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Hoch, J.A.1
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Ohlsen, K.L.1
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7
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0028596145
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Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis
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Perego M, Hanstein C, Welsh KM, Djavakhishvili T, Glaser P, Hoch JA. Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis. Cell. 79:1994;1047-1055.
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Perego, M.1
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8
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Trach K, Hoch JA. The Bacillus subtilis spoOB stage O sporulation operon encodes an essential GTP-binding protein. J Bacteriol. 171:1993;1362-1371.
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Trach, K.1
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Ireton, K.1
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10
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0028915966
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Krebs cycle function is required for activation of the SpoOA transcription factor in Bacillus subtilis
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of special interest. The authors use a constitutively active SpoOA mutant to establish a link between the Krebs cycle and the phosphorelay.
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Ireton K, Jin S, Grossman AD, Sonenshein AL. Krebs cycle function is required for activation of the SpoOA transcription factor in Bacillus subtilis. of special interest Proc Natl Acad Sci USA. 92:1995;2845-2849 The authors use a constitutively active SpoOA mutant to establish a link between the Krebs cycle and the phosphorelay.
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Ireton, K.1
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11
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0029883587
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Cell - Cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis
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of outstanding interest. This report shows that the RapA protein aspartyl phosphatase is inhibited by a processed peptide derived from the small protein PhrA that is encoded in the same transcript as RapA. The small peptide functions as a cell - cell signal and may act as a quorum sensor. It is exported and then imported by the oligopeptide transport system.
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Perego M, Hoch JA. Cell - cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis. of outstanding interest Proc Natl Acad Sci USA. 93:1996;1549-1553 This report shows that the RapA protein aspartyl phosphatase is inhibited by a processed peptide derived from the small protein PhrA that is encoded in the same transcript as RapA. The small peptide functions as a cell - cell signal and may act as a quorum sensor. It is exported and then imported by the oligopeptide transport system.
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Proc Natl Acad Sci USA
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Perego, M.1
Hoch, J.A.2
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12
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0029897997
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Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis
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of special interest. A review of several newly-discovered examples of Rap protein-aspartyl phosphatases that may regulate two-component signal-transduction systems, and which themselves may be subject to regulation by peptide export/import.
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Perego M, Glaser P, Hoch JA. Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis. of special interest Mol Microbiol. 19:1996;1151-1157 A review of several newly-discovered examples of Rap protein-aspartyl phosphatases that may regulate two-component signal-transduction systems, and which themselves may be subject to regulation by peptide export/import.
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Mol Microbiol
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Perego, M.1
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Hoch, J.A.3
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13
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Transcriptional regulation of Bacillus subtilis glucose starvation inducible genes: Control of gsiA by the ComP - ComA signal transduction system
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Mueller JP, Bukusoglu G, Sonenshein AL. Transcriptional regulation of Bacillus subtilis glucose starvation inducible genes: control of gsiA by the ComP - ComA signal transduction system. J Bacteriol. 174:1992;4361-4373.
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Mueller, J.P.1
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Magnuson, R.1
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16
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Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
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Erickson, H.P.1
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Beall, B.1
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18
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0029918758
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Transcription factor SpoOA switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
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of special interest. Here, immunofluorescence is used to show that, during early sporulation, FtsZ localizes to the polar site of the incipient sporulation septum. Activated SpoOA is required for this polar localization of FtsZ.
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Levin PA, Losick R. Transcription factor SpoOA switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. of special interest Genes Dev. 10:1996;478-488 Here, immunofluorescence is used to show that, during early sporulation, FtsZ localizes to the polar site of the incipient sporulation septum. Activated SpoOA is required for this polar localization of FtsZ.
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Levin, P.A.1
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19
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0029050811
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A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis
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of outstanding interest. A report that spoIIIE mutations partially block partitioning of the chromosome into the prespore, resulting in the apparent bisection of the chromosome by the septum. This report also notes sequence similarity of SpoIIIE and some proteins required for plasmid conjugation.
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Wu LJ, Lewis PJ, Allmansberger R, Hauser PM, Errington J. A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis. of outstanding interest Genes Dev. 9:1995;1316-1326 A report that spoIIIE mutations partially block partitioning of the chromosome into the prespore, resulting in the apparent bisection of the chromosome by the septum. This report also notes sequence similarity of SpoIIIE and some proteins required for plasmid conjugation.
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Wu, L.J.1
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Post-septational chromosome partitioning in bacteria
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of outstanding interest. The authors show that spoIIIE mutants are unable to recover if their chromosome has been trapped by a closing septum; the mutants are sensitive to antibiotics, such as nalidixic acid, that interfere with DNA metabolism.
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Sharpe ME, Errington J. Post-septational chromosome partitioning in bacteria. of outstanding interest Proc Natl Acad Sci USA. 92:1995;8630-8634 The authors show that spoIIIE mutants are unable to recover if their chromosome has been trapped by a closing septum; the mutants are sensitive to antibiotics, such as nalidixic acid, that interfere with DNA metabolism.
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Sharpe, M.E.1
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P.J. Piggot, C.P. Jr. Moran, Youngman P. Washington, DC: American Society for Microbiology
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Piggot, P.J.1
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22
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De Lencastre, H.1
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Duncan, L.1
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25
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0029017527
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Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis
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E exclusively in the mother cell.
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E exclusively in the mother cell.
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Harry, E.J.1
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26
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0029969436
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Use of green fluorescent protein for detection of cell-specific gene expression and subcellular protein localization during sporulation in Bacillus subtilis
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E activity (spoIVA) are confined to the prespore and mother cell respectively.
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Lewis, P.J.1
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27
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0029610802
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Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy
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of special interest. The authors visualize the location of some sporulation structural proteins. They show that the SpoIVA protein, which acts as a scaffold for spore coat assembly, is first detected at the spore septum and subsequently forms a shell around the engulfed prespore.
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Pogliani K, Harry E, Losick R. Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy. of special interest Mol Microbiol. 18:1995;459-470 The authors visualize the location of some sporulation structural proteins. They show that the SpoIVA protein, which acts as a scaffold for spore coat assembly, is first detected at the spore septum and subsequently forms a shell around the engulfed prespore.
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Pogliani, K.1
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28
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0028785819
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Use of green fluorescent protein for visualization of cell-specific gene expression and subcellular protein localization during sporulation in Bacillus subtilis
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E-directed genes that have been shown to display compartment-specific gene expression.
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E-directed genes that have been shown to display compartment-specific gene expression.
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Webb, C.D.1
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29
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0029880416
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Analysis of the role of prespore gene expression in the compartmentalization of mother-cell-specific gene expression during sporulation of Bacillus subtilis
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F is not required for the process of compartmentalization.
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F is not required for the process of compartmentalization.
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Zhang, L.1
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0028931410
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E during sporulation in Bacillus subtilis
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E. The spoIIR gene thus provides the link between the program of gene expression in the prespore and that in the mother cell.
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E. The spoIIR gene thus provides the link between the program of gene expression in the prespore and that in the mother cell.
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Karow, M.L.1
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Cell - Cell signaling pathway activating a developmental transcription factor in Bacillus subtilis
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E is reported here (see also [32]).
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E is reported here (see also [32]).
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Extracellular signal protein triggering the proteolytic activation of a developmental transcription factor in B. subtilis
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E. It thus provides biochemical evidence of how gene expression in the mother cell is linked to gene expression in the prespore.
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E. It thus provides biochemical evidence of how gene expression in the mother cell is linked to gene expression in the prespore.
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Hofmeister, A.E.M.1
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Lewis PJ, Partridge SR, Errington J. σ factors, asymmetry, and the determination of cell fate in Bacillus subtilis. Proc Natl Acad Sci USA. 91:1994;3849-3853.
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An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis
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Alper S, Duncan L, Losick R. An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis. Cell. 77:1994;195-205.
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Alper, S.1
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F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-σ factor that is also a protein kinase
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F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-σ factor that is also a protein kinase. Cell. 74:1993;735-742.
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45
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Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division
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F-mediated transcription in the presence of the anti-σ factor SpoIIAB.
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F-mediated transcription in the presence of the anti-σ factor SpoIIAB.
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Duncan, L.1
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47
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0030012129
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Bifunctional protein required for asymmetric cell division and cell-specific transcription in Bacillus subtilis
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F to become active. In spoIIE mutants, SpoIIAA is entirely in the inactive phosphorylated form.
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F to become active. In spoIIE mutants, SpoIIAA is entirely in the inactive phosphorylated form.
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Feucht, A.1
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48
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0029976033
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Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly
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of outstanding interest. A report of the sequence and predicted membrane topology of the SpoIIE protein. The authors use GFP labeling to show that SpoIIE is associated with the incipient sporulation septum.
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Barák I, Behari J, Olmedo G, Guzmán P, Brown DP, Castro E, Walker D, Westpheling J, Youngman P. Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly. of outstanding interest Mol Microbiol. 19:1996;1047-1060 A report of the sequence and predicted membrane topology of the SpoIIE protein. The authors use GFP labeling to show that SpoIIE is associated with the incipient sporulation septum.
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Barák, I.1
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49
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0028857125
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Localization of protein implicated in establishment of cell type to sites of asymmetric division
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F activation, is associated with the nascent sporulation septum. (A back-to-back paper with [45]).
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F activation, is associated with the nascent sporulation septum. (A back-to-back paper with [45]).
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Arigoni, F.1
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50
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Levin PA, Losick R. Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation. J Bacteriol. 176:1994;1451-1459.
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