Localization of the flagellum-specific secretion signal in Salmonella flagellin
The flagellum-specific export system is a specialized type III export machinery. Terminally truncated fragments of flagellin (FliC) were used to identify the secretion signal in the main component of flagellar filaments. The first 13 residues were not essential for export, but removal of 29 or more...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-06, Vol.345 (1), p.93-98 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Végh, Barbara M. Gál, Péter Dobó, József Závodszky, Péter Vonderviszt, Ferenc |
| description | The flagellum-specific export system is a specialized type III export machinery. Terminally truncated fragments of flagellin (FliC) were used to identify the secretion signal in the main component of flagellar filaments. The first 13 residues were not essential for export, but removal of 29 or more residues destroyed export ability. When an 8
kDa human protein domain was fused to various N-terminal fragments of FliC, the 26–47 sequence alone was sufficient to mediate secretion of this protein module through the flagellum specific export pathway. Neither half of this segment was enough to direct export of the attached protein domain. Our results demonstrate that the 22-residue long 26–47 segment within the disordered N-terminal region of
Salmonella flagellin contains the recognition signal for the flagellar export machinery. |
| doi_str_mv | 10.1016/j.bbrc.2006.04.055 |
| format | Article |
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kDa human protein domain was fused to various N-terminal fragments of FliC, the 26–47 sequence alone was sufficient to mediate secretion of this protein module through the flagellum specific export pathway. Neither half of this segment was enough to direct export of the attached protein domain. Our results demonstrate that the 22-residue long 26–47 segment within the disordered N-terminal region of
Salmonella flagellin contains the recognition signal for the flagellar export machinery.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.04.055</identifier><identifier>PMID: 16674914</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Binding Sites ; Export signal ; Flagella - chemistry ; Flagella - metabolism ; Flagellin ; Flagellin - chemistry ; Flagellin - metabolism ; Flagellum-specific export ; Molecular Motor Proteins - chemistry ; Molecular Motor Proteins - metabolism ; Molecular Sequence Data ; Nuclear Export Signals - physiology ; Protein Structure, Tertiary ; Salmonella ; Salmonella - chemistry ; Salmonella - metabolism ; Salmonella - ultrastructure ; Salmonella typhimurium ; Signal Transduction - physiology ; Type III secretion</subject><ispartof>Biochemical and biophysical research communications, 2006-06, Vol.345 (1), p.93-98</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-c08c8b0d98e367571f59ae6bc1722478ac1ecad74e7a2b30e9c6079e17738d973</citedby><cites>FETCH-LOGICAL-c451t-c08c8b0d98e367571f59ae6bc1722478ac1ecad74e7a2b30e9c6079e17738d973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2006.04.055$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16674914$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Végh, Barbara M.</creatorcontrib><creatorcontrib>Gál, Péter</creatorcontrib><creatorcontrib>Dobó, József</creatorcontrib><creatorcontrib>Závodszky, Péter</creatorcontrib><creatorcontrib>Vonderviszt, Ferenc</creatorcontrib><title>Localization of the flagellum-specific secretion signal in Salmonella flagellin</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The flagellum-specific export system is a specialized type III export machinery. Terminally truncated fragments of flagellin (FliC) were used to identify the secretion signal in the main component of flagellar filaments. The first 13 residues were not essential for export, but removal of 29 or more residues destroyed export ability. When an 8
kDa human protein domain was fused to various N-terminal fragments of FliC, the 26–47 sequence alone was sufficient to mediate secretion of this protein module through the flagellum specific export pathway. Neither half of this segment was enough to direct export of the attached protein domain. Our results demonstrate that the 22-residue long 26–47 segment within the disordered N-terminal region of
Salmonella flagellin contains the recognition signal for the flagellar export machinery.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Export signal</subject><subject>Flagella - chemistry</subject><subject>Flagella - metabolism</subject><subject>Flagellin</subject><subject>Flagellin - chemistry</subject><subject>Flagellin - metabolism</subject><subject>Flagellum-specific export</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Export Signals - physiology</subject><subject>Protein Structure, Tertiary</subject><subject>Salmonella</subject><subject>Salmonella - chemistry</subject><subject>Salmonella - metabolism</subject><subject>Salmonella - ultrastructure</subject><subject>Salmonella typhimurium</subject><subject>Signal Transduction - physiology</subject><subject>Type III secretion</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQhq0KVBbaP9ADyolb0hmvY8dSLxWiUGklDoDEzXImE-pVPrZ2thL99c2yi3qD0xzmed8ZPUJ8QSgQUH9dF3UdqZAAugBVQFl-EAsEC7lEUEdiAfMmlxYfT8RpSmsARKXtR3GCWhtlUS3E7Wok34W_fgrjkI1tNv3irO38E3fdts_Thim0gbLEFPmFSeFp8F0WhuzOd_04zKB_TYThkzhufZf482GeiYcfV_eXN_nq9vrn5fdVTqrEKSeoqKqhsRUvtSkNtqX1rGtCI6UylSdk8o1RbLysl8CWNBjLaMyyaqxZnomLfe8mjr-3nCbXh0S7XwYet8lpY01lJb4LzgdRllU5g3IPUhxTity6TQy9j88Owe18u7Xb-XY73w6Um33PofND-7buufkfOQiegW97gGcZfwJHlyjwQNyEyDS5Zgxv9f8DDGWReg</recordid><startdate>20060623</startdate><enddate>20060623</enddate><creator>Végh, Barbara M.</creator><creator>Gál, Péter</creator><creator>Dobó, József</creator><creator>Závodszky, Péter</creator><creator>Vonderviszt, Ferenc</creator><general>Elsevier Inc</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20060623</creationdate><title>Localization of the flagellum-specific secretion signal in Salmonella flagellin</title><author>Végh, Barbara M. ; Gál, Péter ; Dobó, József ; Závodszky, Péter ; Vonderviszt, Ferenc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-c08c8b0d98e367571f59ae6bc1722478ac1ecad74e7a2b30e9c6079e17738d973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Export signal</topic><topic>Flagella - chemistry</topic><topic>Flagella - metabolism</topic><topic>Flagellin</topic><topic>Flagellin - chemistry</topic><topic>Flagellin - metabolism</topic><topic>Flagellum-specific export</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Molecular Motor Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Export Signals - physiology</topic><topic>Protein Structure, Tertiary</topic><topic>Salmonella</topic><topic>Salmonella - chemistry</topic><topic>Salmonella - metabolism</topic><topic>Salmonella - ultrastructure</topic><topic>Salmonella typhimurium</topic><topic>Signal Transduction - physiology</topic><topic>Type III secretion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Végh, Barbara M.</creatorcontrib><creatorcontrib>Gál, Péter</creatorcontrib><creatorcontrib>Dobó, József</creatorcontrib><creatorcontrib>Závodszky, Péter</creatorcontrib><creatorcontrib>Vonderviszt, Ferenc</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Végh, Barbara M.</au><au>Gál, Péter</au><au>Dobó, József</au><au>Závodszky, Péter</au><au>Vonderviszt, Ferenc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of the flagellum-specific secretion signal in Salmonella flagellin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-06-23</date><risdate>2006</risdate><volume>345</volume><issue>1</issue><spage>93</spage><epage>98</epage><pages>93-98</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The flagellum-specific export system is a specialized type III export machinery. 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kDa human protein domain was fused to various N-terminal fragments of FliC, the 26–47 sequence alone was sufficient to mediate secretion of this protein module through the flagellum specific export pathway. Neither half of this segment was enough to direct export of the attached protein domain. Our results demonstrate that the 22-residue long 26–47 segment within the disordered N-terminal region of
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| ispartof | Biochemical and biophysical research communications, 2006-06, Vol.345 (1), p.93-98 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Binding Sites Export signal Flagella - chemistry Flagella - metabolism Flagellin Flagellin - chemistry Flagellin - metabolism Flagellum-specific export Molecular Motor Proteins - chemistry Molecular Motor Proteins - metabolism Molecular Sequence Data Nuclear Export Signals - physiology Protein Structure, Tertiary Salmonella Salmonella - chemistry Salmonella - metabolism Salmonella - ultrastructure Salmonella typhimurium Signal Transduction - physiology Type III secretion |
| title | Localization of the flagellum-specific secretion signal in Salmonella flagellin |
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