Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the...
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| Veröffentlicht in: | Genes & development 1998-11, Vol.12 (21), p.3419-3430 |
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| creator | Marston, A L Thomaides, H B Edwards, D H Sharpe, M E Errington, J |
| description | Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD. |
| doi_str_mv | 10.1101/gad.12.21.3419 |
| format | Article |
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Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. 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Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphatases - physiology</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - physiology</subject><subject>Bacterial Proteins - physiology</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Cycle Proteins - physiology</subject><subject>Cell Division - physiology</subject><subject>Cell Polarity - physiology</subject><subject>Escherichia coli Proteins</subject><subject>Green Fluorescent Proteins</subject><subject>Luminescent Proteins - genetics</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Biological</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Research Paper</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1vFDEQxS0ECkegpUNyRbfLzHr9VVBAgAQpUVJAbXm93sTItz5sb6Tw12ePnKJQUY0083tPb_QIeYvQIgJ-uLZji13bYct61M_IBnmvG95L-ZxsQGloNBP6JXlVyi8AECDEETnSCpTo1IaUqxRtpjE5G8MfW0OaaZpovfH0Isxf6C6n6sPf3WfrQoxLoWUZaoihUDuPNNRCc4qerlDx0bunFtswNs7HSMdwG8r-UEL1r8mLycbi3xzmMfn57euPk7Pm_PL0-8mn88b1Cmsj-OC0dtBZDdx5OanBy3ECzsfOSccBOI4WuWVSMAShPGrLtfXDup8UsGPy8cF3twxbPzo_12yj2eWwtfnOJBvMv5c53JjrdGsYyo7xVf_-oM_p9-JLNdtQ9u_Y2aelGLkm6FGo_4Ioseeg2Aq2D6DLqZTsp8cwCGZfp1nrNNiZDs2-zlXw7ukLj_ihP3YPEyadqg</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Marston, A L</creator><creator>Thomaides, H B</creator><creator>Edwards, D H</creator><creator>Sharpe, M E</creator><creator>Errington, J</creator><general>Cold Spring Harbor Laboratory Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19981101</creationdate><title>Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site</title><author>Marston, A L ; Thomaides, H B ; Edwards, D H ; Sharpe, M E ; Errington, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c481t-65bc99c02a905ce7f8be7df055d2c7c50051da15a37631068e19a59aeb51df803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphatases - physiology</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - physiology</topic><topic>Bacterial Proteins - physiology</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Cycle Proteins - physiology</topic><topic>Cell Division - physiology</topic><topic>Cell Polarity - physiology</topic><topic>Escherichia coli Proteins</topic><topic>Green Fluorescent Proteins</topic><topic>Luminescent Proteins - genetics</topic><topic>Microscopy, Fluorescence</topic><topic>Models, Biological</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Research Paper</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marston, A L</creatorcontrib><creatorcontrib>Thomaides, H B</creatorcontrib><creatorcontrib>Edwards, D H</creatorcontrib><creatorcontrib>Sharpe, M E</creatorcontrib><creatorcontrib>Errington, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Genes & development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marston, A L</au><au>Thomaides, H B</au><au>Edwards, D H</au><au>Sharpe, M E</au><au>Errington, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site</atitle><jtitle>Genes & development</jtitle><addtitle>Genes Dev</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>12</volume><issue>21</issue><spage>3419</spage><epage>3430</epage><pages>3419-3430</pages><issn>0890-9369</issn><eissn>1549-5477</eissn><abstract>Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.</abstract><cop>United States</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>9808628</pmid><doi>10.1101/gad.12.21.3419</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0890-9369 |
| ispartof | Genes & development, 1998-11, Vol.12 (21), p.3419-3430 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - physiology Bacillus subtilis Bacillus subtilis - physiology Bacterial Proteins - physiology Cell Cycle Proteins - metabolism Cell Cycle Proteins - physiology Cell Division - physiology Cell Polarity - physiology Escherichia coli Proteins Green Fluorescent Proteins Luminescent Proteins - genetics Microscopy, Fluorescence Models, Biological Recombinant Fusion Proteins - genetics Research Paper |
| title | Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site |
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