Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes
We have incorporated, for the first time, FtsZ and FtsA (the soluble proto-ring proteins from Escherichia coli) into bacterial giant unilamellar inner membrane vesicles (GUIMVs). Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were det...
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| Veröffentlicht in: | The Journal of biological chemistry 2011-04, Vol.286 (13), p.11236-11241 |
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| creator | Jiménez, Mercedes Martos, Ariadna Vicente, Miguel Rivas, Germán |
| description | We have incorporated, for the first time, FtsZ and FtsA (the soluble proto-ring proteins from Escherichia coli) into bacterial giant unilamellar inner membrane vesicles (GUIMVs). Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were determined by confocal microscopy. We found that, in the presence of GDP, FtsZ was homogeneously distributed in the lumen of the vesicle. In the presence of GTP analogs, FtsZ assembled inside the GUIMVs, forming a web of dense spots and fibers. Whereas isolated FtsA was found adsorbed to the inner face of GUIMVs, the addition of FtsZ together with GTP analogs resulted in its dislodgement and its association with the FtsZ fibers in the lumen, suggesting that the FtsA-membrane interaction can be modulated by FtsZ polymers. The use of this novel in vitro system to probe interactions between divisome components will help to determine the biological implications of these findings. |
| doi_str_mv | 10.1074/jbc.M110.194365 |
| format | Article |
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Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were determined by confocal microscopy. We found that, in the presence of GDP, FtsZ was homogeneously distributed in the lumen of the vesicle. In the presence of GTP analogs, FtsZ assembled inside the GUIMVs, forming a web of dense spots and fibers. Whereas isolated FtsA was found adsorbed to the inner face of GUIMVs, the addition of FtsZ together with GTP analogs resulted in its dislodgement and its association with the FtsZ fibers in the lumen, suggesting that the FtsA-membrane interaction can be modulated by FtsZ polymers. The use of this novel in vitro system to probe interactions between divisome components will help to determine the biological implications of these findings.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M110.194365</identifier><identifier>PMID: 21257762</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacterial Cell Division ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Cell Membrane - chemistry ; Cell Membrane - genetics ; Cell Membrane - metabolism ; Cytoskeletal Proteins - chemistry ; Cytoskeletal Proteins - genetics ; Cytoskeletal Proteins - metabolism ; Cytoskeleton ; Escherichia coli - chemistry ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; FtsZ ; Guanosine Diphosphate - chemistry ; Guanosine Diphosphate - genetics ; Guanosine Diphosphate - metabolism ; Molecular Motors ; Protein Assembly ; Protein Self-assembly ; Protein Structure and Folding ; Protein-Protein Interactions ; Unilamellar Liposomes - chemistry</subject><ispartof>The Journal of biological chemistry, 2011-04, Vol.286 (13), p.11236-11241</ispartof><rights>2011 © 2011 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2011 by The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-d1cdf271ef6bd0a83b0e7413503809949ae6f1bb4d74077a7013f2c6de2623123</citedby><cites>FETCH-LOGICAL-c508t-d1cdf271ef6bd0a83b0e7413503809949ae6f1bb4d74077a7013f2c6de2623123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064179/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064179/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,729,782,786,887,27933,27934,53800,53802</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21257762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jiménez, Mercedes</creatorcontrib><creatorcontrib>Martos, Ariadna</creatorcontrib><creatorcontrib>Vicente, Miguel</creatorcontrib><creatorcontrib>Rivas, Germán</creatorcontrib><title>Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have incorporated, for the first time, FtsZ and FtsA (the soluble proto-ring proteins from Escherichia coli) into bacterial giant unilamellar inner membrane vesicles (GUIMVs). Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were determined by confocal microscopy. We found that, in the presence of GDP, FtsZ was homogeneously distributed in the lumen of the vesicle. In the presence of GTP analogs, FtsZ assembled inside the GUIMVs, forming a web of dense spots and fibers. Whereas isolated FtsA was found adsorbed to the inner face of GUIMVs, the addition of FtsZ together with GTP analogs resulted in its dislodgement and its association with the FtsZ fibers in the lumen, suggesting that the FtsA-membrane interaction can be modulated by FtsZ polymers. The use of this novel in vitro system to probe interactions between divisome components will help to determine the biological implications of these findings.</description><subject>Bacterial Cell Division</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane - metabolism</subject><subject>Cytoskeletal Proteins - chemistry</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Cytoskeleton</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>FtsZ</subject><subject>Guanosine Diphosphate - chemistry</subject><subject>Guanosine Diphosphate - genetics</subject><subject>Guanosine Diphosphate - metabolism</subject><subject>Molecular Motors</subject><subject>Protein Assembly</subject><subject>Protein Self-assembly</subject><subject>Protein Structure and Folding</subject><subject>Protein-Protein Interactions</subject><subject>Unilamellar Liposomes - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1v1DAQhi0EokvhzA35BhzS-iOJkwtSqbalUqsiRBHiYjn2ZHeqxC62txL8G_4p3m6p4IAvY4_fecfjh5CXnB1wpurD68EeXPDtqa9l2zwiC846WcmGf31MFowJXvWi6fbIs5SuWVl1z5-SPcFFo1QrFuTXJ7DBp4x5kzF4aryjl3FlPP40d4kw0mWya4ho12ioDRPSjzHkUEX0K7qcYAafE31zktO3u_KyOXpL0Sd0QE_R-EyvPE5mhmkykX6BhHaCRC-HbNCDo2MMM31vbC5NzETPvIdIL2AeovGQnpMno5kSvLiP--TqZPn5-EN1fnl6dnx0XtmGdbly3LpRKA5jOzhmOjkwUDWXDZMd6_u6N9COfBhqp2qmlFGMy1HY1oFoheRC7pN3O9-bzTCDs2WqaCZ9E3E28YcOBvW_Nx7XehVutWRtzVVfDF7fG8TwfQMp6xmT3Q7tIWyS7ppetayvVVEe7pQ2hpQijA9dONNbrrpw1Vuuese1VLz6-3EP-j8gi6DfCaB80S1C1MkieAsOI9isXcD_mv8GQHC1Vw</recordid><startdate>20110401</startdate><enddate>20110401</enddate><creator>Jiménez, Mercedes</creator><creator>Martos, Ariadna</creator><creator>Vicente, Miguel</creator><creator>Rivas, Germán</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110401</creationdate><title>Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes</title><author>Jiménez, Mercedes ; Martos, Ariadna ; Vicente, Miguel ; Rivas, Germán</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-d1cdf271ef6bd0a83b0e7413503809949ae6f1bb4d74077a7013f2c6de2623123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Bacterial Cell Division</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - genetics</topic><topic>Cell Membrane - metabolism</topic><topic>Cytoskeletal Proteins - chemistry</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>Cytoskeleton</topic><topic>Escherichia coli - chemistry</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>FtsZ</topic><topic>Guanosine Diphosphate - chemistry</topic><topic>Guanosine Diphosphate - genetics</topic><topic>Guanosine Diphosphate - metabolism</topic><topic>Molecular Motors</topic><topic>Protein Assembly</topic><topic>Protein Self-assembly</topic><topic>Protein Structure and Folding</topic><topic>Protein-Protein Interactions</topic><topic>Unilamellar Liposomes - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiménez, Mercedes</creatorcontrib><creatorcontrib>Martos, Ariadna</creatorcontrib><creatorcontrib>Vicente, Miguel</creatorcontrib><creatorcontrib>Rivas, Germán</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jiménez, Mercedes</au><au>Martos, Ariadna</au><au>Vicente, Miguel</au><au>Rivas, Germán</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2011-04-01</date><risdate>2011</risdate><volume>286</volume><issue>13</issue><spage>11236</spage><epage>11241</epage><pages>11236-11241</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We have incorporated, for the first time, FtsZ and FtsA (the soluble proto-ring proteins from Escherichia coli) into bacterial giant unilamellar inner membrane vesicles (GUIMVs). Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were determined by confocal microscopy. We found that, in the presence of GDP, FtsZ was homogeneously distributed in the lumen of the vesicle. In the presence of GTP analogs, FtsZ assembled inside the GUIMVs, forming a web of dense spots and fibers. Whereas isolated FtsA was found adsorbed to the inner face of GUIMVs, the addition of FtsZ together with GTP analogs resulted in its dislodgement and its association with the FtsZ fibers in the lumen, suggesting that the FtsA-membrane interaction can be modulated by FtsZ polymers. The use of this novel in vitro system to probe interactions between divisome components will help to determine the biological implications of these findings.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21257762</pmid><doi>10.1074/jbc.M110.194365</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Bacterial Cell Division Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Cell Membrane - chemistry Cell Membrane - genetics Cell Membrane - metabolism Cytoskeletal Proteins - chemistry Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism Cytoskeleton Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism FtsZ Guanosine Diphosphate - chemistry Guanosine Diphosphate - genetics Guanosine Diphosphate - metabolism Molecular Motors Protein Assembly Protein Self-assembly Protein Structure and Folding Protein-Protein Interactions Unilamellar Liposomes - chemistry |
| title | Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes |
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