HOW BACTERIA ASSEMBLE FLAGELLA
The bacterial flagellum is both a motor organelle and a protein export/assembly apparatus. It extends from the cytoplasm to the cell exterior. All the protein subunits of the external elements have to be exported. Export employs a type III pathway, also utilized for secretion of virulence factors. S...
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| Veröffentlicht in: | Annual review of microbiology 2003-01, Vol.57 (1), p.77-100 |
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| creator | Macnab, Robert M |
| description | The bacterial flagellum is both a motor organelle and a protein
export/assembly apparatus. It extends from the cytoplasm to the cell exterior.
All the protein subunits of the external elements have to be exported. Export
employs a type III pathway, also utilized for secretion of virulence factors.
Six of the components of the export apparatus are integral membrane proteins
and are believed to be located within the flagellar basal body. Three others
are soluble: the ATPase that drives export, a regulator of the ATPase, and a
general chaperone. Exported substrates diffuse down a narrow channel in the
growing structure and assemble at the distal end, often with the help of a
capping structure. |
| doi_str_mv | 10.1146/annurev.micro.57.030502.090832 |
| format | Article |
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export/assembly apparatus. It extends from the cytoplasm to the cell exterior.
All the protein subunits of the external elements have to be exported. Export
employs a type III pathway, also utilized for secretion of virulence factors.
Six of the components of the export apparatus are integral membrane proteins
and are believed to be located within the flagellar basal body. Three others
are soluble: the ATPase that drives export, a regulator of the ATPase, and a
general chaperone. Exported substrates diffuse down a narrow channel in the
growing structure and assemble at the distal end, often with the help of a
capping structure.</description><identifier>ISSN: 0066-4227</identifier><identifier>EISSN: 1545-3251</identifier><identifier>DOI: 10.1146/annurev.micro.57.030502.090832</identifier><identifier>PMID: 12730325</identifier><identifier>CODEN: ARMIAZ</identifier><language>eng</language><publisher>Palo Alto, CA 94303-0139: Annual Reviews</publisher><subject>Adenosine Triphosphatases - physiology ; assembly ; Bacteria ; Bacterial Physiological Phenomena ; Bacterial Proteins - physiology ; Bacteriology ; Biological and medical sciences ; Cell division ; Flagella (Microbiology) ; Flagella - physiology ; flagellum ; Fundamental and applied biological sciences. Psychology ; Genes, Regulator - physiology ; Membrane Proteins - physiology ; Microbiology ; Miscellaneous ; Molecular Chaperones - physiology ; Morphogenesis - physiology ; motility ; protein export ; Proteins ; type III pathway</subject><ispartof>Annual review of microbiology, 2003-01, Vol.57 (1), p.77-100</ispartof><rights>Copyright © 2003 by Annual Reviews. All rights reserved</rights><rights>2004 INIST-CNRS</rights><rights>COPYRIGHT 2003 Annual Reviews, Inc.</rights><rights>Copyright Annual Reviews, Inc. 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a614t-738cbaad4245f5fedb3275603fce74f83e1bf3da7a4dbcaaed42d64649e9fd0e3</citedby><cites>FETCH-LOGICAL-a614t-738cbaad4245f5fedb3275603fce74f83e1bf3da7a4dbcaaed42d64649e9fd0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.micro.57.030502.090832?crawler=true&mimetype=application/pdf$$EPDF$$P50$$Gannualreviews$$H</linktopdf><linktohtml>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.micro.57.030502.090832$$EHTML$$P50$$Gannualreviews$$H</linktohtml><link.rule.ids>70,314,780,784,4182,27924,27925,78254,78255</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15232045$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12730325$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Macnab, Robert M</creatorcontrib><title>HOW BACTERIA ASSEMBLE FLAGELLA</title><title>Annual review of microbiology</title><addtitle>Annu Rev Microbiol</addtitle><description>The bacterial flagellum is both a motor organelle and a protein
export/assembly apparatus. It extends from the cytoplasm to the cell exterior.
All the protein subunits of the external elements have to be exported. Export
employs a type III pathway, also utilized for secretion of virulence factors.
Six of the components of the export apparatus are integral membrane proteins
and are believed to be located within the flagellar basal body. Three others
are soluble: the ATPase that drives export, a regulator of the ATPase, and a
general chaperone. Exported substrates diffuse down a narrow channel in the
growing structure and assemble at the distal end, often with the help of a
capping structure.</description><subject>Adenosine Triphosphatases - physiology</subject><subject>assembly</subject><subject>Bacteria</subject><subject>Bacterial Physiological Phenomena</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell division</subject><subject>Flagella (Microbiology)</subject><subject>Flagella - physiology</subject><subject>flagellum</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Regulator - physiology</subject><subject>Membrane Proteins - physiology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Chaperones - physiology</subject><subject>Morphogenesis - physiology</subject><subject>motility</subject><subject>protein export</subject><subject>Proteins</subject><subject>type III pathway</subject><issn>0066-4227</issn><issn>1545-3251</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqVkVtr3DAQRkVpaDZp_0JYCs2bndHdfik4i3MBh0CT0kch26Pg4LVTad3Sf19tbAiUQAl6EIjzzWjmEHJKIaVUqDM7DJPHX-m2a_yYSp0CBwkshRwyzt6RFZVCJpxJ-p6sAJRKBGP6kByF8AgAQkP-gRxSpjlEaEVOrm5_rM-LzX357bpYF3d35c15Va4vquKyrKriIzlwtg_4abmPyfeL8n5zlVS3l9ebokqsomKXaJ41tbWtYEI66bCtOdNSAXcNauEyjrR2vLXairZurMVItkookWPuWkB-TE7nuk9-_Dlh2JltFxrsezvgOAWjpRZC6ey_IM0Z5IrSCH7-B3wcJz_EIQwDmcVlZftqyQw92B5NN7hx523zgAN6248Dui4-F5TSuGKaycinr_DxtBiFvBr4OgeirRA8OvPku631fwwFsxdqFqHmWaiR2sxCzSw0FjhZxpjqLbYv8cVgBL4sgA2N7Z23Q9OFF04yzkDsuc3M7RvaPrbs8Hd463f-AgTevtM</recordid><startdate>20030101</startdate><enddate>20030101</enddate><creator>Macnab, Robert M</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</general><scope>IQODW</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>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PADUT</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>R05</scope><scope>7X8</scope></search><sort><creationdate>20030101</creationdate><title>HOW BACTERIA ASSEMBLE FLAGELLA</title><author>Macnab, Robert M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a614t-738cbaad4245f5fedb3275603fce74f83e1bf3da7a4dbcaaed42d64649e9fd0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adenosine Triphosphatases - physiology</topic><topic>assembly</topic><topic>Bacteria</topic><topic>Bacterial Physiological Phenomena</topic><topic>Bacterial Proteins - physiology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell division</topic><topic>Flagella (Microbiology)</topic><topic>Flagella - physiology</topic><topic>flagellum</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Regulator - physiology</topic><topic>Membrane Proteins - physiology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular Chaperones - physiology</topic><topic>Morphogenesis - physiology</topic><topic>motility</topic><topic>protein export</topic><topic>Proteins</topic><topic>type III pathway</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Macnab, Robert M</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Research Library China</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>MEDLINE - Academic</collection><jtitle>Annual review of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Macnab, Robert M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HOW BACTERIA ASSEMBLE FLAGELLA</atitle><jtitle>Annual review of microbiology</jtitle><addtitle>Annu Rev Microbiol</addtitle><date>2003-01-01</date><risdate>2003</risdate><volume>57</volume><issue>1</issue><spage>77</spage><epage>100</epage><pages>77-100</pages><issn>0066-4227</issn><eissn>1545-3251</eissn><coden>ARMIAZ</coden><abstract>The bacterial flagellum is both a motor organelle and a protein
export/assembly apparatus. It extends from the cytoplasm to the cell exterior.
All the protein subunits of the external elements have to be exported. Export
employs a type III pathway, also utilized for secretion of virulence factors.
Six of the components of the export apparatus are integral membrane proteins
and are believed to be located within the flagellar basal body. Three others
are soluble: the ATPase that drives export, a regulator of the ATPase, and a
general chaperone. Exported substrates diffuse down a narrow channel in the
growing structure and assemble at the distal end, often with the help of a
capping structure.</abstract><cop>Palo Alto, CA 94303-0139</cop><cop>4139 El Camino Way, P.O. Box 10139</cop><cop>USA</cop><pub>Annual Reviews</pub><pmid>12730325</pmid><doi>10.1146/annurev.micro.57.030502.090832</doi><tpages>24</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0066-4227 |
| ispartof | Annual review of microbiology, 2003-01, Vol.57 (1), p.77-100 |
| issn | 0066-4227 1545-3251 |
| language | eng |
| recordid | cdi_gale_infotracacademiconefile_A111502185 |
| source | Annual Reviews; MEDLINE |
| subjects | Adenosine Triphosphatases - physiology assembly Bacteria Bacterial Physiological Phenomena Bacterial Proteins - physiology Bacteriology Biological and medical sciences Cell division Flagella (Microbiology) Flagella - physiology flagellum Fundamental and applied biological sciences. Psychology Genes, Regulator - physiology Membrane Proteins - physiology Microbiology Miscellaneous Molecular Chaperones - physiology Morphogenesis - physiology motility protein export Proteins type III pathway |
| title | HOW BACTERIA ASSEMBLE FLAGELLA |
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