A diffusiophoretic mechanism for ATP-driven transport without motor proteins
The healthy growth and maintenance of a biological system depends on the precise spatial organization of molecules within the cell through the dissipation of energy. Reaction–diffusion mechanisms can facilitate this organization, as can directional cargo transport orchestrated by motor proteins, by...
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Veröffentlicht in: | Nature physics 2021-07, Vol.17 (7), p.850-858 |
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description | The healthy growth and maintenance of a biological system depends on the precise spatial organization of molecules within the cell through the dissipation of energy. Reaction–diffusion mechanisms can facilitate this organization, as can directional cargo transport orchestrated by motor proteins, by relying on specific protein interactions. However, transport of material through the cell can also be achieved by active processes based on non-specific, purely physical mechanisms, a phenomenon that remains poorly explored. Here, using a combined experimental and theoretical approach, we discover and describe a hidden function of the
Escherichia coli
MinDE protein system: in addition to forming dynamic patterns, this system accomplishes the directional active transport of functionally unrelated cargo on membranes. Remarkably, this mechanism enables the sorting of diffusive objects according to their effective size, as evidenced using modular DNA origami–streptavidin nanostructures. We show that the diffusive fluxes of MinDE and non-specific cargo couple via density-dependent friction. This non-specific process constitutes a diffusiophoretic mechanism, as yet unknown in a cell biology setting. This nonlinear coupling between diffusive fluxes could represent a generic physical mechanism for establishing intracellular organization.
Protein oscillations linked to cell division in
Escherichia coli
are shown to localize unrelated molecules on the cell membrane via a diffusiophoretic mechanism, in which an effective friction fosters cargo transport along the fluxes set up by the proteins. |
doi_str_mv | 10.1038/s41567-021-01213-3 |
format | Article |
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Escherichia coli
MinDE protein system: in addition to forming dynamic patterns, this system accomplishes the directional active transport of functionally unrelated cargo on membranes. Remarkably, this mechanism enables the sorting of diffusive objects according to their effective size, as evidenced using modular DNA origami–streptavidin nanostructures. We show that the diffusive fluxes of MinDE and non-specific cargo couple via density-dependent friction. This non-specific process constitutes a diffusiophoretic mechanism, as yet unknown in a cell biology setting. This nonlinear coupling between diffusive fluxes could represent a generic physical mechanism for establishing intracellular organization.
Protein oscillations linked to cell division in
Escherichia coli
are shown to localize unrelated molecules on the cell membrane via a diffusiophoretic mechanism, in which an effective friction fosters cargo transport along the fluxes set up by the proteins.</description><identifier>ISSN: 1745-2473</identifier><identifier>EISSN: 1745-2481</identifier><identifier>DOI: 10.1038/s41567-021-01213-3</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/57 ; 639/766/530 ; 639/766/747 ; Atomic ; Cargo transportation ; Cell division ; Cell membranes ; Classical and Continuum Physics ; Complex Systems ; Condensed Matter Physics ; Coupling (molecular) ; E coli ; Energy dissipation ; Fluxes ; Friction ; Mathematical and Computational Physics ; Molecular ; Molecular motors ; Optical and Plasma Physics ; Physics ; Physics and Astronomy ; Proteins ; Theoretical</subject><ispartof>Nature physics, 2021-07, Vol.17 (7), p.850-858</ispartof><rights>The Author(s) 2021</rights><rights>The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-bca598b28fdeb3c33bfd79825241d3ef5a22bfb910041c3d6b7358b45801f4b33</citedby><cites>FETCH-LOGICAL-c429t-bca598b28fdeb3c33bfd79825241d3ef5a22bfb910041c3d6b7358b45801f4b33</cites><orcidid>0000-0001-6776-9437 ; 0000-0003-1584-9800 ; 0000-0001-8792-3358 ; 0000-0001-9106-9406 ; 0000-0002-6106-4847 ; 0000-0002-7402-1942 ; 0000-0001-8737-2939</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41567-021-01213-3$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41567-021-01213-3$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,27911,27912,41475,42544,51306</link.rule.ids></links><search><creatorcontrib>Ramm, Beatrice</creatorcontrib><creatorcontrib>Goychuk, Andriy</creatorcontrib><creatorcontrib>Khmelinskaia, Alena</creatorcontrib><creatorcontrib>Blumhardt, Philipp</creatorcontrib><creatorcontrib>Eto, Hiromune</creatorcontrib><creatorcontrib>Ganzinger, Kristina A.</creatorcontrib><creatorcontrib>Frey, Erwin</creatorcontrib><creatorcontrib>Schwille, Petra</creatorcontrib><title>A diffusiophoretic mechanism for ATP-driven transport without motor proteins</title><title>Nature physics</title><addtitle>Nat. Phys</addtitle><description>The healthy growth and maintenance of a biological system depends on the precise spatial organization of molecules within the cell through the dissipation of energy. Reaction–diffusion mechanisms can facilitate this organization, as can directional cargo transport orchestrated by motor proteins, by relying on specific protein interactions. However, transport of material through the cell can also be achieved by active processes based on non-specific, purely physical mechanisms, a phenomenon that remains poorly explored. Here, using a combined experimental and theoretical approach, we discover and describe a hidden function of the
Escherichia coli
MinDE protein system: in addition to forming dynamic patterns, this system accomplishes the directional active transport of functionally unrelated cargo on membranes. Remarkably, this mechanism enables the sorting of diffusive objects according to their effective size, as evidenced using modular DNA origami–streptavidin nanostructures. We show that the diffusive fluxes of MinDE and non-specific cargo couple via density-dependent friction. This non-specific process constitutes a diffusiophoretic mechanism, as yet unknown in a cell biology setting. This nonlinear coupling between diffusive fluxes could represent a generic physical mechanism for establishing intracellular organization.
Protein oscillations linked to cell division in
Escherichia coli
are shown to localize unrelated molecules on the cell membrane via a diffusiophoretic mechanism, in which an effective friction fosters cargo transport along the fluxes set up by the proteins.</description><subject>631/57</subject><subject>639/766/530</subject><subject>639/766/747</subject><subject>Atomic</subject><subject>Cargo transportation</subject><subject>Cell division</subject><subject>Cell membranes</subject><subject>Classical and Continuum Physics</subject><subject>Complex Systems</subject><subject>Condensed Matter Physics</subject><subject>Coupling (molecular)</subject><subject>E coli</subject><subject>Energy dissipation</subject><subject>Fluxes</subject><subject>Friction</subject><subject>Mathematical and Computational Physics</subject><subject>Molecular</subject><subject>Molecular motors</subject><subject>Optical and Plasma Physics</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Proteins</subject><subject>Theoretical</subject><issn>1745-2473</issn><issn>1745-2481</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kMtOwzAQRS0EEuXxA6wisTZ4PHbjLKuKl1QJFmVtxYlNXZE42A6IvyelCHasZhbn3hkdQi6AXQFDdZ0EyHlJGQfKgANSPCAzKIWkXCg4_N1LPCYnKW0ZE3wOOCOrRdF658bkw7AJ0WbfFJ1tNnXvU1e4EIvF-om20b_bvsix7tMQYi4-fN6EMRddyBMyxJCt79MZOXL1a7LnP_OUPN_erJf3dPV497BcrGgjeJWpaWpZKcOVa63BBtG4tqwUl1xAi9bJmnPjTAXTl9BgOzclSmWEVAycMIin5HLfOx1-G23KehvG2E8nNZeSCYWCwUTxPdXEkFK0Tg_Rd3X81MD0zpreW9OTNf1tTe-qcR9KE9y_2PhX_U_qC9B_cCo</recordid><startdate>20210701</startdate><enddate>20210701</enddate><creator>Ramm, Beatrice</creator><creator>Goychuk, Andriy</creator><creator>Khmelinskaia, Alena</creator><creator>Blumhardt, Philipp</creator><creator>Eto, Hiromune</creator><creator>Ganzinger, Kristina A.</creator><creator>Frey, Erwin</creator><creator>Schwille, Petra</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7U5</scope><scope>7XB</scope><scope>88I</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>L7M</scope><scope>M2P</scope><scope>P5Z</scope><scope>P62</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><orcidid>https://orcid.org/0000-0001-6776-9437</orcidid><orcidid>https://orcid.org/0000-0003-1584-9800</orcidid><orcidid>https://orcid.org/0000-0001-8792-3358</orcidid><orcidid>https://orcid.org/0000-0001-9106-9406</orcidid><orcidid>https://orcid.org/0000-0002-6106-4847</orcidid><orcidid>https://orcid.org/0000-0002-7402-1942</orcidid><orcidid>https://orcid.org/0000-0001-8737-2939</orcidid></search><sort><creationdate>20210701</creationdate><title>A diffusiophoretic mechanism for ATP-driven transport without motor proteins</title><author>Ramm, Beatrice ; 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Phys</stitle><date>2021-07-01</date><risdate>2021</risdate><volume>17</volume><issue>7</issue><spage>850</spage><epage>858</epage><pages>850-858</pages><issn>1745-2473</issn><eissn>1745-2481</eissn><abstract>The healthy growth and maintenance of a biological system depends on the precise spatial organization of molecules within the cell through the dissipation of energy. Reaction–diffusion mechanisms can facilitate this organization, as can directional cargo transport orchestrated by motor proteins, by relying on specific protein interactions. However, transport of material through the cell can also be achieved by active processes based on non-specific, purely physical mechanisms, a phenomenon that remains poorly explored. Here, using a combined experimental and theoretical approach, we discover and describe a hidden function of the
Escherichia coli
MinDE protein system: in addition to forming dynamic patterns, this system accomplishes the directional active transport of functionally unrelated cargo on membranes. Remarkably, this mechanism enables the sorting of diffusive objects according to their effective size, as evidenced using modular DNA origami–streptavidin nanostructures. We show that the diffusive fluxes of MinDE and non-specific cargo couple via density-dependent friction. This non-specific process constitutes a diffusiophoretic mechanism, as yet unknown in a cell biology setting. This nonlinear coupling between diffusive fluxes could represent a generic physical mechanism for establishing intracellular organization.
Protein oscillations linked to cell division in
Escherichia coli
are shown to localize unrelated molecules on the cell membrane via a diffusiophoretic mechanism, in which an effective friction fosters cargo transport along the fluxes set up by the proteins.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><doi>10.1038/s41567-021-01213-3</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-6776-9437</orcidid><orcidid>https://orcid.org/0000-0003-1584-9800</orcidid><orcidid>https://orcid.org/0000-0001-8792-3358</orcidid><orcidid>https://orcid.org/0000-0001-9106-9406</orcidid><orcidid>https://orcid.org/0000-0002-6106-4847</orcidid><orcidid>https://orcid.org/0000-0002-7402-1942</orcidid><orcidid>https://orcid.org/0000-0001-8737-2939</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 631/57 639/766/530 639/766/747 Atomic Cargo transportation Cell division Cell membranes Classical and Continuum Physics Complex Systems Condensed Matter Physics Coupling (molecular) E coli Energy dissipation Fluxes Friction Mathematical and Computational Physics Molecular Molecular motors Optical and Plasma Physics Physics Physics and Astronomy Proteins Theoretical |
title | A diffusiophoretic mechanism for ATP-driven transport without motor proteins |
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