로고
    • Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • 9. Koronakis, E., Hughes, C., Milisav, I. & Koronakis, V. (1995) Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB. Mol Microbiol. 16, 87-96.
    • (1995) Mol Microbiol. , vol.16 , pp. 87-96
    • Koronakis, E.1    Hughes, C.2    Milisav, I.3    Koronakis, V.4
  • 10
    • 0029867564 scopus 로고    scopus 로고
    • Mutations within the first LSGGQ motif of Ste6p cause defects in α-factor transport and mating in Saccharomyces cerevisiae
    • 10. Browne, B.L., McClendon, V. & Bedwell, D.M. (1996) Mutations within the first LSGGQ motif of Ste6p cause defects in α-factor transport and mating in Saccharomyces cerevisiae. J. Bacteriol. 178, 1712-1719.
    • (1996) J. Bacteriol. , vol.178 , pp. 1712-1719
    • Browne, B.L.1    McClendon, V.2    Bedwell, D.M.3
  • 11
    • 0031007555 scopus 로고    scopus 로고
    • Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region
    • 11. Bakos, E., Klein, I., Welker, E., Szabo, K., Müller, M., Sakardi, B. & Varadi, A. (1997) Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region. Biochem. J. 323, 777-783.
    • (1997) Biochem. J. , vol.323 , pp. 777-783
    • Bakos, E.1    Klein, I.2    Welker, E.3    Szabo, K.4    Müller, M.5    Sakardi, B.6    Varadi, A.7
  • 12
    • 0027162649 scopus 로고
    • Molecular mechanism of CFTR chloride channel dysfunction in cystic fibrosis
    • 12. Welsh, M.J. & Smith, A.E. (1993) Molecular mechanism of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73, 1251-1254.
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 13
    • 0029058027 scopus 로고
    • Sequence homologies between nucleotide binding regions of CFTR and G-proteins suggest structural and functional similarities
    • 13. Manavalan, P., Dearborn, D.G., McPherson, J.M. & Smith, A.E. (1995) Sequence homologies between nucleotide binding regions of CFTR and G-proteins suggest structural and functional similarities. FEBS Lett. 366, 87-91.
    • (1995) FEBS Lett. , vol.366 , pp. 87-91
    • Manavalan, P.1    Dearborn, D.G.2    McPherson, J.M.3    Smith, A.E.4
  • 15
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • 15. Boos, W. & Shuman, H. (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, H.2
  • 16
    • 0026795955 scopus 로고
    • Large scale purification, nucleotide binding properties and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex
    • 16. Walter, C., Höner zu Bentrup, K. & Schneider, E. (1992) Large scale purification, nucleotide binding properties and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex. J. Biol. Chem. 267, 8863-8869.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8863-8869
    • Walter, C.1    Höner Zu Bentrup, K.2    Schneider, E.3
  • 17
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose/maltodextrines of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK-subunit
    • 17. Morbach, S., Tebbe, S. & Schneider, E. (1993) The ATP-binding cassette (ABC) transporter for maltose/maltodextrines of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK-subunit. J. Biol. Chem. 268, 18617-18621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18617-18621
    • Morbach, S.1    Tebbe, S.2    Schneider, E.3
  • 18
    • 0025214263 scopus 로고
    • Overproduction, solubilization and reconstitution of the maltose transport system from Escherichia coli
    • 18. Davidson, A.L. & Nikaido, H. (1990) Overproduction, solubilization and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265, 4254-4260.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 19
    • 0030886132 scopus 로고    scopus 로고
    • Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli
    • 19. Davidson, A.L. & Sharma, S. (1997) Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli. J. Bacteriol. 179, 5458-5464.
    • (1997) J. Bacteriol. , vol.179 , pp. 5458-5464
    • Davidson, A.L.1    Sharma, S.2
  • 21
    • 0031768746 scopus 로고    scopus 로고
    • The ATP-binding cassette subunit MalK antagonizes MalT, the activator of the Escherichia coli mal regulon
    • 21. Panagiotidis, C.H., Boos, W. & Shuman, H.A. (1998) The ATP-binding cassette subunit MalK antagonizes MalT, the activator of the Escherichia coli mal regulon. Mol. Microbiol. 30, 535-546.
    • (1998) Mol. Microbiol. , vol.30 , pp. 535-546
    • Panagiotidis, C.H.1    Boos, W.2    Shuman, H.A.3
  • 22
    • 0025740666 scopus 로고
    • A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium
    • 22. Schneider, E. & Walter, C. (1991) A chimeric nucleotide-binding protein, encoded by a hisP-malK hybrid gene, is functional in maltose transport in Salmonella typhimurium. Mol. Microbiol. 5, 1375-1383.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1375-1383
    • Schneider, E.1    Walter, C.2
  • 23
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations
    • 23. Kühnau, S., Reyes, M., Sievertsen, A., Shuman, H.A. & Boos, W. (1991) The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J. Bacteriol. 173, 2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 24
    • 0031704443 scopus 로고    scopus 로고
    • Domain structure of the ATP-binding cassette protein MalK of Salmonella typhimurium as assessed by coexpressed half molecules and LacK′-′MalK chimeras
    • 24. Schmees, G. & Schneider, E. (1998) Domain structure of the ATP-binding cassette protein MalK of Salmonella typhimurium as assessed by coexpressed half molecules and LacK′-′MalK chimeras. J. Bacteriol. 180, 5299-5305.
    • (1998) J. Bacteriol. , vol.180 , pp. 5299-5305
    • Schmees, G.1    Schneider, E.2
  • 26
    • 0029240313 scopus 로고
    • Functional purification of a bacterial ATP-binding cassette transporter protein (MalK) from the cytoplasmic fraction of an overproducing strain
    • 26. Schneider, E., Linde, M. & Tebbe, S. (1995) Functional purification of a bacterial ATP-binding cassette transporter protein (MalK) from the cytoplasmic fraction of an overproducing strain. Protein Expression Purif. 6, 10-14.
    • (1995) Protein Expression Purif. , vol.6 , pp. 10-14
    • Schneider, E.1    Linde, M.2    Tebbe, S.3
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • 27. Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 28
    • 77956999456 scopus 로고
    • Genetic techniques in studies of bacterial metabolism
    • 28. Roth, J.R. (1970) Genetic techniques in studies of bacterial metabolism. Methods Enzymol. 17, 3-35.
    • (1970) Methods Enzymol. , vol.17 , pp. 3-35
    • Roth, J.R.1
  • 29
    • 0029830549 scopus 로고    scopus 로고
    • 2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool
    • 2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool. Mol. Microbiol. 22, 555-666.
    • (1996) Mol. Microbiol. , vol.22 , pp. 555-666
    • Wilken, S.1    Schmees, G.2    Schneider, E.3
  • 30
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • 30. Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 31
    • 0027126818 scopus 로고
    • Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family
    • 31. Walter, C., Wilken, S. & Schneider, E. (1992) Characterization of site-directed mutations in conserved domains of MalK, a bacterial member of the ATP-binding cassette (ABC) family. FEBS Lett. 303, 41-44.
    • (1992) FEBS Lett. , vol.303 , pp. 41-44
    • Walter, C.1    Wilken, S.2    Schneider, E.3
  • 32
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using polymerase chain reaction
    • 32. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 33
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signalling by periplasmic binding proteins
    • 33. Davidson, A.L., Shuman, H.A. & Nikaido, H. (1992) Mechanism of maltose transport in Escherichia coli: transmembrane signalling 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
  • 34
    • 0028109264 scopus 로고
    • Nucleotide-induced conformational changes of MalK, a bacterial ATP-binding cassette transporter protein
    • 34. Schneider, E., Wilken, S. & Schmid, R. (1994) Nucleotide-induced conformational changes of MalK, a bacterial ATP-binding cassette transporter protein. J. Biol. Chem. 269, 20456-20461.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20456-20461
    • Schneider, E.1    Wilken, S.2    Schmid, R.3
  • 35
    • 0024095619 scopus 로고
    • Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon
    • 35. Reyes, M. & Shuman, H.A. (1988) Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon. J. Bacteriol. 170, 4598-4602.
    • (1988) J. Bacteriol. , vol.170 , pp. 4598-4602
    • Reyes, M.1    Shuman, H.A.2
  • 36
    • 0029897681 scopus 로고    scopus 로고
    • Photoaffinity labeling and photoaffinity crosslinking of enzymes
    • 36. Schäfer, H.-J. & Schuhen, A. (1996) Photoaffinity labeling and photoaffinity crosslinking of enzymes. Biol. Res. 29, 31-46.
    • (1996) Biol. Res. , vol.29 , pp. 31-46
    • Schäfer, H.-J.1    Schuhen, A.2
  • 37
    • 0027375813 scopus 로고
    • Characterization of structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter: The maltose transport system of Escherichia coli
    • 37. Panagiotidis, C.H., Reyes, M., Sievertsen, A., Boos, W. & Shuman, H.A. (1993) Characterization of structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter: the maltose transport system of Escherichia coli. 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
  • 38
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • 38. Qu, B.-H., Strickland, E.H. & Thomas, P.J. (1997) Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J. Biol. Chem. 272, 15739-15744.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15739-15744
    • Qu, B.-H.1    Strickland, E.H.2    Thomas, P.J.3
  • 40
    • 13044258869 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the bacterial ATP-binding-cassette (ABC)-protein MalK
    • 40. Schmees, G., Hoener zu Bentrup, K., Schneider, E., Vinzenz, C. & Ermler, U. (1999) Crystallization and preliminary X-ray analysis of the bacterial ATP-binding-cassette (ABC)-protein MalK. Acta Crystallogr. D55, 285-286.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 285-286
    • Schmees, G.1    Hoener Zu Bentrup, K.2    Schneider, E.3    Vinzenz, C.4    Ermler, U.5
  • 41
    • 0028796334 scopus 로고
    • A common topology of proteins catalyzing ATP-triggered reactions
    • 41. Yoshida, M. & Amano, T. (1995) A common topology of proteins catalyzing ATP-triggered reactions. FEBS Lett. 359, 1-5.
    • (1995) FEBS Lett. , vol.359 , pp. 1-5
    • Yoshida, M.1    Amano, T.2
  • 42
    • 0029657972 scopus 로고    scopus 로고
    • Polysialic acid export in Escherichia coli Kl: The role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation
    • 42. Bliss, J.M., Garon, C.F. & Silver, R.P. (1996) Polysialic acid export in Escherichia coli Kl: 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
  • 43
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperatively in ATP hydrolysis
    • 43. Davidson, A.L., Laghaeian, S.S. & Mannering, D.E. (1996). The maltose transport system of Escherichia coli displays positive cooperatively in ATP hydrolysis. J. Biol. Chem. 271, 4858-4863.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 44
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interaction in ABC transporters. A conserved sequence in hydrophobic membrane proteins of periplasmic permeases define sites of interaction with the helical domain of ABC subunits
    • 44. Mourez, M., Hofnung, M. & Dassa, E. (1997) Subunit interaction in ABC transporters. A conserved sequence in hydrophobic membrane proteins of periplasmic permeases define sites of interaction with the helical domain of ABC subunits. EMBO J. 16, 3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 45
    • 0031756353 scopus 로고    scopus 로고
    • In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: Modulation by ATP
    • 45. Mourez, M., Jéhano, M., Schneider, E. & Dassa, E. (1998) In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP. Mol. Microbiol. 30, 353-363.
    • (1998) Mol. Microbiol. , vol.30 , pp. 353-363
    • Mourez, M.1    Jéhano, M.2    Schneider, E.3    Dassa, E.4
  • 46
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • 46. Studier, F.W. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219, 37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 47
    • 0027410046 scopus 로고
    • The pRSET family of T7 promotor expression vector for Escherichia coli
    • 47. Schoepfer, R. (1993) The pRSET family of T7 promotor expression vector for Escherichia coli. Gene 124, 83-85.
    • (1993) Gene , vol.124 , pp. 83-85
    • Schoepfer, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.