메뉴 건너뛰기




Volumn 2, Issue 1, 2011, Pages

Regulation of the co-evolved HrpR and HrpS AAA+ proteins required for Pseudomonas syringae pathogenicity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN AAA; PROTEIN HRPR; PROTEIN HRPS; RNA POLYMERASE; UNCLASSIFIED DRUG; BETA GALACTOSIDASE; DNA BINDING PROTEIN; HRPL PROTEIN, PSEUDOMONAS SYRINGAE; HRPR PROTEIN, PSEUDOMONAS SYRINGAE; HRPS PROTEIN, PSEUDOMONAS SYRINGAE; MULTIPROTEIN COMPLEX; SIGMA FACTOR; SIGMA FACTOR RPON; TRANSCRIPTION FACTOR;

EID: 79551611518     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1177     Document Type: Article
Times cited : (87)

References (58)
  • 1
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan, J. E. & Wolf-Watz, H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444, 567-573 (2006).
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 2
    • 12944273613 scopus 로고    scopus 로고
    • Pseudomonas syringae Hrp type III secretion system and efector proteins
    • Collmer, A. et al. Pseudomonas syringae Hrp type III secretion system and efector proteins. Proc. Natl Acad. Sci USA 97, 8770-8777 (2000).
    • (2000) Proc. Natl Acad. Sci USA , vol.97 , pp. 8770-8777
    • Collmer, A.1
  • 3
    • 0034038637 scopus 로고    scopus 로고
    • Te alternative sigma factor RpoN is required for hrp activity in Pseudomonas syringae pv. maculicola and acts at the level of hrpL transcription
    • Hendrickson, E. L., Guevera, P. & Ausubel, F. M. Te alternative sigma factor RpoN is required for hrp activity in Pseudomonas syringae pv. maculicola and acts at the level of hrpL transcription. J. Bacteriol. 182, 3508-3516 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 3508-3516
    • Hendrickson, E.L.1    Guevera, P.2    Ausubel, F.M.3
  • 4
  • 5
    • 0027340543 scopus 로고
    • Te sigma 54 bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains
    • Morett, E. & Segovia, L. Te sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 175, 6067-6074 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 6
    • 33749256408 scopus 로고    scopus 로고
    • Structures and organisation of AAA+ enhancer binding proteins in transcriptional activation
    • Schumacher, J., Joly, N., Rappas, M., Zhang, X. & Buck, M. Structures and organisation of AAA+ enhancer binding proteins in transcriptional activation. J. Struct. Biol. 156, 190-199 (2006).
    • (2006) J. Struct. Biol. , vol.156 , pp. 190-199
    • Schumacher, J.1    Joly, N.2    Rappas, M.3    Zhang, X.4    Buck, M.5
  • 7
    • 33750208366 scopus 로고    scopus 로고
    • Regulation of the type III secretion system in phytopathogenic bacteria
    • Tang, X., Xiao, Y. & Zhou, J. M. Regulation of the type III secretion system in phytopathogenic bacteria. Mol. Plant Microbe Interact. 19, 1159-1166 (2006).
    • (2006) Mol. Plant Microbe Interact. , vol.19 , pp. 1159-1166
    • Tang, X.1    Xiao, Y.2    Zhou, J.M.3
  • 8
    • 0034836583 scopus 로고    scopus 로고
    • Enhancer-binding proteins HrpR and HrpS interact to regulate hrp-encoded type III protein secretion in Pseudomonas syringae strains
    • Hutcheson, S. W., Bretz, J., Sussan, T., Jin, S. & Pak, K. Enhancer-binding proteins HrpR and HrpS interact to regulate hrp-encoded type III protein secretion in Pseudomonas syringae strains. J. Bacteriol. 183, 5589-5598 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 5589-5598
    • Hutcheson, S.W.1    Bretz, J.2    Sussan, T.3    Jin, S.4    Pak, K.5
  • 9
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly operation and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. & Koonin, E. V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 10
    • 33744780177 scopus 로고    scopus 로고
    • Te structural basis for regulated assembly and function of the transcriptional activator NtrC
    • De Carlo, S. et al. T e structural basis for regulated assembly and function of the transcriptional activator NtrC. Genes Dev. 20, 1485-1495 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 1485-1495
    • De Carlo, S.1
  • 11
    • 0036293607 scopus 로고    scopus 로고
    • Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspF
    • Elderkin, S., Jones, S., Schumacher, J., Studholme, D. & Buck, M. Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspF. J. Mol. Biol. 320, 23-37 (2002).
    • (2002) J. Mol. Biol. , vol.320 , pp. 23-37
    • Elderkin, S.1    Jones, S.2    Schumacher, J.3    Studholme, D.4    Buck, M.5
  • 12
    • 0031783182 scopus 로고    scopus 로고
    • Negative regulation of hrp genes in Pseudomonas syringae by HrpV
    • Preston, G., Deng, W. L., Huang, H. C. & Collmer, A. Negative regulation of hrp genes in Pseudomonas syringae by HrpV. J. Bacteriol. 180, 4532-4537 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 4532-4537
    • Preston, G.1    Deng, W.L.2    Huang, H.C.3    Collmer, A.4
  • 13
    • 22144492266 scopus 로고    scopus 로고
    • A chaperone-like HrpG protein acts as a suppressor of HrpV in regulation of the Pseudomonas syringae pv. syringae type III secretion system
    • Wei, C. F., Deng, W. L. & Huang, H. C. A chaperone-like HrpG protein acts as a suppressor of HrpV in regulation of the Pseudomonas syringae pv. syringae type III secretion system. Mol. Microbiol. 57, 520-536 (2005).
    • (2005) Mol. Microbiol. , vol.57 , pp. 520-536
    • Wei, C.F.1    Deng, W.L.2    Huang, H.C.3
  • 14
    • 59049088137 scopus 로고    scopus 로고
    • Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase
    • Barry, E. R., Lovett, J. E., Costa, A., Lea, S. M. & Bell, S. D. Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase. Proc Natl Acad. Sci. USA 106, 1051-1056 (2009).
    • (2009) Proc Natl Acad. Sci. USA , vol.106 , pp. 1051-1056
    • Barry, E.R.1    Lovett, J.E.2    Costa, A.3    Lea, S.M.4    Bell, S.D.5
  • 15
    • 0035930346 scopus 로고    scopus 로고
    • Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication
    • Schwacha, A. & Bell, S. P. Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication. Mol. Cell 8, 1093-1104 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1093-1104
    • Schwacha, A.1    Bell, S.P.2
  • 16
    • 77950590422 scopus 로고    scopus 로고
    • Negative regulation of the Hrp type III secretion system in Pseudomonas syringae pv. phaseolicola
    • Ortiz-Martin, I., Twaites, R., Mansfeld, J. W. & Beuzon, C R. Negative regulation of the Hrp type III secretion system in Pseudomonas syringae pv. phaseolicola. Mol. Plant Microbe Interact. 23, 682-701 (2010).
    • (2010) Mol. Plant Microbe Interact. , vol.23 , pp. 682-701
    • Ortiz-Martin, I.1    Twaites, R.2    Mansfeld, J.W.3    Beuzon, C.R.4
  • 17
    • 34250664205 scopus 로고    scopus 로고
    • Mutation of Lon protease diferentially afects the expression of Pseudomonas syringae type III secretion system genes in rich and minimal media and reduces pathogenicity
    • Lan, L., Deng, X., Xiao, Y., Zhou, J. M. & Tang, X. Mutation of Lon protease diferentially afects the expression of Pseudomonas syringae type III secretion system genes in rich and minimal media and reduces pathogenicity Mol. Plant Microbe Interact. 20, 682-696 (2007).
    • (2007) Mol Plant Microbe Interact. , vol.20 , pp. 682-696
    • Lan, L.1    Deng, X.2    Xiao, Y.3    Zhou, J.M.4    Tang, X.5
  • 18
    • 0344495391 scopus 로고    scopus 로고
    • GacA, the response regulator of a two-component system, acts as a master regulator in Pseudomonas syringae pv. tomato DC3000 by controlling regulatory RNA, transcriptional activators, and alternate sigma factors
    • Chatterjee, A. et al. GacA, the response regulator of a two-component system, acts as a master regulator in Pseudomonas syringae pv. tomato DC3000 by controlling regulatory RNA, transcriptional activators, and alternate sigma factors. Mol. Plant Microbe Interact. 16, 1106-1117 (2003).
    • (2003) Mol. Plant Microbe Interact. , vol.16 , pp. 1106-1117
    • Chatterjee, A.1
  • 19
    • 0036065408 scopus 로고    scopus 로고
    • Lon protease functions as a negative regulator of type III protein secretion in Pseudomonas syringae
    • Bretz, J., Losada, L., Lisboa, K. & Hutcheson, S. W. Lon protease functions as a negative regulator of type III protein secretion in Pseudomonas syringae. Mol. Microbiol 45, 397-409 (2002).
    • (2002) Mol. Microbiol , vol.45 , pp. 397-409
    • Bretz, J.1    Losada, L.2    Lisboa, K.3    Hutcheson, S.W.4
  • 20
    • 0033865962 scopus 로고    scopus 로고
    • Phylogenetic afliation of the pseudomonads based on 16S rRNA sequence
    • Anzai, Y., Kim, H., Park, J. Y, Wakabayashi, H. & Oyaizu, H. Phylogenetic afliation of the pseudomonads based on 16S rRNA sequence. Int. J. Syst. Evol. Microbiol 50 (Pt 4), 1563-1589 (2000).
    • (2000) Int. J. Syst. Evol. Microbiol , vol.50 , Issue.PART 4 , pp. 1563-1589
    • Anzai, Y.1    Kim, H.2    Park, J.Y.3    Wakabayashi, H.4    Oyaizu, H.5
  • 21
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: How duplicated genes fnd new functions
    • Conant, G. C & Wolfe, K. H. Turning a hobby into a job: how duplicated genes fnd new functions. Nat Rev. Genet 9, 938-950 (2008).
    • (2008) Nat Rev. Genet , vol.9 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 22
    • 59049099861 scopus 로고    scopus 로고
    • Genetic redundancy: New tricks for old genes
    • Kafri, R., Springer, M. & Pilpel, Y Genetic redundancy: new tricks for old genes. Cell 136, 389-392 (2009).
    • (2009) Cell , vol.136 , pp. 389-392
    • Kafri, R.1    Springer, M.2    Pilpel, Y.3
  • 23
    • 21244482459 scopus 로고    scopus 로고
    • Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: Allosteric control of a protein machine
    • Hersch, G. L., Burton, R. E., Bolon, D. N., Baker, T. A. & Sauer, R. T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121, 1017-1027 (2005).
    • (2005) Cell , vol.121 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 24
    • 46649088723 scopus 로고    scopus 로고
    • Mechanism of homotropic control to coordinate hydrolysis in a hexameric AAA+ ring ATPase
    • Schumacher, J. et al. Mechanism of homotropic control to coordinate hydrolysis in a hexameric AAA+ ring ATPase. J. Mol. Biol. 381, 1-12 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 1-12
    • Schumacher, J.1
  • 25
    • 35448968986 scopus 로고    scopus 로고
    • Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein
    • Joly, N., Rappas, M., Wigneshweraraj, S. R., Zhang, X. & Buck, M. Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein. Mol. Microbiol. 66, 583-595 (2007).
    • (2007) Mol. Microbiol. , vol.66 , pp. 583-595
    • Joly, N.1    Rappas, M.2    Wigneshweraraj, S.R.3    Zhang, X.4    Buck, M.5
  • 26
    • 33344469160 scopus 로고    scopus 로고
    • Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF
    • Rappas, M., Schumacher, J., Niwa, H., Buck, M. & Zhang, X. Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF. J. Mol. Biol. 357, 481-492 (2006).
    • (2006) J. Mol. Biol. , vol.357 , pp. 481-492
    • Rappas, M.1    Schumacher, J.2    Niwa, H.3    Buck, M.4    Zhang, X.5
  • 27
    • 0037418230 scopus 로고    scopus 로고
    • Te ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: Identifying a surface that binds sigma 54
    • Bordes, P. et al. T e ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54. Proc. Natl Acad. Sci. USA 100, 2278-2283 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2278-2283
    • Bordes, P.1
  • 28
    • 0035449829 scopus 로고    scopus 로고
    • Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fuoride: Insights into activator mechanochemical action
    • Chaney, M. et al. Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fuoride: insights into activator mechanochemical action. Genes Dev. 15, 2282-2294 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2282-2294
    • Chaney, M.1
  • 29
    • 34047267824 scopus 로고    scopus 로고
    • ATP ground-and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54
    • Chen, B. et al. ATP ground-and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54. Structure 15, 429-440 (2007).
    • (2007) Structure , vol.15 , pp. 429-440
    • Chen, B.1
  • 30
    • 20144366027 scopus 로고    scopus 로고
    • Structural insights into the activity of enhancer-binding proteins
    • Rappas, M. et al. Structural insights into the activity of enhancer-binding proteins. Science 307, 1972-1975 (2005).
    • (2005) Science , vol.307 , pp. 1972-1975
    • Rappas, M.1
  • 31
    • 70350642059 scopus 로고    scopus 로고
    • Te role of the conserved phenylalanine in the sigma54-interacting GAFTGA motif of bacterial enhancer binding proteins
    • Zhang, N. et al. T e role of the conserved phenylalanine in the sigma54-interacting GAFTGA motif of bacterial enhancer binding proteins. Nucleic Acids Res. 37, 5981-5992 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5981-5992
    • Zhang, N.1
  • 32
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A. & Ladant, D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway Proc. Natl Acad. Sci. USA 95, 5752-5756 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 33
    • 0033536573 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of NtrC with three alanine substitutions
    • Pelton, J. G., Kustu, S. & Wemmer, D. E. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J. Mol. Biol. 292, 1095-1110 (1999).
    • (1999) J. Mol. Biol. , vol.292 , pp. 1095-1110
    • Pelton, J.G.1    Kustu, S.2    Wemmer, D.E.3
  • 34
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains
    • Lee, S. Y. et al. Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains. Genes Dev. 17, 2552-2563 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1
  • 35
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., Dautin, N. & Ladant, D. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187, 2233-2243 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 36
    • 0028038233 scopus 로고
    • Cross-regulation by XylR and DmpR activators of Pseudomonas putida suggests that transcriptional control of biodegradative operons evolves independently of catabolic genes
    • Fernandez, S., Shingler, V. & De Lorenzo, V. Cross-regulation by XylR and DmpR activators of Pseudomonas putida suggests that transcriptional control of biodegradative operons evolves independently of catabolic genes. J. Bacteriol. 176, 5052-5058 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 5052-5058
    • Fernandez, S.1    Shingler, V.2    De Lorenzo, V.3
  • 37
    • 0141925851 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in the sigma54-dependent activator DctD
    • Wang, Y. K., Park, S., Nixon, B. T. & Hoover, T. R. Nucleotide-dependent conformational changes in the sigma54-dependent activator DctD. J. Bacteriol. 185, 6215-6219 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 6215-6219
    • Wang, Y.K.1    Park, S.2    Nixon, B.T.3    Hoover, T.R.4
  • 38
    • 0029166594 scopus 로고
    • Te bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation
    • Wedel, A. & Kustu, S. Te bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 9, 2042-2052 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2042-2052
    • Wedel, A.1    Kustu, S.2
  • 39
    • 2142707172 scopus 로고    scopus 로고
    • ATP-dependent transcriptional activation by bacterial PspF AAA+protein
    • Schumacher, J., Zhang, X., Jones, S., Bordes, P. & Buck, M. ATP-dependent transcriptional activation by bacterial PspF AAA+protein. J. Mol. Biol. 338, 863-875 (2004).
    • (2004) J. Mol. Biol. , vol.338 , pp. 863-875
    • Schumacher, J.1    Zhang, X.2    Jones, S.3    Bordes, P.4    Buck, M.5
  • 40
    • 39449114777 scopus 로고    scopus 로고
    • Regulation and action of the bacterial enhancer-binding protein AAA+ domains
    • Chen, B., Sysoeva, T. A., Chowdhury, S. & Nixon, B. T. Regulation and action of the bacterial enhancer-binding protein AAA+ domains. Biochem. Soc Trans. 36, 89-93 (2008).
    • (2008) Biochem. Soc Trans. , vol.36 , pp. 89-93
    • Chen, B.1    Sysoeva, T.A.2    Chowdhury, S.3    Nixon, B.T.4
  • 41
    • 0028888881 scopus 로고
    • In vitro studies of the domains of the nitrogen fxation regulatory protein NIFA
    • Berger, D. K., Narberhaus, F., Lee, H. S. & Kustu, S. In vitro studies of the domains of the nitrogen fxation regulatory protein NIFA. J. Bacteriol. 177, 191-199 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 191-199
    • Berger, D.K.1    Narberhaus, F.2    Lee, H.S.3    Kustu, S.4
  • 42
    • 37649013167 scopus 로고    scopus 로고
    • Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fuoride
    • Joly, N., Rappas, M., Buck, M. & Zhang, X. Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fuoride. J. Mol. Biol. 375, 1206-1211 (2008).
    • (2008) J. Mol. Biol. , vol.375 , pp. 1206-1211
    • Joly, N.1    Rappas, M.2    Buck, M.3    Zhang, X.4
  • 43
    • 77950363329 scopus 로고    scopus 로고
    • Essential roles of three enhancer sites in {sigma}54-dependent transcription by the nitric oxide sensing regulatory protein NorR
    • Tucker, N. P, Ghosh, T., Bush, M., Zhang, X. & Dixon, R. Essential roles of three enhancer sites in {sigma}54-dependent transcription by the nitric oxide sensing regulatory protein NorR. Nucleic Acids Res. 38, 1182-1194 (2009).
    • (2009) Nucleic Acids Res. , vol.38 , pp. 1182-1194
    • Tucker, N.P.1    Ghosh, T.2    Bush, M.3    Zhang, X.4    Dixon, R.5
  • 44
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
    • Martin, A., Baker, T. A. & Sauer, R. T. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines. Nature 437, 1115-1120 (2005).
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 45
    • 34248206721 scopus 로고    scopus 로고
    • Sensor i threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of {sigma}54-RNA polymerase
    • Schumacher, J. et al. Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of {sigma}54-RNA polymerase. J. Biol. Chem. 282, 9825-9833 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 9825-9833
    • Schumacher, J.1
  • 47
    • 0032766242 scopus 로고    scopus 로고
    • MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein
    • Rombel, I. et al. MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein. J. Bacteriol. 181, 4628-4638 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 4628-4638
    • Rombel, I.1
  • 48
  • 49
    • 75549087305 scopus 로고    scopus 로고
    • Te evolution of gene duplications: Classifying and distinguishing between models
    • Innan, H. & Kondrashov, F. T e evolution of gene duplications: classifying and distinguishing between models. Nat. Rev. Genet 11, 97-108 (2010).
    • (2010) Nat. Rev. Genet , vol.11 , pp. 97-108
    • Innan, H.1    Kondrashov, F.2
  • 51
    • 0035150957 scopus 로고    scopus 로고
    • Concerted inhibition of the transcriptional activation functions of the enhancer-binding protein NIFA by the anti-activator NIFL
    • Barrett, J., Ray P., Sobczyk, A., Little, R. & Dixon, R. Concerted inhibition of the transcriptional activation functions of the enhancer-binding protein NIFA by the anti-activator NIFL. Mol. Microbiol. 39, 480-493 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 480-493
    • Barrett, J.1    Ray, P.2    Sobczyk, A.3    Little, R.4    Dixon, R.5
  • 52
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: Adaptor proteins for Hsp100/Clp and AAA+ proteases
    • Kirstein, J., Moliere, N., Dougan, D. A. & Turgay K. Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nat Rev. Microbiol. 7, 589-599 (2009).
    • (2009) Nat Rev. Microbiol. , vol.7 , pp. 589-599
    • Kirstein, J.1    Moliere, N.2    Dougan, D.A.3    Turgay, K.4
  • 53
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • Puri, T., Wendler, P, Sigala, B., Saibil, H. & Tsaneva, I. R. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J. Mol. Biol. 366, 179-192 (2007).
    • (2007) J. Mol. Biol. , vol.366 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 54
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., Houman, F. & Kleckner, N. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53, 85-96 (1987).
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 55
    • 0032570006 scopus 로고    scopus 로고
    • A new system to place single copies of genes, sites and lacZ fusions on the Escherichia coli chromosome
    • Yu, D. & Court, D. L. A new system to place single copies of genes, sites and lacZ fusions on the Escherichia coli chromosome. Gene 223, 77-81 (1998).
    • (1998) Gene , vol.223 , pp. 77-81
    • Yu, D.1    Court, D.L.2
  • 57
    • 0023408583 scopus 로고
    • Overproduction of Escherichia coli integration host factor, a protein with nonidentical subunits
    • Nash, H. A., Robertson, C A., Flamm, E., Weisberg, R. A. & Miller, H. I. Overproduction of Escherichia coli integration host factor, a protein with nonidentical subunits. J. Bacteriol. 169, 4124-4127 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 4124-4127
    • Nash, H.A.1    Robertson, C.A.2    Flamm, E.3    Weisberg, R.A.4    Miller, H.I.5
  • 58
    • 69849092792 scopus 로고    scopus 로고
    • Functional roles of the pre-sensor i insertion sequence in an AAA+ bacterial enhancer binding protein
    • Burrows, P. C et al. Functional roles of the pre-sensor I insertion sequence in an AAA+ bacterial enhancer binding protein. Mol. Microbiol. 73, 519-533 (2009).
    • (2009) Mol. Microbiol. , vol.73 , pp. 519-533
    • Burrows, P.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.