Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane
The bacterial flagellum exemplifies a system where even small deviations from the highly regulated flagellar assembly process can abolish motility and cause negative physiological outcomes. Consequently, bacteria have evolved elegant and robust regulatory mechanisms to ensure that flagellar morphoge...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2017-04, Vol.356 (6334), p.197-200 |
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| creator | Cohen, Eli J. Ferreira, Josie L. Ladinsky, Mark S. Beeby, Morgan Hughes, Kelly T. |
| description | The bacterial flagellum exemplifies a system where even small deviations from the highly regulated flagellar assembly process can abolish motility and cause negative physiological outcomes. Consequently, bacteria have evolved elegant and robust regulatory mechanisms to ensure that flagellar morphogenesis follows a defined path, with each component self-assembling to predetermined dimensions. The flagellar rod acts as a driveshaft to transmit torque from the cytoplasmic rotor to the external filament. The rod self-assembles to a defined length of ~25 nanometers. Here, we provide evidence that rod length is limited by the width of the periplasmic space between the inner and outer membranes. The length of Braun's lipoprotein determines periplasmic width by tethering the outer membrane to the peptidoglycan layer. |
| doi_str_mv | 10.1126/science.aam6512 |
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Consequently, bacteria have evolved elegant and robust regulatory mechanisms to ensure that flagellar morphogenesis follows a defined path, with each component self-assembling to predetermined dimensions. The flagellar rod acts as a driveshaft to transmit torque from the cytoplasmic rotor to the external filament. The rod self-assembles to a defined length of ~25 nanometers. Here, we provide evidence that rod length is limited by the width of the periplasmic space between the inner and outer membranes. The length of Braun's lipoprotein determines periplasmic width by tethering the outer membrane to the peptidoglycan layer.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aam6512</identifier><identifier>PMID: 28408605</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Automation ; Bacteria ; Bacteria - ultrastructure ; Bacterial proteins ; Bacterial Proteins - ultrastructure ; Biofilms ; Cell Membrane - ultrastructure ; Crystal structure ; Deviation ; Escherichia coli - ultrastructure ; Filaments ; Flagella ; Flagella - ultrastructure ; Lipids ; Lipoproteins - ultrastructure ; Manufacturing engineering ; Membranes ; Morphogenesis ; Nanostructure ; Nanotechnology devices ; Outer membranes ; Pathogenesis ; Peptidoglycan - ultrastructure ; Peptidoglycans ; Periplasm ; Periplasm - ultrastructure ; Periplasmic space ; Regulatory mechanisms (biology) ; Robotics ; Salmonella enterica - ultrastructure ; Self-assembly ; Shafts (machine elements) ; Tethering ; Torque</subject><ispartof>Science (American Association for the Advancement of Science), 2017-04, Vol.356 (6334), p.197-200</ispartof><rights>Copyright © 2017 American Association for the Advancement of Science</rights><rights>Copyright © 2017, American Association for the Advancement of Science.</rights><rights>Copyright © 2017, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c579t-1c056e34005f0ab0efb644bcef971d8af1b46d11272e9b02abe8f226c5481e693</citedby><cites>FETCH-LOGICAL-c579t-1c056e34005f0ab0efb644bcef971d8af1b46d11272e9b02abe8f226c5481e693</cites><orcidid>0000-0001-9265-7517 ; 0000-0002-4411-6131 ; 0000-0002-1036-3513 ; 0000-0001-5344-0972 ; 0000-0001-6413-9835</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24918215$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24918215$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28408605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cohen, Eli J.</creatorcontrib><creatorcontrib>Ferreira, Josie L.</creatorcontrib><creatorcontrib>Ladinsky, Mark S.</creatorcontrib><creatorcontrib>Beeby, Morgan</creatorcontrib><creatorcontrib>Hughes, Kelly T.</creatorcontrib><title>Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The bacterial flagellum exemplifies a system where even small deviations from the highly regulated flagellar assembly process can abolish motility and cause negative physiological outcomes. Consequently, bacteria have evolved elegant and robust regulatory mechanisms to ensure that flagellar morphogenesis follows a defined path, with each component self-assembling to predetermined dimensions. The flagellar rod acts as a driveshaft to transmit torque from the cytoplasmic rotor to the external filament. The rod self-assembles to a defined length of ~25 nanometers. Here, we provide evidence that rod length is limited by the width of the periplasmic space between the inner and outer membranes. The length of Braun's lipoprotein determines periplasmic width by tethering the outer membrane to the peptidoglycan layer.</description><subject>Automation</subject><subject>Bacteria</subject><subject>Bacteria - ultrastructure</subject><subject>Bacterial proteins</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Biofilms</subject><subject>Cell Membrane - ultrastructure</subject><subject>Crystal structure</subject><subject>Deviation</subject><subject>Escherichia coli - ultrastructure</subject><subject>Filaments</subject><subject>Flagella</subject><subject>Flagella - ultrastructure</subject><subject>Lipids</subject><subject>Lipoproteins - ultrastructure</subject><subject>Manufacturing engineering</subject><subject>Membranes</subject><subject>Morphogenesis</subject><subject>Nanostructure</subject><subject>Nanotechnology devices</subject><subject>Outer membranes</subject><subject>Pathogenesis</subject><subject>Peptidoglycan - ultrastructure</subject><subject>Peptidoglycans</subject><subject>Periplasm</subject><subject>Periplasm - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cohen, Eli J.</au><au>Ferreira, Josie L.</au><au>Ladinsky, Mark S.</au><au>Beeby, Morgan</au><au>Hughes, Kelly T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2017-04-14</date><risdate>2017</risdate><volume>356</volume><issue>6334</issue><spage>197</spage><epage>200</epage><pages>197-200</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>The bacterial flagellum exemplifies a system where even small deviations from the highly regulated flagellar assembly process can abolish motility and cause negative physiological outcomes. Consequently, bacteria have evolved elegant and robust regulatory mechanisms to ensure that flagellar morphogenesis follows a defined path, with each component self-assembling to predetermined dimensions. The flagellar rod acts as a driveshaft to transmit torque from the cytoplasmic rotor to the external filament. The rod self-assembles to a defined length of ~25 nanometers. Here, we provide evidence that rod length is limited by the width of the periplasmic space between the inner and outer membranes. 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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Automation Bacteria Bacteria - ultrastructure Bacterial proteins Bacterial Proteins - ultrastructure Biofilms Cell Membrane - ultrastructure Crystal structure Deviation Escherichia coli - ultrastructure Filaments Flagella Flagella - ultrastructure Lipids Lipoproteins - ultrastructure Manufacturing engineering Membranes Morphogenesis Nanostructure Nanotechnology devices Outer membranes Pathogenesis Peptidoglycan - ultrastructure Peptidoglycans Periplasm Periplasm - ultrastructure Periplasmic space Regulatory mechanisms (biology) Robotics Salmonella enterica - ultrastructure Self-assembly Shafts (machine elements) Tethering Torque |
| title | Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane |
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