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Volumn 46, Issue 11, 2007, Pages 3084-3095

Structural and functional analysis of ProQ: An osmoregulatory protein of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

EXTRACELLULAR OSMOLALITY; HOMOLOGY MODELING; NEUTRAL BUFFERS;

EID: 33947405688     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi6023786     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by Bacteria: Signals and membrane-based sensors
    • Wood, J. M. (1999) Osmosensing by Bacteria: signals and membrane-based sensors, Microbiol. Mol. Biol. Rev. 63, 230-262.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 3
    • 0023755693 scopus 로고
    • Proline porter II is activated by a hyperosmotic shift in both whole cells and membrane vesicles of Escherichia coli K12
    • Milner, J. L., Grothe, S., and Wood, J. M. (1988) Proline porter II is activated by a hyperosmotic shift in both whole cells and membrane vesicles of Escherichia coli K12, J. Biol. Chem. 263, 14900-14905.
    • (1988) J. Biol. Chem , vol.263 , pp. 14900-14905
    • Milner, J.L.1    Grothe, S.2    Wood, J.M.3
  • 5
    • 17144398849 scopus 로고    scopus 로고
    • Structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli
    • Wood, J. M., Culham, D. E., Hillar, A., Vernikovska, Ya. I., Liu, F., Boggs, J. M., and Keates, R. A. B. (2005) Structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli, Biochemistry 44, 5634-5646.
    • (2005) Biochemistry , vol.44 , pp. 5634-5646
    • Wood, J.M.1    Culham, D.E.2    Hillar, A.3    Vernikovska, Y.I.4    Liu, F.5    Boggs, J.M.6    Keates, R.A.B.7
  • 6
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M., and Wang, D.-N. (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli, Science 301, 616-620.
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 7
    • 0033833792 scopus 로고    scopus 로고
    • The role of the carboxyl terminal α-helical coiled-coil domain in osmosensing by transporter ProP of Escherichia coli
    • Culham, D. E., Tripet, B., Racher, K. I., Voegele, R. T., Hodges, R. S., and Wood, J. M. (2000) The role of the carboxyl terminal α-helical coiled-coil domain in osmosensing by transporter ProP of Escherichia coli, J. Mol. Recognit. 13, 1-14.
    • (2000) J. Mol. Recognit , vol.13 , pp. 1-14
    • Culham, D.E.1    Tripet, B.2    Racher, K.I.3    Voegele, R.T.4    Hodges, R.S.5    Wood, J.M.6
  • 8
    • 0348224027 scopus 로고    scopus 로고
    • Detection of α-helical coiled-coil dimer formation by spin-labeled synthetic peptides: A model parallel coiled-coil peptide and the antiparallel coiled-coil formed by a replica of the ProP C-terminus
    • Hillar, A., Tripet, B., Zoetewey, D., Wood, J. M., Hodges, R. S., and Boggs, J. M. (2003) Detection of α-helical coiled-coil dimer formation by spin-labeled synthetic peptides: a model parallel coiled-coil peptide and the antiparallel coiled-coil formed by a replica of the ProP C-terminus, Biochemistry 42, 15170-15178.
    • (2003) Biochemistry , vol.42 , pp. 15170-15178
    • Hillar, A.1    Tripet, B.2    Zoetewey, D.3    Wood, J.M.4    Hodges, R.S.5    Boggs, J.M.6
  • 9
    • 0344010237 scopus 로고    scopus 로고
    • Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP
    • Zoetewey, D. L., Tripet, B. P., Kutateladze, T. G., Overduin, M. J., Wood, J. M., and Hodges, R. S. (2003) Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP, J. Mol. Biol. 334, 1063-1076.
    • (2003) J. Mol. Biol , vol.334 , pp. 1063-1076
    • Zoetewey, D.L.1    Tripet, B.P.2    Kutateladze, T.G.3    Overduin, M.J.4    Wood, J.M.5    Hodges, R.S.6
  • 10
    • 23044451841 scopus 로고    scopus 로고
    • Formation of an antiparallel, intermolecular coiled-coil is associated with in vivo dimerization of osmosensor and osmoprotectant transporter ProP in Escherichia coli
    • Hillar, A., Culham, D. E., Vernikovska, Ya. I., Wood, J. M., and Boggs, J. M. (2005) Formation of an antiparallel, intermolecular coiled-coil is associated with in vivo dimerization of osmosensor and osmoprotectant transporter ProP in Escherichia coli, Biochemistry 44, 10170-10180.
    • (2005) Biochemistry , vol.44 , pp. 10170-10180
    • Hillar, A.1    Culham, D.E.2    Vernikovska, Y.I.3    Wood, J.M.4    Boggs, J.M.5
  • 11
    • 29244463867 scopus 로고    scopus 로고
    • The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition
    • Tsatskis, Y., Khambati, J., Dobson, M., Bogdanov, M., Dowhan, W., and Wood, J. M. (2005) The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition, J. Biol. Chem. 280, 41387-41394.
    • (2005) J. Biol. Chem , vol.280 , pp. 41387-41394
    • Tsatskis, Y.1    Khambati, J.2    Dobson, M.3    Bogdanov, M.4    Dowhan, W.5    Wood, J.M.6
  • 12
    • 0024614224 scopus 로고    scopus 로고
    • Milner, J. L., and Wood, J. M. (1989) Insertion proQ220::Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli, J. Bacteriol. 171, 947-951.
    • Milner, J. L., and Wood, J. M. (1989) Insertion proQ220::Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli, J. Bacteriol. 171, 947-951.
  • 13
    • 0033057057 scopus 로고    scopus 로고
    • Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12
    • Kunte, H. J., Crane, R. A., Culham, D. E., Richmond, D., and Wood, J. M. (1999) Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12, J. Bacteriol. 181, 1537-1543.
    • (1999) J. Bacteriol , vol.181 , pp. 1537-1543
    • Kunte, H.J.1    Crane, R.A.2    Culham, D.E.3    Richmond, D.4    Wood, J.M.5
  • 14
    • 5444265451 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of ProQ, a post-translational regulator for osmoregulatory transporter ProP of Escherichia coli
    • Smith, M. N., Crane, R. A., Keates, R. A. B., and Wood, J. M. (2004) Overexpression, purification and characterization of ProQ, a post-translational regulator for osmoregulatory transporter ProP of Escherichia coli, Biochemistry 43, 12979-12989.
    • (2004) Biochemistry , vol.43 , pp. 12979-12989
    • Smith, M.N.1    Crane, R.A.2    Keates, R.A.B.3    Wood, J.M.4
  • 15
    • 0028063103 scopus 로고
    • The FinO protein of IncF plasmids binds FinP antisense RNA and its target, traJ mRNA, and promotes duplex formation
    • van Biesen, T., and Frost, L. S. (1994) The FinO protein of IncF plasmids binds FinP antisense RNA and its target, traJ mRNA, and promotes duplex formation, Mol. Microbiol. 14, 427-436.
    • (1994) Mol. Microbiol , vol.14 , pp. 427-436
    • van Biesen, T.1    Frost, L.S.2
  • 16
    • 0031555481 scopus 로고    scopus 로고
    • X-ray crystal structure and solution fluorescence characterization of Mg.2′(3′)-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain
    • Bauer, C. B., Kuhlman, C. A., Bagshaw, C. R., and Rayment, I. (1997) X-ray crystal structure and solution fluorescence characterization of Mg.2′(3′)-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain, J. Mol. Biol. 274, 394-407.
    • (1997) J. Mol. Biol , vol.274 , pp. 394-407
    • Bauer, C.B.1    Kuhlman, C.A.2    Bagshaw, C.R.3    Rayment, I.4
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids, J. Mol. Biol. 166, 557-569.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-569
    • Hanahan, D.1
  • 19
    • 0026690379 scopus 로고
    • Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
    • Brown, E. D., and Wood, J. M. (1992) Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli, J. Biol. Chem. 267, 13086-13092.
    • (1992) J. Biol. Chem , vol.267 , pp. 13086-13092
    • Brown, E.D.1    Wood, J.M.2
  • 20
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • 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
  • 21
  • 22
    • 0037457916 scopus 로고    scopus 로고
    • Osmosensor ProP of Escherichia coli responds to the concentration, chemistry and molecular size of osmolytes in the proteoliposome lumen
    • Culham, D. E., Henderson, J., Crane, R. A., and Wood, J. M. (2003) Osmosensor ProP of Escherichia coli responds to the concentration, chemistry and molecular size of osmolytes in the proteoliposome lumen, Biochemistry 42, 410-420.
    • (2003) Biochemistry , vol.42 , pp. 410-420
    • Culham, D.E.1    Henderson, J.2    Crane, R.A.3    Wood, J.M.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 25
    • 32344443865 scopus 로고    scopus 로고
    • Characterization of the major capsid proteins of myxoma virus particles using MALDI-TOF mass spectrometry
    • Zachertowska, A., Brewer, D., and Evans, D. H. (2006) Characterization of the major capsid proteins of myxoma virus particles using MALDI-TOF mass spectrometry, J. Virol. Methods 132, 1-12.
    • (2006) J. Virol. Methods , vol.132 , pp. 1-12
    • Zachertowska, A.1    Brewer, D.2    Evans, D.H.3
  • 26
    • 0034213595 scopus 로고    scopus 로고
    • Propound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang, W., and Chait, B. T. (2000) Propound: an expert system for protein identification using mass spectrometric peptide mapping information, Anal. Chem. 72, 2482-2489.
    • (2000) Anal. Chem , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2
  • 27
    • 16644402929 scopus 로고    scopus 로고
    • A preliminary solubility screen used to improve crystal trials: Crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1
    • Collins, B. K., Tomanicek, S. J., Lyamicheva, N., Kaiser, M. W., and Meuser, T. C. (2004) A preliminary solubility screen used to improve crystal trials: crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1, Acta Crystallogr., Sect. D 60, 1674-1678.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 1674-1678
    • Collins, B.K.1    Tomanicek, S.J.2    Lyamicheva, N.3    Kaiser, M.W.4    Meuser, T.C.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 30
    • 0021031927 scopus 로고
    • Two proline porters in Escherichia coli K-12
    • Stalmach, M. E., Grothe, S., and Wood, J. M. (1983) Two proline porters in Escherichia coli K-12, J. Bacterial 156, 481-486.
    • (1983) J. Bacterial , vol.156 , pp. 481-486
    • Stalmach, M.E.1    Grothe, S.2    Wood, J.M.3
  • 31
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B. J. (2001) SH3 domains: complexity in moderation, J. Cell Sci. 114, 1253-1263.
    • (2001) J. Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 32
    • 0032542018 scopus 로고    scopus 로고
    • Mutagenesis of a buried polar interaction in an SH3 domain: Sequence conservation provides the best prediction of stability effects
    • Maxwell, K., and Davidson, A. R. (1998) Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects, Biochemistry 37, 16172-16182.
    • (1998) Biochemistry , vol.37 , pp. 16172-16182
    • Maxwell, K.1    Davidson, A.R.2
  • 33
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.-M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter, J. Bacterial. 177, 4121-4130.
    • (1995) J. Bacterial , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4


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