Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro
Summary The E. coli Min system forms a cell‐pole‐to‐cell‐pole oscillator that positions the divisome at mid‐cell. The MinD ATPase binds the membrane and recruits the cell division inhibitor MinC. MinE interacts with and releases MinD (and MinC) from the membrane. The chase of MinD by MinE creates th...
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| Veröffentlicht in: | Molecular microbiology 2014-08, Vol.93 (3), p.453-463 |
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| creator | Vecchiarelli, Anthony G. Li, Min Mizuuchi, Michiyo Mizuuchi, Kiyoshi |
| description | Summary
The E. coli Min system forms a cell‐pole‐to‐cell‐pole oscillator that positions the divisome at mid‐cell. The MinD ATPase binds the membrane and recruits the cell division inhibitor MinC. MinE interacts with and releases MinD (and MinC) from the membrane. The chase of MinD by MinE creates the in vivo oscillator that maintains a low level of the division inhibitor at mid‐cell. In vitro reconstitution and visualization of Min proteins on a supported lipid bilayer has provided significant advances in understanding Min patterns in vivo. Here we studied the effects of flow, lipid composition, and salt concentration on Min patterning. Flow and no‐flow conditions both supported Min protein patterns with somewhat different characteristics. Without flow, MinD and MinE formed spiraling waves. MinD and, to a greater extent MinE, have stronger affinities for anionic phospholipid. MinD‐independent binding of MinE to anionic lipid resulted in slower and narrower waves. MinE binding to the bilayer was also more susceptible to changes in ionic strength than MinD. We find that modulating protein diffusion with flow, or membrane binding affinities with changes in lipid composition or salt concentration, can differentially affect the retention time of MinD and MinE, leading to spatiotemporal changes in Min patterning. |
| doi_str_mv | 10.1111/mmi.12669 |
| format | Article |
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The E. coli Min system forms a cell‐pole‐to‐cell‐pole oscillator that positions the divisome at mid‐cell. The MinD ATPase binds the membrane and recruits the cell division inhibitor MinC. MinE interacts with and releases MinD (and MinC) from the membrane. The chase of MinD by MinE creates the in vivo oscillator that maintains a low level of the division inhibitor at mid‐cell. In vitro reconstitution and visualization of Min proteins on a supported lipid bilayer has provided significant advances in understanding Min patterns in vivo. Here we studied the effects of flow, lipid composition, and salt concentration on Min patterning. Flow and no‐flow conditions both supported Min protein patterns with somewhat different characteristics. Without flow, MinD and MinE formed spiraling waves. MinD and, to a greater extent MinE, have stronger affinities for anionic phospholipid. MinD‐independent binding of MinE to anionic lipid resulted in slower and narrower waves. MinE binding to the bilayer was also more susceptible to changes in ionic strength than MinD. We find that modulating protein diffusion with flow, or membrane binding affinities with changes in lipid composition or salt concentration, can differentially affect the retention time of MinD and MinE, leading to spatiotemporal changes in Min patterning.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/mmi.12669</identifier><identifier>PMID: 24930948</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - metabolism ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; Cell Division ; E coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Lipid Bilayers - chemistry ; Microbiology ; Molecular biology ; Phospholipids - chemistry ; Phospholipids - metabolism</subject><ispartof>Molecular microbiology, 2014-08, Vol.93 (3), p.453-463</ispartof><rights>Published 2014. This article is a U.S. Government work and is in the public domain in the USA.</rights><rights>Copyright Blackwell Publishing Ltd. Aug 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5099-4de8a49d5f709fcfa58296b8adfe6961fc695710f06b9e0d0b947a5c2dd5b60b3</citedby><cites>FETCH-LOGICAL-c5099-4de8a49d5f709fcfa58296b8adfe6961fc695710f06b9e0d0b947a5c2dd5b60b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fmmi.12669$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fmmi.12669$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24930948$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vecchiarelli, Anthony G.</creatorcontrib><creatorcontrib>Li, Min</creatorcontrib><creatorcontrib>Mizuuchi, Michiyo</creatorcontrib><creatorcontrib>Mizuuchi, Kiyoshi</creatorcontrib><title>Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
The E. coli Min system forms a cell‐pole‐to‐cell‐pole oscillator that positions the divisome at mid‐cell. The MinD ATPase binds the membrane and recruits the cell division inhibitor MinC. MinE interacts with and releases MinD (and MinC) from the membrane. The chase of MinD by MinE creates the in vivo oscillator that maintains a low level of the division inhibitor at mid‐cell. In vitro reconstitution and visualization of Min proteins on a supported lipid bilayer has provided significant advances in understanding Min patterns in vivo. Here we studied the effects of flow, lipid composition, and salt concentration on Min patterning. Flow and no‐flow conditions both supported Min protein patterns with somewhat different characteristics. Without flow, MinD and MinE formed spiraling waves. MinD and, to a greater extent MinE, have stronger affinities for anionic phospholipid. MinD‐independent binding of MinE to anionic lipid resulted in slower and narrower waves. MinE binding to the bilayer was also more susceptible to changes in ionic strength than MinD. We find that modulating protein diffusion with flow, or membrane binding affinities with changes in lipid composition or salt concentration, can differentially affect the retention time of MinD and MinE, leading to spatiotemporal changes in Min patterning.</description><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Division</subject><subject>E coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Lipid Bilayers - chemistry</subject><subject>Microbiology</subject><subject>Molecular biology</subject><subject>Phospholipids - chemistry</subject><subject>Phospholipids - metabolism</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1LHTEQhoO06NH2wj8ggd60F6vJbpKzuRHEj1bw4I2F3oVsPnTsbrImu5bz75vTY6UtNDBkYB4eZngROqTkmJZ3MgxwTGsh5A5a0Ebwqpa8fYMWRHJSNW39bQ_t5_xICG2IaHbRXs1kQyRrF-j7BXjvkgsT6B5r7yHABC7j6PEKwgXWwW6aSzzF0kMMYPD4EHOpHkawGILvZxeM22B41NPkUoBwj-066AFMLgR-hinFd-it131271_-A_T16vLu_Et1c_v5-vzspjKcSFkx61rNpOV-SaQ3XvO2lqJrtfVOSEG9EZIvKfFEdNIRSzrJlpqb2lreCdI1B-h06x3nbnDWlOOS7tWYYNBpraIG9fckwIO6j8-KUSoYY0Xw8UWQ4tPs8qQGyMb1vQ4uzllRzqRoasZIQT_8gz7GOYVyXqE4laJetm2hPm0pk2LOyfnXZShRmwhViVD9irCwR39u_0r-zqwAJ1vgB_Ru_X-TWq2ut8qfFsqn3A</recordid><startdate>201408</startdate><enddate>201408</enddate><creator>Vecchiarelli, Anthony G.</creator><creator>Li, Min</creator><creator>Mizuuchi, Michiyo</creator><creator>Mizuuchi, Kiyoshi</creator><general>Blackwell Publishing Ltd</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201408</creationdate><title>Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro</title><author>Vecchiarelli, Anthony G. ; Li, Min ; Mizuuchi, Michiyo ; Mizuuchi, Kiyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5099-4de8a49d5f709fcfa58296b8adfe6961fc695710f06b9e0d0b947a5c2dd5b60b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Cell Cycle Proteins - chemistry</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Division</topic><topic>E coli</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Lipid Bilayers - chemistry</topic><topic>Microbiology</topic><topic>Molecular biology</topic><topic>Phospholipids - chemistry</topic><topic>Phospholipids - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vecchiarelli, Anthony G.</creatorcontrib><creatorcontrib>Li, Min</creatorcontrib><creatorcontrib>Mizuuchi, Michiyo</creatorcontrib><creatorcontrib>Mizuuchi, Kiyoshi</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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</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>PubMed Central (Full Participant titles)</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vecchiarelli, Anthony G.</au><au>Li, Min</au><au>Mizuuchi, Michiyo</au><au>Mizuuchi, Kiyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2014-08</date><risdate>2014</risdate><volume>93</volume><issue>3</issue><spage>453</spage><epage>463</epage><pages>453-463</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
The E. coli Min system forms a cell‐pole‐to‐cell‐pole oscillator that positions the divisome at mid‐cell. The MinD ATPase binds the membrane and recruits the cell division inhibitor MinC. MinE interacts with and releases MinD (and MinC) from the membrane. The chase of MinD by MinE creates the in vivo oscillator that maintains a low level of the division inhibitor at mid‐cell. In vitro reconstitution and visualization of Min proteins on a supported lipid bilayer has provided significant advances in understanding Min patterns in vivo. Here we studied the effects of flow, lipid composition, and salt concentration on Min patterning. Flow and no‐flow conditions both supported Min protein patterns with somewhat different characteristics. Without flow, MinD and MinE formed spiraling waves. MinD and, to a greater extent MinE, have stronger affinities for anionic phospholipid. MinD‐independent binding of MinE to anionic lipid resulted in slower and narrower waves. MinE binding to the bilayer was also more susceptible to changes in ionic strength than MinD. We find that modulating protein diffusion with flow, or membrane binding affinities with changes in lipid composition or salt concentration, can differentially affect the retention time of MinD and MinE, leading to spatiotemporal changes in Min patterning.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>24930948</pmid><doi>10.1111/mmi.12669</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Cell Cycle Proteins - chemistry Cell Cycle Proteins - metabolism Cell Division E coli Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Lipid Bilayers - chemistry Microbiology Molecular biology Phospholipids - chemistry Phospholipids - metabolism |
| title | Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro |
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