Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli
The Min protein system creates a dynamic spatial pattern in Escherichia coli cells where the proteins MinD and MinE oscillate from pole to pole. MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is us...
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| description | The Min protein system creates a dynamic spatial pattern in Escherichia coli cells where the proteins MinD and MinE oscillate from pole to pole. MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is used to decompose experimental and model MinD spatial distributions into time-dependent harmonic components. In both experiment and model, the second harmonic component is responsible for producing a mid-cell minimum in MinD concentration. The features of this harmonic are robust in both experiment and model. Fourier analysis reveals a close correspondence between the time-dependent behaviour of the harmonic components in the experimental data and model. Given this, each molecular species in the model was analysed individually. This analysis revealed that membrane-bound MinD dimer shows the mid-cell minimum with the highest contrast when averaged over time, carrying the strongest signal for positioning the cell division ring. This concurs with previous data showing that the MinD dimer binds to MinC inhibiting FtsZ ring formation. These results show that non-linear interactions of Min proteins are essential for producing the mid-cell positioning signal via the generation of second-order harmonic components in the time-dependent spatial protein distribution. |
| doi_str_mv | 10.1371/journal.pone.0185947 |
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MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is used to decompose experimental and model MinD spatial distributions into time-dependent harmonic components. In both experiment and model, the second harmonic component is responsible for producing a mid-cell minimum in MinD concentration. The features of this harmonic are robust in both experiment and model. Fourier analysis reveals a close correspondence between the time-dependent behaviour of the harmonic components in the experimental data and model. Given this, each molecular species in the model was analysed individually. This analysis revealed that membrane-bound MinD dimer shows the mid-cell minimum with the highest contrast when averaged over time, carrying the strongest signal for positioning the cell division ring. This concurs with previous data showing that the MinD dimer binds to MinC inhibiting FtsZ ring formation. These results show that non-linear interactions of Min proteins are essential for producing the mid-cell positioning signal via the generation of second-order harmonic components in the time-dependent spatial protein distribution.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0185947</identifier><identifier>PMID: 29040283</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biology and Life Sciences ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell Division ; Computer and Information Sciences ; Cytoskeletal Proteins - genetics ; Cytoskeletal Proteins - metabolism ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Fourier Analysis ; Gene Expression Regulation, Bacterial ; Kinetics ; Localization ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Min protein ; Morphogenesis ; Nonlinear Dynamics ; Partial differential equations ; Physical sciences ; Protein interaction ; Protein Multimerization ; Proteins ; Research and Analysis Methods ; Signal Transduction ; Spatial distribution ; Time dependence ; Time Factors</subject><ispartof>PloS one, 2017-10, Vol.12 (10), p.e0185947-e0185947</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Walsh et al. 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MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is used to decompose experimental and model MinD spatial distributions into time-dependent harmonic components. In both experiment and model, the second harmonic component is responsible for producing a mid-cell minimum in MinD concentration. The features of this harmonic are robust in both experiment and model. Fourier analysis reveals a close correspondence between the time-dependent behaviour of the harmonic components in the experimental data and model. Given this, each molecular species in the model was analysed individually. This analysis revealed that membrane-bound MinD dimer shows the mid-cell minimum with the highest contrast when averaged over time, carrying the strongest signal for positioning the cell division ring. This concurs with previous data showing that the MinD dimer binds to MinC inhibiting FtsZ ring formation. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Walsh, James C</au><au>Angstmann, Christopher N</au><au>Duggin, Iain G</au><au>Curmi, Paul M G</au><au>Aguilar, Ruben Claudio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-10-17</date><risdate>2017</risdate><volume>12</volume><issue>10</issue><spage>e0185947</spage><epage>e0185947</epage><pages>e0185947-e0185947</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The Min protein system creates a dynamic spatial pattern in Escherichia coli cells where the proteins MinD and MinE oscillate from pole to pole. MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is used to decompose experimental and model MinD spatial distributions into time-dependent harmonic components. In both experiment and model, the second harmonic component is responsible for producing a mid-cell minimum in MinD concentration. The features of this harmonic are robust in both experiment and model. Fourier analysis reveals a close correspondence between the time-dependent behaviour of the harmonic components in the experimental data and model. Given this, each molecular species in the model was analysed individually. This analysis revealed that membrane-bound MinD dimer shows the mid-cell minimum with the highest contrast when averaged over time, carrying the strongest signal for positioning the cell division ring. This concurs with previous data showing that the MinD dimer binds to MinC inhibiting FtsZ ring formation. These results show that non-linear interactions of Min proteins are essential for producing the mid-cell positioning signal via the generation of second-order harmonic components in the time-dependent spatial protein distribution.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29040283</pmid><doi>10.1371/journal.pone.0185947</doi><tpages>e0185947</tpages><orcidid>https://orcid.org/0000-0001-5762-7638</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Biology and Life Sciences Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell Division Computer and Information Sciences Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism E coli Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fourier Analysis Gene Expression Regulation, Bacterial Kinetics Localization Membrane Proteins - genetics Membrane Proteins - metabolism Min protein Morphogenesis Nonlinear Dynamics Partial differential equations Physical sciences Protein interaction Protein Multimerization Proteins Research and Analysis Methods Signal Transduction Spatial distribution Time dependence Time Factors |
| title | Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli |
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