메뉴 건너뛰기




Volumn 23, Issue 1, 2009, Pages 93-104

Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression

Author keywords

Caulobacter crescentus; Cell cycle; Cyclic di gmp; Popa; Protein degradation; Second messenger

Indexed keywords

CYCLIC GMP; NUCLEIC ACID BINDING PROTEIN; PROTEIN POPA; PROTEIN RCDA; REPLICATION INITIATOR PROTEIN CTRA; UNCLASSIFIED DRUG;

EID: 58149485506     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.502409     Document Type: Article
Times cited : (251)

References (59)
  • 2
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge, P., Paul, R., Goymer, P., Rainey, P., and Jenal, U. 2003. Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol. Microbiol. 47: 1695-1708.
    • (2003) Mol. Microbiol , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 7
    • 31444436935 scopus 로고    scopus 로고
    • Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease
    • Chen, J.C., Hottes, A.K., McAdams, H.H., McGrath, P.T., Viollier, P.H., and Shapiro, L. 2006. Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease. EMBO J. 25: 377-386.
    • (2006) EMBO J , vol.25 , pp. 377-386
    • Chen, J.C.1    Hottes, A.K.2    McAdams, H.H.3    McGrath, P.T.4    Viollier, P.H.5    Shapiro, L.6
  • 8
    • 34249855507 scopus 로고    scopus 로고
    • Direct and adaptor-mediated substrate recognition by an essential AAA+ protease
    • Chien, P., Perchuk, B.S., Laub, M.T., Sauer, R.T., and Baker, T.A. 2007. Direct and adaptor-mediated substrate recognition by an essential AAA+ protease. Proc. Natl. Acad. Sci. 104: 6590-6595.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 6590-6595
    • Chien, P.1    Perchuk, B.S.2    Laub, M.T.3    Sauer, R.T.4    Baker, T.A.5
  • 9
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen, M., Christen, B., Folcher, M., Schauerte, A., and Jenal, U. 2005. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 280: 30829-30837.
    • (2005) J. Biol. Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 11
    • 0030747761 scopus 로고    scopus 로고
    • Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle
    • Domian, I.J., Quon, K.C., and Shapiro, L. 1997. Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 90: 415-424.
    • (1997) Cell , vol.90 , pp. 415-424
    • Domian, I.J.1    Quon, K.C.2    Shapiro, L.3
  • 12
    • 0033536009 scopus 로고    scopus 로고
    • Feedback control of a master bacterial cell-cycle regulator
    • Domian, I.J., Reisenauer, A., and Shapiro, L. 1999. Feedback control of a master bacterial cell-cycle regulator. Proc. Natl. Acad. Sci. 96: 6648-6653.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 6648-6653
    • Domian, I.J.1    Reisenauer, A.2    Shapiro, L.3
  • 13
    • 0025888266 scopus 로고
    • Genetics of Caulobacter crescentus
    • Ely, B., 1991. Genetics of Caulobacter crescentus. Methods Enzymol. 204: 372-384.
    • (1991) Methods Enzymol , vol.204 , pp. 372-384
    • Ely, B.1
  • 14
    • 36049032519 scopus 로고    scopus 로고
    • 2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages
    • 2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages. Proc. Natl. Acad. Sci. 104: 16176-16181.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 16176-16181
    • Evans, J.H.1    Falke, J.J.2
  • 15
    • 0034596991 scopus 로고    scopus 로고
    • Subunit-specific degradation of the UmuD/D' hetero-dimer by the ClpXP protease: The role of trans recognition in UmuD' stability
    • Gonzalez, M., Rasulova, F., Maurizi, M.R., and Woodgate, R. 2000. Subunit-specific degradation of the UmuD/D' hetero-dimer by the ClpXP protease: The role of trans recognition in UmuD' stability. EMBO J. 19: 5251-5258.
    • (2000) EMBO J , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 16
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S., 2003. Proteolysis in bacterial regulatory circuits. Annu. Rev. Cell Dev. Biol. 19: 565-587.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 18
    • 0037329155 scopus 로고    scopus 로고
    • The Caulobacter crescentus polar organelle development protein PodJ is differentially localized and is required for polar targeting of the PleC development regulator
    • Hinz, A.J., Larson, D.E., Smith, C.S., and Brun, Y.V. 2003. The Caulobacter crescentus polar organelle development protein PodJ is differentially localized and is required for polar targeting of the PleC development regulator. Mol. Microbiol. 47: 929-941.
    • (2003) Mol. Microbiol , vol.47 , pp. 929-941
    • Hinz, A.J.1    Larson, D.E.2    Smith, C.S.3    Brun, Y.V.4
  • 19
    • 33746610535 scopus 로고    scopus 로고
    • A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression
    • Iniesta, A.A., McGrath, P.T., Reisenauer, A., McAdams, H.H., and Shapiro, L. 2006. A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression. Proc. Natl. Acad. Sci. 103: 10935-10940.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 10935-10940
    • Iniesta, A.A.1    McGrath, P.T.2    Reisenauer, A.3    McAdams, H.H.4    Shapiro, L.5
  • 20
    • 36549007483 scopus 로고    scopus 로고
    • Chemotaxis in Dictyostelium: How to walk straight using parallel pathways
    • Insall, R., and Andrew, N. 2007. Chemotaxis in Dictyostelium: How to walk straight using parallel pathways. Curr. Opin. Microbiol. 10: 578-581.
    • (2007) Curr. Opin. Microbiol , vol.10 , pp. 578-581
    • Insall, R.1    Andrew, N.2
  • 21
    • 16244377763 scopus 로고    scopus 로고
    • Temporal and spatial regulation of phos-phoinositide signaling mediates cytokinesis
    • Janetopoulos, C., Borleis, J., Vazquez, F., Iijima, M., and Devreotes, P. 2005. Temporal and spatial regulation of phos-phoinositide signaling mediates cytokinesis. Dev. Cell 8: 467-477.
    • (2005) Dev. Cell , vol.8 , pp. 467-477
    • Janetopoulos, C.1    Borleis, J.2    Vazquez, F.3    Iijima, M.4    Devreotes, P.5
  • 22
    • 0032189273 scopus 로고    scopus 로고
    • An essential protease involved in bacterial cell-cycle control
    • Jenal, U. and Fuchs, T. 1998. An essential protease involved in bacterial cell-cycle control. EMBO J. 17: 5658-5669.
    • (1998) EMBO J , vol.17 , pp. 5658-5669
    • Jenal, U.1    Fuchs, T.2
  • 23
    • 0038690474 scopus 로고    scopus 로고
    • Regulation by proteolysis in bacterial cells
    • Jenal, U. and Hengge-Aronis, R. 2003. Regulation by proteolysis in bacterial cells. Curr. Opin. Microbiol. 6: 163-172.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 163-172
    • Jenal, U.1    Hengge-Aronis, R.2
  • 24
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal, U. and Malone, J. 2006. Mechanisms of cyclic-di-GMP signaling in bacteria. Annu. Rev. Genet. 40: 385-407.
    • (2006) Annu. Rev. Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 25
    • 0029936883 scopus 로고    scopus 로고
    • Cell cycle-controlled proteolysis of a flagellar motor protein that is asymmetrically distributed in the Caulobacter predivisional cell
    • Jenal, U. and Shapiro, L. 1996. Cell cycle-controlled proteolysis of a flagellar motor protein that is asymmetrically distributed in the Caulobacter predivisional cell. EMBO J. 15: 2393-2406.
    • (1996) EMBO J , vol.15 , pp. 2393-2406
    • Jenal, U.1    Shapiro, L.2
  • 26
    • 0032825041 scopus 로고    scopus 로고
    • Differential protease- mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli
    • Johansson, U. and Uhlin, B.E. 1999. Differential protease- mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli. Proc. Natl. Acad. Sci. 96: 10776-10781.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 10776-10781
    • Johansson, U.1    Uhlin, B.E.2
  • 27
    • 33645819810 scopus 로고    scopus 로고
    • Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium
    • Kader, A., Simm, R., Gerstel, U., Morr, M., and Romling, U. 2006. Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 60: 602-616.
    • (2006) Mol. Microbiol , vol.60 , pp. 602-616
    • Kader, A.1    Simm, R.2    Gerstel, U.3    Morr, M.4    Romling, U.5
  • 29
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. 1998. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. 95: 5752-5756.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 30
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K.C., Waller, P.R., and Sauer, R.T. 1996. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 31
    • 0348010311 scopus 로고    scopus 로고
    • Crystal structure of ClpX molecular chaperone from Helicobacter pylori
    • Kim, D.Y. and Kim, K.K. 2003. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J. Biol. Chem. 278: 50664-50670.
    • (2003) J. Biol. Chem , vol.278 , pp. 50664-50670
    • Kim, D.Y.1    Kim, K.K.2
  • 32
  • 33
    • 31444440985 scopus 로고    scopus 로고
    • Dissection of functional domains of the polar localization factor PodJ in Caulobacter crescentus
    • Lawler, M.L., Larson, D.E., Hinz, A.J., Klein, D., and Brun, Y.V. 2006. Dissection of functional domains of the polar localization factor PodJ in Caulobacter crescentus. Mol. Microbiol. 59: 301-316.
    • (2006) Mol. Microbiol , vol.59 , pp. 301-316
    • Lawler, M.L.1    Larson, D.E.2    Hinz, A.J.3    Klein, D.4    Brun, Y.V.5
  • 34
    • 33745898224 scopus 로고    scopus 로고
    • Holdfast formation in motile Swarmer cells optimizes surface attachment during Caulo-bacter crescentus development
    • Levi, A. and Jenal, U. 2006. Holdfast formation in motile Swarmer cells optimizes surface attachment during Caulo-bacter crescentus development. J. Bacteriol. 188: 5315-5318.
    • (2006) J. Bacteriol , vol.188 , pp. 5315-5318
    • Levi, A.1    Jenal, U.2
  • 35
    • 33645296297 scopus 로고    scopus 로고
    • Cyclic-di-GMP signal transduction systems in Vibrio cholerae: Modulation of rugosity and biofilm formation
    • Lim, B., Beyhan, S., Meir, J., and Yildiz, F.H. 2006. Cyclic-di-GMP signal transduction systems in Vibrio cholerae: Modulation of rugosity and biofilm formation. Mol. Microbiol. 60: 331-348.
    • (2006) Mol. Microbiol , vol.60 , pp. 331-348
    • Lim, B.1    Beyhan, S.2    Meir, J.3    Yildiz, F.H.4
  • 36
    • 34247202706 scopus 로고    scopus 로고
    • The structure-function relationship of WspR; a Pseudomonas fluorescens response regulator with a GGDEF output domain
    • Malone, J.G., Williams, R., Christen, M., Spiers, A.J., Jenal, U., and Rainey, P.B. 2006. The structure-function relationship of WspR; a Pseudomonas fluorescens response regulator with a GGDEF output domain. Microbiology 153: 980-994.
    • (2006) Microbiology , vol.153 , pp. 980-994
    • Malone, J.G.1    Williams, R.2    Christen, M.3    Spiers, A.J.4    Jenal, U.5    Rainey, P.B.6
  • 37
    • 32044454838 scopus 로고    scopus 로고
    • A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator
    • McGrath, P.T., Iniesta, A.A., Ryan, K.R., Shapiro, L., and McAdams, H.H. 2006. A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator. Cell 124: 535-547.
    • (2006) Cell , vol.124 , pp. 535-547
    • McGrath, P.T.1    Iniesta, A.A.2    Ryan, K.R.3    Shapiro, L.4    McAdams, H.H.5
  • 38
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki, A., and Tsien, R.Y. 2000. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol. 327: 472-500.
    • (2000) Methods Enzymol , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 39
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di- guanylate cyclase output domain
    • Paul, R., Weiser, S., Amiot, N.C., Chan, C., Schirmer, T., Giese, B., and Jenal, U. 2004. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di- guanylate cyclase output domain. Genes & Dev. 18: 715-727.
    • (2004) Genes & Dev , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 40
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase pleD by phosphorylation-mediated dimerization
    • Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H., and Jenal, U. 2007. Activation of the diguanylate cyclase pleD by phosphorylation-mediated dimerization. J. Biol. Chem. 282: 29170-29177.
    • (2007) J. Biol. Chem , vol.282 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 41
    • 42949140533 scopus 로고    scopus 로고
    • Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate
    • Paul, R., Jaeger, T., Abel, S., Wiederkehr, I., Folcher, M., Biondi, E.G., Laub, M.T., and Jenal, U. 2008. Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate. Cell 133: 452-461.
    • (2008) Cell , vol.133 , pp. 452-461
    • Paul, R.1    Jaeger, T.2    Abel, S.3    Wiederkehr, I.4    Folcher, M.5    Biondi, E.G.6    Laub, M.T.7    Jenal, U.8
  • 42
    • 0031940593 scopus 로고    scopus 로고
    • Negative control of bacterial DNA replication by a cell cycle regulatory protein that binds at the chromosome origin
    • Quon, K.C., Yang, B., Domian, I.J., Shapiro, L., and Marczynski, G.T. 1998. Negative control of bacterial DNA replication by a cell cycle regulatory protein that binds at the chromosome origin. Proc. Natl. Acad. Sci. 95: 120-125.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 120-125
    • Quon, K.C.1    Yang, B.2    Domian, I.J.3    Shapiro, L.4    Marczynski, G.T.5
  • 43
    • 0036443740 scopus 로고    scopus 로고
    • The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis
    • Ryan, K.R., Judd, E.M., and Shapiro, L. 2002. The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis. J. Mol. Biol. 324: 443-455.
    • (2002) J. Mol. Biol , vol.324 , pp. 443-455
    • Ryan, K.R.1    Judd, E.M.2    Shapiro, L.3
  • 44
    • 2442531895 scopus 로고    scopus 로고
    • Recruitment of a cytoplasmic response regulator to the cell pole is linked to its cell cycle-regulated proteolysis
    • Ryan, K.R., Huntwork, S., and Shapiro, L. 2004. Recruitment of a cytoplasmic response regulator to the cell pole is linked to its cell cycle-regulated proteolysis. Proc. Natl. Acad. Sci. 101: 7415-7420.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 7415-7420
    • Ryan, K.R.1    Huntwork, S.2    Shapiro, L.3
  • 45
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M.C. 2003. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 46
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P.R., 2000. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7: 730-734.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 47
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • Simm, R., Morr, M., Kader, A., Nimtz, M., and Romling, U. 2004. GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol. 53: 1123-1134.
    • (2004) Mol. Microbiol , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 48
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V., and Berg, H.C. 2002. Receptor sensitivity in bacterial chemotaxis. Proc. Natl. Acad. Sci. 99: 123-127.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 49
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo, R., Pratt, J.T., and Camilli, A. 2007. Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu Rev Microbiol. 61: 131-148.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 50
    • 36749049715 scopus 로고    scopus 로고
    • A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus
    • doi:10.1093/nar/gkm818
    • Thanbichler, M., Iniesta, A.A., and Shapiro, L. 2007. A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus. Nucleic Acids Res. 35: e137. doi:10.1093/nar/gkm818.
    • (2007) Nucleic Acids Res , vol.35
    • Thanbichler, M.1    Iniesta, A.A.2    Shapiro, L.3
  • 51
    • 0034884131 scopus 로고    scopus 로고
    • Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX- dependent pathway
    • Tsai, J.W. and Alley, M.R. 2001. Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX- dependent pathway. J. Bacteriol. 183: 5001-5007.
    • (2001) J. Bacteriol , vol.183 , pp. 5001-5007
    • Tsai, J.W.1    Alley, M.R.2
  • 52
    • 0032538886 scopus 로고    scopus 로고
    • Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
    • Turgay, K., Hahn, J., Burghoorn, J., and Dubnau, D. 1998. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 17: 6730-6738.
    • (1998) EMBO J , vol.17 , pp. 6730-6738
    • Turgay, K.1    Hahn, J.2    Burghoorn, J.3    Dubnau, D.4
  • 53
    • 0037108973 scopus 로고    scopus 로고
    • Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins
    • Viollier, P.H., Sternheim, N., and Shapiro, L. 2002. Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins. Proc. Natl. Acad. Sci. 99: 13831-13836.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 13831-13836
    • Viollier, P.H.1    Sternheim, N.2    Shapiro, L.3
  • 54
    • 0027475809 scopus 로고
    • A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus
    • Wang, S.P., Sharma, P.L., Schoenlein, P.V., and Ely, B. 1993. A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus. Proc. Natl. Acad. Sci. 90: 630-634.
    • (1993) Proc. Natl. Acad. Sci , vol.90 , pp. 630-634
    • Wang, S.P.1    Sharma, P.L.2    Schoenlein, P.V.3    Ely, B.4
  • 55
    • 0032469437 scopus 로고    scopus 로고
    • Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask
    • Wang, J., Hartling, J.A., and Flanagan, J.M. 1998. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124: 151-163.
    • (1998) J. Struct. Biol , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 56
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF-modified response regulator PleD: Implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann, P., Chan, C., Paul, R., Beck, A., Heerklotz, H., Jenal, U., and Schirmer, T. 2007. Structure of BeF-modified response regulator PleD: Implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15: 915-927.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6    Schirmer, T.7
  • 59
    • 0035852714 scopus 로고    scopus 로고
    • The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization
    • Zhu, J. and Winans, S.C. 2001. The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization. Proc. Natl. Acad. Sci. 98: 1507-1512.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 1507-1512
    • Zhu, J.1    Winans, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.