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Volumn 291, Issue 3, 1999, Pages 683-692

Proximity relationships between helices I and XI or XII in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking

Author keywords

Cross linking; Helix packing; Helix tilt; Mutagenesis; Site directed; Split permease

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; LACTOSE PERMEASE; MEMBRANE ENZYME;

EID: 0033588117     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2948     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0025310534 scopus 로고
    • In vivo expression of the lacY gene in two segments leads to functional lac permease
    • Bibi E., Kaback H. R. In vivo expression of the lacY gene in two segments leads to functional lac permease. Proc. Natl Acad. Sci. USA. 87:1990;4325-4329.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4325-4329
    • Bibi, E.1    Kaback, H.R.2
  • 2
    • 0026553380 scopus 로고
    • The N-terminal 22 amino acid residues in the lactose permease of Escherichia coli are not obligatory for membrane insertion or transport activity
    • Bibi E., Stearns S. M., Kaback H. R. The N-terminal 22 amino acid residues in the lactose permease of Escherichia coli are not obligatory for membrane insertion or transport activity. Proc. Natl Acad. Sci. USA. 89:1992;3180-3184.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3180-3184
    • Bibi, E.1    Stearns, S.M.2    Kaback, H.R.3
  • 3
    • 0020431995 scopus 로고
    • Preparation, characterization, and properties of monoclonal antibodies against the lac carrier protein from Escherichia coli
    • Carrasco N., Tahara S. M., Patel L., Goldkorn T., Kaback H. R. Preparation, characterization, and properties of monoclonal antibodies against the lac carrier protein from Escherichia coli. Proc. Natl Acad. Sci. USA. 79:1982;6894-6898.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 6894-6898
    • Carrasco, N.1    Tahara, S.M.2    Patel, L.3    Goldkorn, T.4    Kaback, H.R.5
  • 5
    • 0025865318 scopus 로고
    • Role of proline residues in the structure and function of a membrane transport protein
    • Consler T. G., Tsolas O., Kaback H. R. Role of proline residues in the structure and function of a membrane transport protein. Biochemistry. 30:1991;1291-1298.
    • (1991) Biochemistry , vol.30 , pp. 1291-1298
    • Consler, T.G.1    Tsolas, O.2    Kaback, H.R.3
  • 7
    • 33751385088 scopus 로고
    • Cysteine scanning mutagenesis of putative helix XI in the lactose permease of Escherichia coli
    • Dunten R. L., Sahin-Tóth M., Kaback H. R. Cysteine scanning mutagenesis of putative helix XI in the lactose permease of Escherichia coli. Biochemistry. 32:1993;12644-12650.
    • (1993) Biochemistry , vol.32 , pp. 12644-12650
    • Dunten, R.L.1    Sahin-Tóth, M.2    Kaback, H.R.3
  • 8
    • 0028200090 scopus 로고
    • Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli
    • Frillingos S., Sahin-Tóth M., Persson B., Kaback H. R. Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli. Biochemistry. 33:1994;8074-8081.
    • (1994) Biochemistry , vol.33 , pp. 8074-8081
    • Frillingos, S.1    Sahin-Tóth, M.2    Persson, B.3    Kaback, H.R.4
  • 9
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-functions relationships in polytopic membrane proteins
    • Frillingos S., Sahin-Tóth M., Wu J., Kaback H. R. Cys-scanning mutagenesis: a novel approach to structure-functions relationships in polytopic membrane proteins. FASEB J. 12:1998;1281-1299.
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Tóth, M.2    Wu, J.3    Kaback, H.R.4
  • 10
    • 0022633609 scopus 로고
    • Dideoxy sequencing method using denatured plasmid templates
    • Hattori M., Sakaki Y. Dideoxy sequencing method using denatured plasmid templates. Anal. Biochem. 152:1986;1291-1297.
    • (1986) Anal. Biochem. , vol.152 , pp. 1291-1297
    • Hattori, M.1    Sakaki, Y.2
  • 11
    • 0029813985 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of putative helix X11 in the lactose permease of Escherichia coli
    • He M. M., Sun J., Kaback H. R. Cysteine scanning mutagenesis of putative helix X11 in the lactose permease of Escherichia coli. Biochemistry. 35:1996;12909-12914.
    • (1996) Biochemistry , vol.35 , pp. 12909-12914
    • He, M.M.1    Sun, J.2    Kaback, H.R.3
  • 12
    • 0017049441 scopus 로고
    • Molecular biology and energetics of membrane transport
    • Kaback H. R. Molecular biology and energetics of membrane transport. J. Cell Physiol. 89:1976;575-593.
    • (1976) J. Cell Physiol. , vol.89 , pp. 575-593
    • Kaback, H.R.1
  • 13
    • 0021066915 scopus 로고
    • The lac carrier protein in Escherichia coli: From membrane to molecule
    • Kaback H. R. The lac carrier protein in Escherichia coli: from membrane to molecule. J. Membr. Biol. 76:1983;95-112.
    • (1983) J. Membr. Biol. , vol.76 , pp. 95-112
    • Kaback, H.R.1
  • 14
    • 77956817521 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Past, present and future
    • W. N. Konings, H. R. Kaback, & J. S. Lolkema. Amsterdam: Elsevier
    • Kaback H. R. The lactose permease of Escherichia coli: past, present and future. Konings W. N., Kaback H. R., Lolkema J. S. Handbook of Biological Physics: Transport Processes in Eukaryotic and Prokaryotic Organisms. 1996;203-227 Elsevier, Amsterdam.
    • (1996) Handbook of Biological Physics: Transport Processes in Eukaryotic and Prokaryotic Organisms , pp. 203-227
    • Kaback, H.R.1
  • 15
    • 0031398840 scopus 로고    scopus 로고
    • From membrane to molecule to the third amino acid from the left with the lactose permease of Escherichia coli
    • Kaback H. R., Wu J. From membrane to molecule to the third amino acid from the left with the lactose permease of Escherichia coli. Quart. Rev. Biophys. 30:1997;333-364.
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 333-364
    • Kaback, H.R.1    Wu, J.2
  • 16
    • 0032819684 scopus 로고    scopus 로고
    • What to do while awaiting crystals of a membrane transport protein and thereafter
    • Kaback H. R., Wu J. What to do while awaiting crystals of a membrane transport protein and thereafter. Acc. Chem. Res. in the press:1999.
    • (1999) Acc. Chem. Res.
    • Kaback, H.R.1    Wu, J.2
  • 17
    • 0030769787 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: The lactose permease of Escherichia coli
    • Kaback H. R., Voss J., Wu J. Helix packing in polytopic membrane proteins: the lactose permease of Escherichia coli. Curr. Opin. Struct. Biol. 7:1997;537-542.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 537-542
    • Kaback, H.R.1    Voss, J.2    Wu, J.3
  • 18
  • 19
    • 0028291250 scopus 로고
    • Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli
    • Sahin-Tóth M., Lawrence M. C., Kaback H. R. Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli. Proc. Natl Acad. Sci. USA. 91:1994a;5421-5425.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5421-5425
    • Sahin-Tóth, M.1    Lawrence, M.C.2    Kaback, H.R.3
  • 20
    • 0028206024 scopus 로고
    • Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli
    • Sahin-Tóth M., Persson B., Schwieger L., Cohan M., Kaback H. R. Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli. Protein Sci. 3:1994b;240-247.
    • (1994) Protein Sci. , vol.3 , pp. 240-247
    • Sahin-Tóth, M.1    Persson, B.2    Schwieger, L.3    Cohan, M.4    Kaback, H.R.5
  • 22
    • 0030760970 scopus 로고    scopus 로고
    • Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed crosslinking
    • Sun J., Kaback H. R. Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed crosslinking. Biochemistry. 1997;11959-11965.
    • (1997) Biochemistry , pp. 11959-11965
    • Sun, J.1    Kaback, H.R.2
  • 23
    • 0018850485 scopus 로고
    • Lactose carrier protein of Escherichia coli. Structure and expression of plasmids carrying the Y-gene. of the lac operon
    • Teather R. M., Bramhall L., Riede L., Wright J. K., Furst M., Aichele G., Wilhelm V., Overath P. Lactose carrier protein of Escherichia coli. Structure and expression of plasmids carrying the Y-gene. of the lac operon. Eur. J. Biochem. 108:1980;223-231.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 223-231
    • Teather, R.M.1    Bramhall, L.2    Riede, L.3    Wright, J.K.4    Furst, M.5    Aichele, G.6    Wilhelm, V.7    Overath, P.8
  • 24
    • 0030573676 scopus 로고    scopus 로고
    • Molecular biology of the lactose carrier of Escherichia coli
    • Varela M. F., Wilson T. H. Molecular biology of the lactose carrier of Escherichia coli. Biochim. Biophys. Acta. 1276:1996;21-34.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 21-34
    • Varela, M.F.1    Wilson, T.H.2
  • 25
    • 0022558555 scopus 로고
    • Purification, reconstitution, and characterization of the lac permease of Escherichia coli
    • Viitanen P., Newman M. L., Foster D. L., Wilson T. H., Kaback H. R. Purification, reconstitution, and characterization of the lac permease of Escherichia coli. Methods Enzymol. 125:1986;429-452.
    • (1986) Methods Enzymol. , vol.125 , pp. 429-452
    • Viitanen, P.1    Newman, M.L.2    Foster, D.L.3    Wilson, T.H.4    Kaback, H.R.5
  • 26
    • 0033537639 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol crosslinking: Helix I is close to helices V and XI
    • Wang Q., Kaback H. R. Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol crosslinking: helix I is close to helices V and XI. Biochemistry. 38:1998;3120-3126.
    • (1998) Biochemistry , vol.38 , pp. 3120-3126
    • Wang, Q.1    Kaback, H.R.2
  • 27
    • 0028783805 scopus 로고
    • Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: Structural properties and evidence for a substrate-induced conformational change
    • Weitzman C., Consler T. G., Kaback H. R. Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change. Protein Sci. 4:1995;2310-2318.
    • (1995) Protein Sci. , vol.4 , pp. 2310-2318
    • Weitzman, C.1    Consler, T.G.2    Kaback, H.R.3
  • 28
    • 0025006452 scopus 로고
    • Reconstitution of an active lactose carrier in vivo by simultaneous synthesis of two complementary protein fragments
    • Wrubel W., Stochaj U., Sonnewald U., Theres C., Ehring R. Reconstitution of an active lactose carrier in vivo by simultaneous synthesis of two complementary protein fragments. J. Bacteriol. 172:1990;5374-5381.
    • (1990) J. Bacteriol. , vol.172 , pp. 5374-5381
    • Wrubel, W.1    Stochaj, U.2    Sonnewald, U.3    Theres, C.4    Ehring, R.5
  • 29
    • 0028122679 scopus 로고
    • Construction and in vivo analysis of new split lactose permeases
    • Wrubel W., Stochaj U., Ehring R. Construction and in vivo analysis of new split lactose permeases. FEBS Letters. 349:1994;433-438.
    • (1994) FEBS Letters , vol.349 , pp. 433-438
    • Wrubel, W.1    Stochaj, U.2    Ehring, R.3
  • 30
    • 0029988250 scopus 로고    scopus 로고
    • A general method for determining helix packing in membrane proteins in situ: Helices I and II are close to helix VII in the lactose permease of Escherichia coli
    • Wu J., Kaback H. R. A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli. Proc. Natl Acad. Sci. USA. 93:1996;14498-14502.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14498-14502
    • Wu, J.1    Kaback, H.R.2
  • 31
    • 0030747620 scopus 로고    scopus 로고
    • Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking
    • Wu J., Kaback H. R. Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking. J. Mol. Biol. 270:1997;285-293.
    • (1997) J. Mol. Biol. , vol.270 , pp. 285-293
    • Wu, J.1    Kaback, H.R.2
  • 32
    • 0029043941 scopus 로고
    • Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spetroscopy
    • Wu J., Frillingos S., Kaback H. R. Dynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spetroscopy. Biochemistry. 34:1995;8257-8263.
    • (1995) Biochemistry , vol.34 , pp. 8257-8263
    • Wu, J.1    Frillingos, S.2    Kaback, H.R.3
  • 33
    • 0029789304 scopus 로고    scopus 로고
    • Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli
    • Wu J., Voss J., Hubbell W. L., Kaback H. R. Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli. Proc. Natl Acad. Sci. USA. 93:1996;10123-10127.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10123-10127
    • Wu, J.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 34
    • 0032506162 scopus 로고    scopus 로고
    • Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical crosslinking in situ
    • Wu J., Hardy D., Kaback H. R. Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical crosslinking in situ. Biochemistry. 37:1998a;15785-15790.
    • (1998) Biochemistry , vol.37 , pp. 15785-15790
    • Wu, J.1    Hardy, D.2    Kaback, H.R.3
  • 35
    • 0032500626 scopus 로고    scopus 로고
    • Transmembrane helix tilting and ligand-induced conformational changes in the lactose permease determined by site-directed chemical crosslinking in situ
    • Wu J., Hardy D., Kaback H. R. Transmembrane helix tilting and ligand-induced conformational changes in the lactose permease determined by site-directed chemical crosslinking in situ. J. Mol. Biol. 282:1998b;959-967.
    • (1998) J. Mol. Biol. , vol.282 , pp. 959-967
    • Wu, J.1    Hardy, D.2    Kaback, H.R.3
  • 36
    • 0033010801 scopus 로고    scopus 로고
    • Site-directed chemical crosslinking demonstrate that helix IV is close to helices VII and XI in the lactose permease
    • Wu J., Hardy D., Kaback H. R. Site-directed chemical crosslinking demonstrate that helix IV is close to helices VII and XI in the lactose permease. Biochemistry. 38:1999;1715-1720.
    • (1999) Biochemistry , vol.38 , pp. 1715-1720
    • Wu, J.1    Hardy, D.2    Kaback, H.R.3
  • 37
    • 0028037639 scopus 로고
    • Expression of lactose permease in contiguous fragments as a probe for membrane-spanning domains
    • Zen K. H., McKenna E., Bibi E., Hardy D., Kaback H. R. Expression of lactose permease in contiguous fragments as a probe for membrane-spanning domains. Biochemistry. 33:1994;8198-8206.
    • (1994) Biochemistry , vol.33 , pp. 8198-8206
    • Zen, K.H.1    McKenna, E.2    Bibi, E.3    Hardy, D.4    Kaback, H.R.5


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