메뉴 건너뛰기




Volumn , Issue , 2007, Pages 39-54

Membranes and transport proteins of thermophilic microorganisms

Author keywords

[No Author keywords available]

Indexed keywords


EID: 58149275149     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (80)
  • 1
    • 0000394325 scopus 로고
    • Lipid phase transitions and regulation of membrane fluidity in prokaryotes
    • Melchior, D. L. 1982. Lipid phase transitions and regulation of membrane fluidity in prokaryotes. Curr. Top. Membr. Transp. 17:263-316.
    • (1982) Curr. Top. Membr. Transp. , vol.17 , pp. 263-316
    • Melchior, D.L.1
  • 2
    • 0030014942 scopus 로고    scopus 로고
    • Structural analysis of phospholipids and glycolipids in extremely halophilic archaebacteria
    • Kates, M. 1996. Structural analysis of phospholipids and glycolipids in extremely halophilic archaebacteria. J. Microbiol. Meth. 25:113-128.
    • (1996) J. Microbiol. Meth. , vol.25 , pp. 113-128
    • Kates, M.1
  • 3
    • 0027161989 scopus 로고
    • On the revised structure of the major phospholipid of Halobacterium salinarium
    • Kates, M., N. Moldoveanu, and L. C. Stewart. 1993. On the revised structure of the major phospholipid of Halobacterium salinarium. Biochim. Biophys. Acta 1169:46-53.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 46-53
    • Kates, M.1    Moldoveanu, N.2    Stewart, L.C.3
  • 4
    • 0028060491 scopus 로고
    • Lipids of extremely halophilic archaeobacteria from saline environments in India: A novel glycolipid in Natronobacterium strains
    • Upasani, V. N., S. G. Desai, N. Moldoveanu, and M. Kates. 1994. Lipids of extremely halophilic archaeobacteria from saline environments in India: a novel glycolipid in Natronobacterium strains. Microbiology 140:1959-1966.
    • (1994) Microbiology , vol.140 , pp. 1959-1966
    • Upasani, V.N.1    Desai, S.G.2    Moldoveanu, N.3    Kates, M.4
  • 5
    • 0002453871 scopus 로고
    • Archaebacteria: Lipids, membrane structures, and adaptations to environmental stresses
    • G. di Prisco (ed.), Springer-Verlag, Berlin Heidelberg
    • De Rosa, M., A. Trincone, B. Nicolaus, and A. Gambacorta. 1991. Archaebacteria: lipids, membrane structures, and adaptations to environmental stresses. In G. di Prisco (ed.), Life under extreme conditions. Springer-Verlag, Berlin Heidelberg, pp. 61-87.
    • (1991) Life under extreme conditions. , pp. 61-87
    • De Rosa, M.1    Trincone, A.2    Nicolaus, B.3    Gambacorta, A.4
  • 6
    • 0026543822 scopus 로고
    • Functional reconstitution of membrane proteins in monolayer liposomes from bipolar lipids of Sulfolobus acidocaldarius
    • Elferink, M. G. L., J. G. De Wit, R. Demel, A. J. M. Driessen, and W. N. Konings. 1992. Functional reconstitution of membrane proteins in monolayer liposomes from bipolar lipids of Sulfolobus acidocaldarius. J. Biol. Chem. 267:1375-1381.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1375-1381
    • Elferink, M.G.L.1    De Wit, J.G.2    Demel, R.3    Driessen, A.J.M.4    Konings, W.N.5
  • 7
    • 85057673971 scopus 로고
    • Lipids of Thermoplasma
    • Langworthy, T. A. 1982. Lipids of Thermoplasma. Methods Enzymol. 88:369-406.
    • (1982) Methods Enzymol. , vol.88 , pp. 369-406
    • Langworthy, T.A.1
  • 8
  • 9
    • 0025816504 scopus 로고
    • Proportions of diether, macrocyclic diether, and tetraether lipids in Methanococcus jannaschii grown at different temperatures
    • Sprott, G. D., M. Meloche, and J. C. Richards. 1991. Proportions of diether, macrocyclic diether, and tetraether lipids in Methanococcus jannaschii grown at different temperatures. J. Bacteriol. 173:3907-3910.
    • (1991) J. Bacteriol. , vol.173 , pp. 3907-3910
    • Sprott, G.D.1    Meloche, M.2    Richards, J.C.3
  • 10
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill, O. P. and B. Martinac. 2001. Molecular basis of mechanotransduction in living cells. Physiol. Rev. 81:685-740.
    • (2001) Physiol. Rev. , vol.81 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 11
    • 0035132229 scopus 로고    scopus 로고
    • Molecular identification of a mechanosensitive channel in archaea
    • Kloda, A. and B. Martinac. 2001. Molecular identification of a mechanosensitive channel in archaea. Biophys. J. 80:229-240.
    • (2001) Biophys. J. , vol.80 , pp. 229-240
    • Kloda, A.1    Martinac, B.2
  • 12
    • 0032524340 scopus 로고    scopus 로고
    • Mechanosensitive ion channels of the archaeon Haloferax volcanii
    • Le Dain, A. C., N. Saint, A. Kloda, A. Ghazi, and B. Martinac. 1998. Mechanosensitive ion channels of the archaeon Haloferax volcanii. J. Biol. Chem. 273:12116-12119.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12116-12119
    • Le Dain, A.C.1    Saint, N.2    Kloda, A.3    Ghazi, A.4    Martinac, B.5
  • 13
    • 0035756772 scopus 로고    scopus 로고
    • Mechanosensitive channel of Thermoplasma, the cell wall-less archaea: Cloning and molecular characterization
    • Kloda, A. and B. Martinac. 2001. Mechanosensitive channel of Thermoplasma, the cell wall-less archaea: cloning and molecular characterization. Cell Biochem. Biophys. 34:321-347.
    • (2001) Cell Biochem. Biophys. , vol.34 , pp. 321-347
    • Kloda, A.1    Martinac, B.2
  • 14
    • 0035901511 scopus 로고    scopus 로고
    • Structural and functional differences between two homologous mechanosensitive channels of Methanococcus jannaschii
    • Kloda, A. and B. Martinac. 2001. Structural and functional differences between two homologous mechanosensitive channels of Methanococcus jannaschii. EMBO J. 20:1888-1896.
    • (2001) EMBO J. , vol.20 , pp. 1888-1896
    • Kloda, A.1    Martinac, B.2
  • 15
    • 3042853029 scopus 로고    scopus 로고
    • Mechanosensitive ion channels: Molecules of mechanotransduction
    • Martinac, B. 2004. Mechanosensitive ion channels: molecules of mechanotransduction. J. Cell Sci. 117:2449-2460.
    • (2004) J. Cell Sci. , vol.117 , pp. 2449-2460
    • Martinac, B.1
  • 16
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B. T. Chait, and R. MacKinnon. 2002. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 20
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • Chanda, B., O. Kwame Asamoah, R. Blunck, B. Roux, and F. Bezanilla. 2005. Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement. Nature 436:852-856.
    • (2005) Nature , vol.436 , pp. 852-856
    • Chanda, B.1    Kwame Asamoah, O.2    Blunck, R.3    Roux, B.4    Bezanilla, F.5
  • 22
    • 33746549925 scopus 로고    scopus 로고
    • Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
    • Eshaghi, S., D. Niegowski, A. Kohl, M. D. Martinez, S. A. Lesley, and P. Nordlund. 2006. Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution. Science 313:354-357.
    • (2006) Science , vol.313 , pp. 354-357
    • Eshaghi, S.1    Niegowski, D.2    Kohl, A.3    Martinez, M.D.4    Lesley, S.A.5    Nordlund, P.6
  • 24
    • 33748031116 scopus 로고    scopus 로고
    • 2+ homeostasis and the CorA translocation cycle
    • 2+ homeostasis and the CorA translocation cycle. EMBO J. 25:3762-3773.
    • (2006) EMBO J. , vol.25 , pp. 3762-3773
    • Payandeh, J.1    Pai, E.F.2
  • 25
    • 0037494948 scopus 로고    scopus 로고
    • Characterization and functional complementation of a nonlethal deletion in the chromosome of a beta-glycosidase mutant of Sulfolobus solfataricus
    • Bartolucci, S., M. Rossi, and R. Cannio. 2003. Characterization and functional complementation of a nonlethal deletion in the chromosome of a beta-glycosidase mutant of Sulfolobus solfataricus. J. Bacteriol. 185:3948-3957.
    • (2003) J. Bacteriol. , vol.185 , pp. 3948-3957
    • Bartolucci, S.1    Rossi, M.2    Cannio, R.3
  • 26
    • 0028956151 scopus 로고
    • A gene encoding a putative membrane protein homologous to the major facilitator superfamily of transporters maps upstream of the β-glycosidase gene in the Archaeon Sulfolobus solfataricus
    • Prisco, A., M. Moracci, M. Rossi, and M. Ciaramella. 1995. A gene encoding a putative membrane protein homologous to the major facilitator superfamily of transporters maps upstream of the β-glycosidase gene in the Archaeon Sulfolobus solfataricus. J. Bacteriol. 177:1614-1619.
    • (1995) J. Bacteriol. , vol.177 , pp. 1614-1619
    • Prisco, A.1    Moracci, M.2    Rossi, M.3    Ciaramella, M.4
  • 27
    • 0031009130 scopus 로고    scopus 로고
    • The methanogenic archaeon Methanosarcina thermophila TM-1 possesses a high-affinity glycine betaine transporter involved in osmotic adaptation
    • Proctor, L. M., R. Lai, and R. P. Gunsalus. 1997. The methanogenic archaeon Methanosarcina thermophila TM-1 possesses a high-affinity glycine betaine transporter involved in osmotic adaptation. Appl. Environ. Microbiol. 63:2252-2257.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2252-2257
    • Proctor, L.M.1    Lai, R.2    Gunsalus, R.P.3
  • 28
    • 0033872766 scopus 로고    scopus 로고
    • Glycine betaine transport in the obligate halophilic archaeon Methanohalophilus portucalensis
    • Lai, M. C., T. Y. Hong, and R. P. Gunsalus. 2000. Glycine betaine transport in the obligate halophilic archaeon Methanohalophilus portucalensis. J. Bacteriol. 182:5020-5024.
    • (2000) J. Bacteriol. , vol.182 , pp. 5020-5024
    • Lai, M.C.1    Hong, T.Y.2    Gunsalus, R.P.3
  • 29
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., O. Boudker, Y. Jin, and E. Gouaux. 2004. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811-818.
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 30
    • 33750360302 scopus 로고    scopus 로고
    • Structure and function of prokaryotic glutamate transporters from Escherichia coli and Pyrococcus horikoshii
    • Raunser, S., M. Appel, C. Ganea, U. Geldmacher-Kaufer, K. Fendler, and W. Kuhlbrandt. 2006. Structure and function of prokaryotic glutamate transporters from Escherichia coli and Pyrococcus horikoshii. Biochemistry 45:12796-12805.
    • (2006) Biochemistry , vol.45 , pp. 12796-12805
    • Raunser, S.1    Appel, M.2    Ganea, C.3    Geldmacher-Kaufer, U.4    Fendler, K.5    Kuhlbrandt, W.6
  • 31
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., R. M. Ryan, D. Yernool, K. Shimamoto, and E. Gouaux. 2007. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445:387-393.
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 32
    • 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
  • 33
    • 0035010435 scopus 로고    scopus 로고
    • ABC transporters catalyzing carbohydrate uptake
    • Schneider, E. 2001. ABC transporters catalyzing carbohydrate uptake. Res. Microbiol. 152:303-310.
    • (2001) Res. Microbiol. , vol.152 , pp. 303-310
    • Schneider, E.1
  • 34
    • 0034885332 scopus 로고    scopus 로고
    • Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter
    • Koning, S. M., M. G. Elferink, W. N. Konings, and A. J. M. Driessen. 2001. Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter. J. Bacteriol. 183:4979-4984.
    • (2001) J. Bacteriol. , vol.183 , pp. 4979-4984
    • Koning, S.M.1    Elferink, M.G.2    Konings, W.N.3    Driessen, A.J.M.4
  • 35
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink, M. G. L., S.-V. Albers, W. N. Konings, and A. J. M. Driessen. 2001. Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39:1494-1503.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.L.1    Albers, S.-V.2    Konings, W.N.3    Driessen, A.J.M.4
  • 37
    • 0037470149 scopus 로고    scopus 로고
    • Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima
    • Chhabra, S. R., K. R. Shockley, S. B. Conners, K. L. Scott, R. D. Wolfinger, and R. M. Kelly. 2003. Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima. J. Biol. Chem. 278:7540-7552.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7540-7552
    • Chhabra, S.R.1    Shockley, K.R.2    Conners, S.B.3    Scott, K.L.4    Wolfinger, R.D.5    Kelly, R.M.6
  • 38
    • 33144472334 scopus 로고    scopus 로고
    • Several archaeal homologs of putative oligopeptide- binding proteins encoded by Thermotoga maritima bind sugars
    • Nanavati, D. M., K. Thirangoon, and K. M. Noll. 2006. Several archaeal homologs of putative oligopeptide- binding proteins encoded by Thermotoga maritima bind sugars. Appl. Environ. Microbiol. 72:1336-1345.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1336-1345
    • Nanavati, D.M.1    Thirangoon, K.2    Noll, K.M.3
  • 39
    • 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
  • 40
    • 0033575309 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Greller, G., R. Horlacher, J. DiRuggiero, and W. Boos. 1999. Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 274:20259-20264.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20259-20264
    • Greller, G.1    Horlacher, R.2    DiRuggiero, J.3    Boos, W.4
  • 41
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs, K., J. Diez, G. Greller, C. Muller, J. Breed, C. Schnell, C. Vonrhein, W. Boos, and W. Welte. 2000. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19:5951-5961.
    • (2000) EMBO J. , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Muller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 42
    • 0035951304 scopus 로고    scopus 로고
    • The Crystal Structure of a Liganded Trehalose/Maltose-binding Protein from the Hyperthermophilic Archaeon Thermococcus litoralis at 1.85 Å
    • Diez, J., K. Diederichs, G. Greller, R. Horlacher, W. Boos, and W. Welte. 2001. The Crystal Structure of a Liganded Trehalose/Maltose-binding Protein from the Hyperthermophilic Archaeon Thermococcus litoralis at 1.85 Å. J. Mol. Biol. 305:905-915.
    • (2001) J. Mol. Biol. , vol.305 , pp. 905-915
    • Diez, J.1    Diederichs, K.2    Greller, G.3    Horlacher, R.4    Boos, W.5    Welte, W.6
  • 43
    • 0034828112 scopus 로고    scopus 로고
    • Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis
    • Greller, G., R. Riek, and W. Boos. 2001. Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis. Eur. J. Biochem. 268:4011-4018.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4011-4018
    • Greller, G.1    Riek, R.2    Boos, W.3
  • 44
    • 0033973103 scopus 로고    scopus 로고
    • The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
    • Reich-Slotky, R., C. Panagiotidis, M. Reyes, and H. A. Shuman. 2000. The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil. J. Bacteriol. 182:993-1000.
    • (2000) J. Bacteriol. , vol.182 , pp. 993-1000
    • Reich-Slotky, R.1    Panagiotidis, C.2    Reyes, M.3    Shuman, H.A.4
  • 45
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F. A. and P. S. Ledvina. 1996. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20:17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 46
    • 0035951289 scopus 로고    scopus 로고
    • Structural basis for oligosaccharide recognition by Pyrococcus furiosus maltodextrin-binding protein
    • Evdokimov, A. G., D. E. Anderson, K. M. Routzahn, and D. S. Waugh. 2001. Structural basis for oligosaccharide recognition by Pyrococcus furiosus maltodextrin-binding protein. J. Mol. Biol. 305:891-904.
    • (2001) J. Mol. Biol. , vol.305 , pp. 891-904
    • Evdokimov, A.G.1    Anderson, D.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 47
    • 9144257311 scopus 로고    scopus 로고
    • Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Schiefner, A., G. Holtmann, K. Diederichs, W. Welte, and E. Bremer. 2004. Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus. J. Biol. Chem. 279:48270-48281.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48270-48281
    • Schiefner, A.1    Holtmann, G.2    Diederichs, K.3    Welte, W.4    Bremer, E.5
  • 48
    • 85057709589 scopus 로고    scopus 로고
    • Thesis. University of Marbug, Germany
    • Holtmann, G. 2004. Thesis. University of Marbug, Germany.
    • (2004)
    • Holtmann, G.1
  • 49
    • 33748777679 scopus 로고    scopus 로고
    • Tungsten transport protein A (WtpA) in Pyrococcus furiosus: The first member of a new class of tungstate and molybdate transporters
    • Bevers, L. E., P. L. Hagedoorn, G. C. Krijger, and W. R. Hagen. 2006. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188:6498-6505.
    • (2006) J. Bacteriol. , vol.188 , pp. 6498-6505
    • Bevers, L.E.1    Hagedoorn, P.L.2    Krijger, G.C.3    Hagen, W.R.4
  • 50
    • 0032908691 scopus 로고    scopus 로고
    • The type II pullulanase of Thermococcus hydrothermalis: Molecular characterization of the gene and expression of the catalytic domain
    • Erra-Pujada, M., P. Debeire, F. Duchiron, and M. J. O’Donohue. 1999. The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J. Bacteriol. 181:3284-3287.
    • (1999) J. Bacteriol. , vol.181 , pp. 3284-3287
    • Erra-Pujada, M.1    Debeire, P.2    Duchiron, F.3    O’Donohue, M.J.4
  • 51
    • 0032523235 scopus 로고    scopus 로고
    • Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound b-type hemoprotein
    • Hettmann, T., C. L. Schmidt, S. Anemuller, U. Zahringer, H. Moll, A. Petersen, and G. Schafer. 1998. Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel highly glycosylated, membrane-bound b-type hemoprotein. J. Biol. Chem. 273:12032-12040.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12032-12040
    • Hettmann, T.1    Schmidt, C.L.2    Anemuller, S.3    Zahringer, U.4    Moll, H.5    Petersen, A.6    Schafer, G.7
  • 52
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., E. Berg, R. Mengele, and I. Strobel. 1990. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J. Bacteriol. 172:7111-7118.
    • (1990) J. Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 53
    • 0011731008 scopus 로고    scopus 로고
    • Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyroccocus furiosus
    • Koning, S. M., W. N. Konings, and A. J. M. Driessen. 2002. Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyroccocus furiosus. Archaea 1:19-25.
    • (2002) Archaea , vol.1 , pp. 19-25
    • Koning, S.M.1    Konings, W.N.2    Driessen, A.J.M.3
  • 55
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a highaffinity membrane-integrated binding protein
    • Albers, S. V., M. G. Elferink, R. L. Charlebois, C. W. Sensen, A. J. M. Driessen, and W. N. Konings. 1999. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a highaffinity membrane-integrated binding protein. J. Bacteriol. 181:4285-4291.
    • (1999) J. Bacteriol. , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.M.5    Konings, W.N.6
  • 56
    • 0000953403 scopus 로고
    • Archaeobacterial cell envelopes
    • Koenig, H. 1988. Archaeobacterial cell envelopes. Can. J. Microbiol. 34:395-406.
    • (1988) Can. J. Microbiol. , vol.34 , pp. 395-406
    • Koenig, H.1
  • 58
    • 0028246909 scopus 로고
    • The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation
    • Mattar, S., B. Scharf, S. B. Kent, K. Rodewald, D. Oesterhelt, and M. Engelhard. 1994. The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. J. Biol. Chem. 269:14939-14945.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14939-14945
    • Mattar, S.1    Scharf, B.2    Kent, S.B.3    Rodewald, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 59
    • 0032984481 scopus 로고    scopus 로고
    • A unique short signal sequence in membrane anchored proteins of Archaea
    • Albers, S. V., W. N. Konings, and A. J. M. Driessen. 1999. A unique short signal sequence in membrane anchored proteins of Archaea. Mol. Microbiol. 31:1595-1596.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1595-1596
    • Albers, S.V.1    Konings, W.N.2    Driessen, A.J.M.3
  • 60
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: A different kind of prokaryotic motility structure
    • Thomas, N. A., S. L. Bardy, and K. F. Jarrell. 2001. The archaeal flagellum: a different kind of prokaryotic motility structure. FEMS Microbiol. Rev. 25:147-174.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 61
    • 15844409025 scopus 로고    scopus 로고
    • Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus
    • Albers, S. V. and A. J. M. Driessen. 2005. Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus. Microbiology 151:763-773.
    • (2005) Microbiology , vol.151 , pp. 763-773
    • Albers, S.V.1    Driessen, A.J.M.2
  • 62
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • Albers, S. V., Z. Szabó, and A. J. M. Driessen. 2003. Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. J. Bacteriol. 185:3918-3925.
    • (2003) J. Bacteriol. , vol.185 , pp. 3918-3925
    • Albers, S.V.1    Szabó, Z.2    Driessen, A.J.M.3
  • 63
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • Bardy, S. L. and K. F. Jarrell. 2002. FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity. FEMS Microbiol. Lett. 208:53-59.
    • (2002) FEMS Microbiol. Lett. , vol.208 , pp. 53-59
    • Bardy, S.L.1    Jarrell, K.F.2
  • 64
    • 13244298136 scopus 로고    scopus 로고
    • Site-directed mutagenesis analysis of amino acids critical for activity of the type I signal peptidase of the archaeon Methanococcus voltae
    • Bardy, S. L., S. Y. Ng, D. S. Carnegie, and K. F. Jarrell. 2005. Site-directed mutagenesis analysis of amino acids critical for activity of the type I signal peptidase of the archaeon Methanococcus voltae. J. Bacteriol. 187:1188-1191.
    • (2005) J. Bacteriol. , vol.187 , pp. 1188-1191
    • Bardy, S.L.1    Ng, S.Y.2    Carnegie, D.S.3    Jarrell, K.F.4
  • 65
    • 0141995025 scopus 로고    scopus 로고
    • Cloning and characterization of archaeal type I signal peptidase from Methanococcus voltae
    • Ng, S. Y. and K. F. Jarrell. 2003. Cloning and characterization of archaeal type I signal peptidase from Methanococcus voltae. J. Bacteriol. 185:5936-5942.
    • (2003) J. Bacteriol. , vol.185 , pp. 5936-5942
    • Ng, S.Y.1    Jarrell, K.F.2
  • 66
    • 0037106458 scopus 로고    scopus 로고
    • Lipid modification of proteins in Archaea: Attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation
    • Konrad, Z. and J. Eichler. 2002. Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation. Biochem. J. 366:959-964.
    • (2002) Biochem. J. , vol.366 , pp. 959-964
    • Konrad, Z.1    Eichler, J.2
  • 67
    • 33749860199 scopus 로고    scopus 로고
    • Identification of the first archaeal oligopeptide-binding protein from the hyperthermophile Aeropyrum pernix
    • Palmieri, G., A. Casbarra, I. Fiume, G. Catara, A. Capasso, G. Marino, S. Onesti, and M. Rossi. 2006. Identification of the first archaeal oligopeptide-binding protein from the hyperthermophile Aeropyrum pernix. Extremophiles. 10:393-402.
    • (2006) Extremophiles. , vol.10 , pp. 393-402
    • Palmieri, G.1    Casbarra, A.2    Fiume, I.3    Catara, G.4    Capasso, A.5    Marino, G.6    Onesti, S.7    Rossi, M.8
  • 68
    • 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, H.2
  • 69
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J. E., L. Millen, D. Binns, J. F. Hunt, and P. J. Thomas. 2002. Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277:21111-21114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 70
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette: Implications for the structural consequences of ATP hydrolysis in the active site of an ABC-transporter
    • Yuan, Y. R., S. Blecker, O. Martsinkevich, L. Millen, P. J. Thomas, and J. F. Hunt. 2001. The crystal structure of the MJ0796 ATP-binding cassette: Implications for the structural consequences of ATP hydrolysis in the active site of an ABC-transporter. J. Biol. Chem. 276:32313-32321.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 71
    • 0038374988 scopus 로고    scopus 로고
    • Crystal Structures of the ATPase Subunit of the Glucose ABC Transporter from Sulfolobus solfataricus: Nucleotide-free and Nucleotide-bound Conformations
    • Verdon, G., S. V. Albers, B. W. Dijkstra, A. J. Driessen, and A. M. Thunnissen. 2003. Crystal Structures of the ATPase Subunit of the Glucose ABC Transporter from Sulfolobus solfataricus: Nucleotide-free and Nucleotide-bound Conformations. J. Mol. Biol. 330:343-358.
    • (2003) J. Mol. Biol. , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 73
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., G. Lu, J. Lin, A. L. Davidson, and F. A. Quiocho. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12:651-661.
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 74
    • 0031768746 scopus 로고    scopus 로고
    • The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon
    • Panagiotidis, C. H., W. Boos, and H. A. Shuman. 1998. The ATP-binding cassette subunit of the maltose transporter 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
  • 75
    • 0037428467 scopus 로고    scopus 로고
    • TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis
    • Lee, S. J., A. Engelmann, R. Horlacher, Q. Qu, G. Vierke, C. Hebbeln, M. Thomm, and W. Boos. 2003. TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 278:983-990.
    • (2003) J. Biol. Chem. , vol.278 , pp. 983-990
    • Lee, S.J.1    Engelmann, A.2    Horlacher, R.3    Qu, Q.4    Vierke, G.5    Hebbeln, C.6    Thomm, M.7    Boos, W.8
  • 76
    • 25144461083 scopus 로고    scopus 로고
    • TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers
    • Lee, S. J., C. Moulakakis, S. M. Koning, W. Hausner, M. Thomm, and W. Boos. 2005. TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers. Mol. Microbiol. 57:1797-1807.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1797-1807
    • Lee, S.J.1    Moulakakis, C.2    Koning, S.M.3    Hausner, W.4    Thomm, M.5    Boos, W.6
  • 77
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • Karpowich, N., O. Martsinkevich, L. Millen, Y. R. Yuan, P. L. Dai, K. MacVey, P. J. Thomas, and J. F. Hunt. 2001. Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure 9:571-586.
    • (2001) Structure , vol.9 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Millen, L.3    Yuan, Y.R.4    Dai, P.L.5    MacVey, K.6    Thomas, P.J.7    Hunt, J.F.8
  • 78
    • 6344223320 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3
    • Ose, T., T. Fujie, M. Yao, N. Watanabe, and I. Tanaka. 2004. Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3. Proteins 57:635-638.
    • (2004) Proteins , vol.57 , pp. 635-638
    • Ose, T.1    Fujie, T.2    Yao, M.3    Watanabe, N.4    Tanaka, I.5
  • 79
    • 27244444582 scopus 로고    scopus 로고
    • Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc
    • Andrade, S. L., A. Dickmanns, R. Ficner, and O. Einsle. 2005. Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc. Natl. Acad. Sci. U. S. A. 102:14994-14999.
    • (2005) Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14994-14999
    • Andrade, S.L.1    Dickmanns, A.2    Ficner, R.3    Einsle, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.