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Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis
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| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of Bacteriology, 182, 2000, 16, S. 4478-4490 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Antelmann, Haike Scharf, Christian Hecker, Michael Antelmann, Haike Scharf, Christian Hecker, Michael |
|---|---|
| author |
Antelmann, Haike Scharf, Christian Hecker, Michael |
| spellingShingle |
Antelmann, Haike Scharf, Christian Hecker, Michael Journal of Bacteriology Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis Molecular Biology Microbiology |
| author_sort |
antelmann, haike |
| spelling |
Antelmann, Haike Scharf, Christian Hecker, Michael 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.182.16.4478-4490.2000 <jats:title>ABSTRACT</jats:title> <jats:p> The phosphate starvation response in <jats:italic>Bacillus subtilis</jats:italic> was analyzed using two-dimensional (2D) polyacrylamide gel electrophoresis of cell extracts and supernatants from phosphate-starved cells. Most of the phosphate starvation-induced proteins are under the control of ς <jats:sup>B</jats:sup> , the activity of which is increased by energy depletion. In order to define the proteins belonging to the Pho regulon, which is regulated by the two-component regulatory proteins PhoP and PhoR, the 2D protein pattern of the wild type was compared with those of a <jats:italic>sigB</jats:italic> mutant and a <jats:italic>phoR</jats:italic> mutant. By matrix-assisted laser desorption ionization–time of flight mass spectrometry, two alkaline phosphatases (APases) (PhoA and PhoB), an APase-alkaline phosphodiesterase (PhoD), a glycerophosphoryl diester phosphodiesterase (GlpQ), and the lipoprotein YdhF were identified as very strongly induced PhoPR-dependent proteins secreted into the extracellular medium. In the cytoplasmic fraction, PstB1, PstB2, and TuaD were identified as already known PhoPR-dependent proteins, in addition to PhoB, PhoD, and the previously described PstS. Transcriptional studies of <jats:italic>glpQ</jats:italic> and <jats:italic>ydhF</jats:italic> confirmed the strong PhoPR dependence. Northern hybridization and primer extension experiments showed that <jats:italic>glpQ</jats:italic> is transcribed monocistronically from a ς <jats:sup>A</jats:sup> promoter which is overlapped by four putative TT(A/T)ACA-like PhoP binding sites. Furthermore, <jats:italic>ydhF</jats:italic> might be cotranscribed with <jats:italic>phoB</jats:italic> initiating from the <jats:italic>phoB</jats:italic> promoter. Only a small group of proteins remained phosphate starvation inducible in both <jats:italic>phoR</jats:italic> and <jats:italic>sigB</jats:italic> mutant and did not form a unique regulation group. Among these, YfhM and YjbC were controlled by ς <jats:sup>B</jats:sup> -dependent and unknown PhoPR-independent mechanisms. Furthermore, YtxH and YvyD seemed to be induced after phosphate starvation in the wild type in a ς <jats:sup>B</jats:sup> -dependent manner and in the <jats:italic>sigB</jats:italic> mutant probably via ς <jats:sup>H</jats:sup> . YxiE was induced by phosphate starvation independently of ς <jats:sup>B</jats:sup> and PhoPR. </jats:p> Phosphate Starvation-Inducible Proteins of <i>Bacillus subtilis</i> : Proteomics and Transcriptional Analysis Journal of Bacteriology |
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10.1128/jb.182.16.4478-4490.2000 |
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Biologie |
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American Society for Microbiology, 2000 |
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American Society for Microbiology, 2000 |
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0021-9193 1098-5530 |
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0021-9193 1098-5530 |
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2000 |
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American Society for Microbiology |
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ai |
| series |
Journal of Bacteriology |
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49 |
| title |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_unstemmed |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_full |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_fullStr |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_full_unstemmed |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_short |
Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_sort |
phosphate starvation-inducible proteins of
<i>bacillus subtilis</i>
: proteomics and transcriptional analysis |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.182.16.4478-4490.2000 |
| publishDate |
2000 |
| physical |
4478-4490 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
The phosphate starvation response in
<jats:italic>Bacillus subtilis</jats:italic>
was analyzed using two-dimensional (2D) polyacrylamide gel electrophoresis of cell extracts and supernatants from phosphate-starved cells. Most of the phosphate starvation-induced proteins are under the control of ς
<jats:sup>B</jats:sup>
, the activity of which is increased by energy depletion. In order to define the proteins belonging to the Pho regulon, which is regulated by the two-component regulatory proteins PhoP and PhoR, the 2D protein pattern of the wild type was compared with those of a
<jats:italic>sigB</jats:italic>
mutant and a
<jats:italic>phoR</jats:italic>
mutant. By matrix-assisted laser desorption ionization–time of flight mass spectrometry, two alkaline phosphatases (APases) (PhoA and PhoB), an APase-alkaline phosphodiesterase (PhoD), a glycerophosphoryl diester phosphodiesterase (GlpQ), and the lipoprotein YdhF were identified as very strongly induced PhoPR-dependent proteins secreted into the extracellular medium. In the cytoplasmic fraction, PstB1, PstB2, and TuaD were identified as already known PhoPR-dependent proteins, in addition to PhoB, PhoD, and the previously described PstS. Transcriptional studies of
<jats:italic>glpQ</jats:italic>
and
<jats:italic>ydhF</jats:italic>
confirmed the strong PhoPR dependence. Northern hybridization and primer extension experiments showed that
<jats:italic>glpQ</jats:italic>
is transcribed monocistronically from a ς
<jats:sup>A</jats:sup>
promoter which is overlapped by four putative TT(A/T)ACA-like PhoP binding sites. Furthermore,
<jats:italic>ydhF</jats:italic>
might be cotranscribed with
<jats:italic>phoB</jats:italic>
initiating from the
<jats:italic>phoB</jats:italic>
promoter. Only a small group of proteins remained phosphate starvation inducible in both
<jats:italic>phoR</jats:italic>
and
<jats:italic>sigB</jats:italic>
mutant and did not form a unique regulation group. Among these, YfhM and YjbC were controlled by ς
<jats:sup>B</jats:sup>
-dependent and unknown PhoPR-independent mechanisms. Furthermore, YtxH and YvyD seemed to be induced after phosphate starvation in the wild type in a ς
<jats:sup>B</jats:sup>
-dependent manner and in the
<jats:italic>sigB</jats:italic>
mutant probably via ς
<jats:sup>H</jats:sup>
. YxiE was induced by phosphate starvation independently of ς
<jats:sup>B</jats:sup>
and PhoPR.
</jats:p> |
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| author | Antelmann, Haike, Scharf, Christian, Hecker, Michael |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> The phosphate starvation response in <jats:italic>Bacillus subtilis</jats:italic> was analyzed using two-dimensional (2D) polyacrylamide gel electrophoresis of cell extracts and supernatants from phosphate-starved cells. Most of the phosphate starvation-induced proteins are under the control of ς <jats:sup>B</jats:sup> , the activity of which is increased by energy depletion. In order to define the proteins belonging to the Pho regulon, which is regulated by the two-component regulatory proteins PhoP and PhoR, the 2D protein pattern of the wild type was compared with those of a <jats:italic>sigB</jats:italic> mutant and a <jats:italic>phoR</jats:italic> mutant. By matrix-assisted laser desorption ionization–time of flight mass spectrometry, two alkaline phosphatases (APases) (PhoA and PhoB), an APase-alkaline phosphodiesterase (PhoD), a glycerophosphoryl diester phosphodiesterase (GlpQ), and the lipoprotein YdhF were identified as very strongly induced PhoPR-dependent proteins secreted into the extracellular medium. In the cytoplasmic fraction, PstB1, PstB2, and TuaD were identified as already known PhoPR-dependent proteins, in addition to PhoB, PhoD, and the previously described PstS. Transcriptional studies of <jats:italic>glpQ</jats:italic> and <jats:italic>ydhF</jats:italic> confirmed the strong PhoPR dependence. Northern hybridization and primer extension experiments showed that <jats:italic>glpQ</jats:italic> is transcribed monocistronically from a ς <jats:sup>A</jats:sup> promoter which is overlapped by four putative TT(A/T)ACA-like PhoP binding sites. Furthermore, <jats:italic>ydhF</jats:italic> might be cotranscribed with <jats:italic>phoB</jats:italic> initiating from the <jats:italic>phoB</jats:italic> promoter. Only a small group of proteins remained phosphate starvation inducible in both <jats:italic>phoR</jats:italic> and <jats:italic>sigB</jats:italic> mutant and did not form a unique regulation group. Among these, YfhM and YjbC were controlled by ς <jats:sup>B</jats:sup> -dependent and unknown PhoPR-independent mechanisms. Furthermore, YtxH and YvyD seemed to be induced after phosphate starvation in the wild type in a ς <jats:sup>B</jats:sup> -dependent manner and in the <jats:italic>sigB</jats:italic> mutant probably via ς <jats:sup>H</jats:sup> . YxiE was induced by phosphate starvation independently of ς <jats:sup>B</jats:sup> and PhoPR. </jats:p> |
| doi_str_mv | 10.1128/jb.182.16.4478-4490.2000 |
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| imprint | American Society for Microbiology, 2000 |
| imprint_str_mv | American Society for Microbiology, 2000 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
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| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 4478-4490 |
| publishDate | 2000 |
| publishDateSort | 2000 |
| publisher | American Society for Microbiology |
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| series | Journal of Bacteriology |
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| spelling | Antelmann, Haike Scharf, Christian Hecker, Michael 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.182.16.4478-4490.2000 <jats:title>ABSTRACT</jats:title> <jats:p> The phosphate starvation response in <jats:italic>Bacillus subtilis</jats:italic> was analyzed using two-dimensional (2D) polyacrylamide gel electrophoresis of cell extracts and supernatants from phosphate-starved cells. Most of the phosphate starvation-induced proteins are under the control of ς <jats:sup>B</jats:sup> , the activity of which is increased by energy depletion. In order to define the proteins belonging to the Pho regulon, which is regulated by the two-component regulatory proteins PhoP and PhoR, the 2D protein pattern of the wild type was compared with those of a <jats:italic>sigB</jats:italic> mutant and a <jats:italic>phoR</jats:italic> mutant. By matrix-assisted laser desorption ionization–time of flight mass spectrometry, two alkaline phosphatases (APases) (PhoA and PhoB), an APase-alkaline phosphodiesterase (PhoD), a glycerophosphoryl diester phosphodiesterase (GlpQ), and the lipoprotein YdhF were identified as very strongly induced PhoPR-dependent proteins secreted into the extracellular medium. In the cytoplasmic fraction, PstB1, PstB2, and TuaD were identified as already known PhoPR-dependent proteins, in addition to PhoB, PhoD, and the previously described PstS. Transcriptional studies of <jats:italic>glpQ</jats:italic> and <jats:italic>ydhF</jats:italic> confirmed the strong PhoPR dependence. Northern hybridization and primer extension experiments showed that <jats:italic>glpQ</jats:italic> is transcribed monocistronically from a ς <jats:sup>A</jats:sup> promoter which is overlapped by four putative TT(A/T)ACA-like PhoP binding sites. Furthermore, <jats:italic>ydhF</jats:italic> might be cotranscribed with <jats:italic>phoB</jats:italic> initiating from the <jats:italic>phoB</jats:italic> promoter. Only a small group of proteins remained phosphate starvation inducible in both <jats:italic>phoR</jats:italic> and <jats:italic>sigB</jats:italic> mutant and did not form a unique regulation group. Among these, YfhM and YjbC were controlled by ς <jats:sup>B</jats:sup> -dependent and unknown PhoPR-independent mechanisms. Furthermore, YtxH and YvyD seemed to be induced after phosphate starvation in the wild type in a ς <jats:sup>B</jats:sup> -dependent manner and in the <jats:italic>sigB</jats:italic> mutant probably via ς <jats:sup>H</jats:sup> . YxiE was induced by phosphate starvation independently of ς <jats:sup>B</jats:sup> and PhoPR. </jats:p> Phosphate Starvation-Inducible Proteins of <i>Bacillus subtilis</i> : Proteomics and Transcriptional Analysis Journal of Bacteriology |
| spellingShingle | Antelmann, Haike, Scharf, Christian, Hecker, Michael, Journal of Bacteriology, Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis, Molecular Biology, Microbiology |
| title | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_full | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_fullStr | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_full_unstemmed | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_short | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| title_sort | phosphate starvation-inducible proteins of <i>bacillus subtilis</i> : proteomics and transcriptional analysis |
| title_unstemmed | Phosphate Starvation-Inducible Proteins of Bacillus subtilis : Proteomics and Transcriptional Analysis |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.182.16.4478-4490.2000 |