Novel regulator PgrR for switch control of peptidoglycan recycling in Escherichia coli
Peptidoglycan (PG), also designated as murein, forms a skeletal mesh within the periplasm of bacterial membrane. PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill‐defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties ar...
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| Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2013-02, Vol.18 (2), p.123-134 |
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| container_title | Genes to cells : devoted to molecular & cellular mechanisms |
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| creator | Shimada, Tomohiro Yamazaki, Kaoru Ishihama, Akira |
| description | Peptidoglycan (PG), also designated as murein, forms a skeletal mesh within the periplasm of bacterial membrane. PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill‐defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties are either recycled or used as self‐generated nutrients for cell growth. At present, the control of PG degradation remains uncharacterized. Using the Genomic SELEX screening system, we identified an uncharacterized transcription factor YcjZ is a repressor of the expression of the initial step enzymes for PG peptide degradation. Under nutrient starvation, the genes encoding the enzymes for PG peptide degradation are derepressed so as to generate amino acids but are tightly repressed at high osmotic conditions so as to maintain the rigid membrane for withstanding the turgor. Taken together, we propose to rename YcjZ as PgrR (regulator of peptide glycan recycling). |
| doi_str_mv | 10.1111/gtc.12026 |
| format | Article |
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PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill‐defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties are either recycled or used as self‐generated nutrients for cell growth. At present, the control of PG degradation remains uncharacterized. Using the Genomic SELEX screening system, we identified an uncharacterized transcription factor YcjZ is a repressor of the expression of the initial step enzymes for PG peptide degradation. Under nutrient starvation, the genes encoding the enzymes for PG peptide degradation are derepressed so as to generate amino acids but are tightly repressed at high osmotic conditions so as to maintain the rigid membrane for withstanding the turgor. 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PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill‐defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties are either recycled or used as self‐generated nutrients for cell growth. At present, the control of PG degradation remains uncharacterized. Using the Genomic SELEX screening system, we identified an uncharacterized transcription factor YcjZ is a repressor of the expression of the initial step enzymes for PG peptide degradation. Under nutrient starvation, the genes encoding the enzymes for PG peptide degradation are derepressed so as to generate amino acids but are tightly repressed at high osmotic conditions so as to maintain the rigid membrane for withstanding the turgor. 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Yamazaki, Kaoru ; Ishihama, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j4136-86a16fa9dfe339f7bdd2d1969688e0eaeb1620e608fe64ff67b3dcafaa6017cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes, Reporter</topic><topic>Nucleotide Motifs</topic><topic>Operator Regions, Genetic</topic><topic>Peptidoglycan - metabolism</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shimada, Tomohiro</creatorcontrib><creatorcontrib>Yamazaki, Kaoru</creatorcontrib><creatorcontrib>Ishihama, Akira</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shimada, Tomohiro</au><au>Yamazaki, Kaoru</au><au>Ishihama, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel regulator PgrR for switch control of peptidoglycan recycling in Escherichia coli</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2013-02</date><risdate>2013</risdate><volume>18</volume><issue>2</issue><spage>123</spage><epage>134</epage><pages>123-134</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><coden>GECEFL</coden><abstract>Peptidoglycan (PG), also designated as murein, forms a skeletal mesh within the periplasm of bacterial membrane. PG is a metabolically stable cell architecture in Escherichia coli, but under as yet ill‐defined conditions, a portion of PG is degraded, of which both amino sugar and peptide moieties are either recycled or used as self‐generated nutrients for cell growth. At present, the control of PG degradation remains uncharacterized. Using the Genomic SELEX screening system, we identified an uncharacterized transcription factor YcjZ is a repressor of the expression of the initial step enzymes for PG peptide degradation. Under nutrient starvation, the genes encoding the enzymes for PG peptide degradation are derepressed so as to generate amino acids but are tightly repressed at high osmotic conditions so as to maintain the rigid membrane for withstanding the turgor. 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| ispartof | Genes to cells : devoted to molecular & cellular mechanisms, 2013-02, Vol.18 (2), p.123-134 |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Open Access Titles of Japan; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Base Sequence Binding Sites DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism E coli Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial Genes, Reporter Nucleotide Motifs Operator Regions, Genetic Peptidoglycan - metabolism Protein Binding Proteins Proteolysis Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic |
| title | Novel regulator PgrR for switch control of peptidoglycan recycling in Escherichia coli |
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