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Iniesta A.A., McGrath P.T., Reisenauer A., McAdams H.H., and Shapiro L. A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression. Proc Natl Acad Sci U S A 103 (2006) 10935-10940
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This paper reports a feedback loop that facilitates re-accumulation of the cell cycle regulator CtrA after its degradation by the ClpXP protease during the G1-to-S-transition. CpdR, a response regulator that is required for the activation of ClpXP is found to be itself subject to ClpXP-mediated proteolysis, thereby stimulating its own inactivation and, thus, effecting stabilization of CtrA.
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Iniesta A.A., and Shapiro L. A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade. Proc Natl Acad Sci U S A 105 (2008) 16602-16607. This paper reports a feedback loop that facilitates re-accumulation of the cell cycle regulator CtrA after its degradation by the ClpXP protease during the G1-to-S-transition. CpdR, a response regulator that is required for the activation of ClpXP is found to be itself subject to ClpXP-mediated proteolysis, thereby stimulating its own inactivation and, thus, effecting stabilization of CtrA.
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This paper reports a positive feedback loop that ensures robust progression of the C. crescentus cell cycle. The authors find that the response regulator DivK promotes its own phosphorylation by stimulating the activity of its cognate histidine kinase DivJ and by switching its phosphatase PleC into the kinase mode, once a certain level of DivK∼P has accumulated in the cell. In addition, the PleC kinase activity is found to be required for the activation of the PleD, a response regulator with guanylate cyclase activity that is essential for the expression of adhesive properties and sessility.
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This study shows that the response regulator PleD dimerizes upon phosphorylation, leading to the stimulation of its guanylate cyclase activity and to its sequestration to the incipient stalked cell pole.
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Purcell E.B., Siegal-Gaskins D., Rawling D.C., Fiebig A., and Crosson S. A photosensory two-component system regulates bacterial cell attachment. Proc Natl Acad Sci U S A 104 (2007) 18241-18246. This paper reports the identification of a two-component system that modulates the adhesive properties of C. crescentus in response to light.
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Duerig A., Abel S., Folcher M., Nicollier M., Schwede T., Amiot N., Giese B., and Jenal U. Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 23 (2009) 93-104. This study identifies a novel c-di-GMP-binding protein, PopA that is required for degradation of the cell cycle regulator CtrA. PopA senses c-di-GMP with the help of a catalytically inactive guanylate cyclase domain. Upon ligand binding, it recruits CtrA to the differentiating pole, thus stimulating elimination of CtrA by the polar ClpXP protease complex.
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This paper identifies the protein SpmX as a factor that required for the polar localization and activity of the histidine kinase DivJ, a key player in the regulatory network that governs the C. crescentus cell cycle. Synthesis and translation of the spmX mRNA occur at different developmental stages, controlled by a complex transcriptional cascade involving the cell cycle master regulator CtrA. SpmX carries a lysozyme-like domain that is necessary and sufficient for localization, suggesting that its localization is guided by structural cues in the cell wall.
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Radhakrishnan S.K., Thanbichler M., and Viollier P.H. The dynamic interplay between a cell fate determinant and a lysozyme homolog drives the asymmetric division cycle of Caulobacter crescentus. Genes Dev 22 (2008) 212-225. This paper identifies the protein SpmX as a factor that required for the polar localization and activity of the histidine kinase DivJ, a key player in the regulatory network that governs the C. crescentus cell cycle. Synthesis and translation of the spmX mRNA occur at different developmental stages, controlled by a complex transcriptional cascade involving the cell cycle master regulator CtrA. SpmX carries a lysozyme-like domain that is necessary and sufficient for localization, suggesting that its localization is guided by structural cues in the cell wall.
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This study demonstrates that, in C. crescentus, rapid inactivation of DnaA (RIDA) by the replisome-associated protein Hda is essential for suppressing supernumerary initiation events once the first round of replication has been started.
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A moving DNA replication factory in Caulobacter crescentus
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Jensen R.B., Wang S.C., and Shapiro L. A moving DNA replication factory in Caulobacter crescentus. EMBO J 20 (2001) 4952-4963
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Growth conditions regulate the requirements for Caulobacter chromosome segregation
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Shebelut C.W., Jensen R.B., and Gitai Z. Growth conditions regulate the requirements for Caulobacter chromosome segregation. J Bacteriol 191 (2009) 1097-1100
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Caulobacter requires a dedicated mechanism to initiate chromosome segregation
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This paper provides convincing evidence for the long-standing hypothesis that segregation of the origin regions is largely mediated by the ParAB DNA-partitioning system in C. crescentus. The binding sites for the centromer-binding protein ParB (parS) are shown to impair the segregation process when introduced in trans. Moreover, using defined chromosome inversions and site-specific fluorescence labeling, the parS sites are identified as attachment points for the machineries mediating segregation and polar anchoring of the origin regions.
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Toro E., Hong S.H., McAdams H.H., and Shapiro L. Caulobacter requires a dedicated mechanism to initiate chromosome segregation. Proc Natl Acad Sci U S A 105 (2008) 15435-15440. This paper provides convincing evidence for the long-standing hypothesis that segregation of the origin regions is largely mediated by the ParAB DNA-partitioning system in C. crescentus. The binding sites for the centromer-binding protein ParB (parS) are shown to impair the segregation process when introduced in trans. Moreover, using defined chromosome inversions and site-specific fluorescence labeling, the parS sites are identified as attachment points for the machineries mediating segregation and polar anchoring of the origin regions.
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Proc Natl Acad Sci U S A
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Toro, E.1
Hong, S.H.2
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46
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The chromosome partitioning protein, ParB, is required for cytokinesis in Caulobacter crescentus
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Mohl D.A., Easter Jr. J., and Gober J.W. The chromosome partitioning protein, ParB, is required for cytokinesis in Caulobacter crescentus. Mol Microbiol 42 (2001) 741-755
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Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus
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Mohl D.A., and Gober J.W. Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus. Cell 88 (1997) 675-684
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Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus
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Figge R.M., Easter J., and Gober J.W. Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus. Mol Microbiol 47 (2003) 1225-1237
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ParB-stimulated nucleotide exchange regulates a switch in functionally distinct ParA activities
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Easter Jr. J., and Gober J.W. ParB-stimulated nucleotide exchange regulates a switch in functionally distinct ParA activities. Mol Cell 10 (2002) 427-434
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A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole
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••]).
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Cell
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Bowman, G.R.1
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51
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A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter
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••], this paper reports the identification of a coiled-coil protein, PopZ, that mediates attachment of the replication origin regions to the cell poles. PopZ assembles into a polymeric network that is sequestered to the tips of the cell and interacts with the origin-proximal ParB-parS nucleoprotein complex, a centromer-like structure involved in chromosome segregation.
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••], this paper reports the identification of a coiled-coil protein, PopZ, that mediates attachment of the replication origin regions to the cell poles. PopZ assembles into a polymeric network that is sequestered to the tips of the cell and interacts with the origin-proximal ParB-parS nucleoprotein complex, a centromer-like structure involved in chromosome segregation.
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Cell
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Ebersbach, G.1
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Diverse paths to midcell: assembly of the bacterial cell division machinery
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Goehring N.W., and Beckwith J. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15 (2005) R514-526
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MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
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Thanbichler M., and Shapiro L. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126 (2006) 147-162
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The bifunctional FtsK protein mediates chromosome partitioning and cell division in Caulobacter
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Wang S.C., West L., and Shapiro L. The bifunctional FtsK protein mediates chromosome partitioning and cell division in Caulobacter. J Bacteriol 188 (2006) 1497-1508
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FtsK, a literate chromosome segregation machine
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Bigot S., Sivanathan V., Possoz C., Barre F.X., and Cornet F. FtsK, a literate chromosome segregation machine. Mol Microbiol 64 (2007) 1434-1441
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56
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Bacterial birth scar proteins mark future flagellum assembly site
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Huitema E., Pritchard S., Matteson D., Radhakrishnan S.K., and Viollier P.H. Bacterial birth scar proteins mark future flagellum assembly site. Cell 124 (2006) 1025-1037
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57
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A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell
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Lam H., Schofield W.B., and Jacobs-Wagner C. A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell. Cell 124 (2006) 1011-1023
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PflI, a protein involved in flagellar positioning in Caulobacter crescentus
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Obuchowski P.L., and Jacobs-Wagner C. PflI, a protein involved in flagellar positioning in Caulobacter crescentus. J Bacteriol 190 (2008) 1718-1729
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Obuchowski, P.L.1
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34248364322
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The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
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This study demonstrates that C. crescentus shows FtsZ-dependent medial growth, occurring independently of the MreB cytoskeleton. This observation is correlated with the recruitment of MurG, an enzyme involved in the synthesis of peptidoglycan precursors, to the cell division site.
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Aaron M., Charbon G., Lam H., Schwarz H., Vollmer W., and Jacobs-Wagner C. The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol Microbiol 64 (2007) 938-952. This study demonstrates that C. crescentus shows FtsZ-dependent medial growth, occurring independently of the MreB cytoskeleton. This observation is correlated with the recruitment of MurG, an enzyme involved in the synthesis of peptidoglycan precursors, to the cell division site.
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Mol Microbiol
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Aaron, M.1
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60
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The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
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•], this paper shows the existence of a medial growth zone in C. crescentus.
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•], this paper shows the existence of a medial growth zone in C. crescentus.
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Mol Microbiol
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Divakaruni, A.V.1
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61
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RodZ, a component of the bacterial core morphogenic apparatus
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This study reports the identification of a highly conserved membrane protein that mediates interaction between the MreB cytoskeleton and the cell wall biosynthetic machinery.
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Alyahya S.A., Alexander R., Costa T., Henriques A.O., Emonet T., and Jacobs-Wagner C. RodZ, a component of the bacterial core morphogenic apparatus. Proc Natl Acad Sci U S A 106 (2009) 1239-1244. This study reports the identification of a highly conserved membrane protein that mediates interaction between the MreB cytoskeleton and the cell wall biosynthetic machinery.
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Proc Natl Acad Sci U S A
, vol.106
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Alyahya, S.A.1
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Jacobs-Wagner, C.6
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