Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin‐like conjugative structure on Agrobacterium tumefaciens
The virB operon of the Agrobacterium tumefaciens Ti plasmid encodes 11 proteins. Specific antisera to VirB2, VirB3 and VirB9 were used to locate these virulence proteins in the A. tumefaciens cell. Immunoblot analysis located VirB2 protein to the inner and outer membranes; VirB3 and VirB9 were likew...
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Veröffentlicht in: | FEMS microbiology letters 1993-08, Vol.111 (2‐3), p.287-293 |
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description | The virB operon of the Agrobacterium tumefaciens Ti plasmid encodes 11 proteins. Specific antisera to VirB2, VirB3 and VirB9 were used to locate these virulence proteins in the A. tumefaciens cell. Immunoblot analysis located VirB2 protein to the inner and outer membranes; VirB3 and VirB9 were likewise associated with both membranes, but mainly in the outer membrane. VirB2 is processed from a 12.3‐kDa protein into a 7.2‐kDa polypeptide. Such sized protein results from cleavage at residue Ala47, upstream of which two additional alanine residues Ala45‐Ala46 are contained and bearing resemblance to a signal peptide peptidase‐I cleavage sequence. VirB2 and VirB3 sequences are strikingly similar to the pilin biosynthetic proteins TraA and TraL encoded by the tra operon of F and R1‐19 plasmids. Since traA encodes a propilin that is cleaved into a 7.2‐kDa conjugative pilin product and since this cleavage site is present in both TraA and VirB2, we propose that virB2 encodes a pilin‐like protein which together with VirB3 and VirB9 as well as other VirB proteins may be used for interkingdom T‐DNA transfer between bacteria and plants. |
doi_str_mv | 10.1111/j.1574-6968.1993.tb06400.x |
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Specific antisera to VirB2, VirB3 and VirB9 were used to locate these virulence proteins in the A. tumefaciens cell. Immunoblot analysis located VirB2 protein to the inner and outer membranes; VirB3 and VirB9 were likewise associated with both membranes, but mainly in the outer membrane. VirB2 is processed from a 12.3‐kDa protein into a 7.2‐kDa polypeptide. Such sized protein results from cleavage at residue Ala47, upstream of which two additional alanine residues Ala45‐Ala46 are contained and bearing resemblance to a signal peptide peptidase‐I cleavage sequence. VirB2 and VirB3 sequences are strikingly similar to the pilin biosynthetic proteins TraA and TraL encoded by the tra operon of F and R1‐19 plasmids. Since traA encodes a propilin that is cleaved into a 7.2‐kDa conjugative pilin product and since this cleavage site is present in both TraA and VirB2, we propose that virB2 encodes a pilin‐like protein which together with VirB3 and VirB9 as well as other VirB proteins may be used for interkingdom T‐DNA transfer between bacteria and plants.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1993.tb06400.x</identifier><identifier>PMID: 8405938</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Agrobacterium tumefaciens ; Agrobacterium tumefaciens - genetics ; Agrobacterium tumefaciens - metabolism ; Agrobacterium tumefaciens - pathogenicity ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins - biosynthesis ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Proteins ; Bacteriology ; Biological and medical sciences ; Cell Membrane - metabolism ; Conjugation, Genetic ; Fimbriae Proteins ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Microbiology ; Molecular Sequence Data ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Plasmids ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Ti plasmid ; VirB protein ; Virulence - genetics ; Virulence Factors</subject><ispartof>FEMS microbiology letters, 1993-08, Vol.111 (2‐3), p.287-293</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3987-d9a8c9ec80d105645ea5736d854a7c84a1444e576ddd1bf65902bd10ad62e613</citedby><cites>FETCH-LOGICAL-c3987-d9a8c9ec80d105645ea5736d854a7c84a1444e576ddd1bf65902bd10ad62e613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1993.tb06400.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1993.tb06400.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3769854$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8405938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shirasu, Ken</creatorcontrib><creatorcontrib>Kado, Clarence I.</creatorcontrib><title>Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin‐like conjugative structure on Agrobacterium tumefaciens</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>The virB operon of the Agrobacterium tumefaciens Ti plasmid encodes 11 proteins. Specific antisera to VirB2, VirB3 and VirB9 were used to locate these virulence proteins in the A. tumefaciens cell. Immunoblot analysis located VirB2 protein to the inner and outer membranes; VirB3 and VirB9 were likewise associated with both membranes, but mainly in the outer membrane. VirB2 is processed from a 12.3‐kDa protein into a 7.2‐kDa polypeptide. Such sized protein results from cleavage at residue Ala47, upstream of which two additional alanine residues Ala45‐Ala46 are contained and bearing resemblance to a signal peptide peptidase‐I cleavage sequence. VirB2 and VirB3 sequences are strikingly similar to the pilin biosynthetic proteins TraA and TraL encoded by the tra operon of F and R1‐19 plasmids. Since traA encodes a propilin that is cleaved into a 7.2‐kDa conjugative pilin product and since this cleavage site is present in both TraA and VirB2, we propose that virB2 encodes a pilin‐like protein which together with VirB3 and VirB9 as well as other VirB proteins may be used for interkingdom T‐DNA transfer between bacteria and plants.</description><subject>Agrobacterium tumefaciens</subject><subject>Agrobacterium tumefaciens - genetics</subject><subject>Agrobacterium tumefaciens - metabolism</subject><subject>Agrobacterium tumefaciens - pathogenicity</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Outer Membrane Proteins - biosynthesis</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Conjugation, Genetic</subject><subject>Fimbriae Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Plasmids</subject><subject>Protein Processing, Post-Translational</subject><subject>Sequence Homology, Amino Acid</subject><subject>Ti plasmid</subject><subject>VirB protein</subject><subject>Virulence - genetics</subject><subject>Virulence Factors</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkcuO0zAUhiMEGsrAIyBZCLFLsBvHFxZIw4gBpI7YVGwtxz4ZXJy42EmZ7ngEJN6QJ8GhUfd44yOd79z-vyheEFyR_F7vKtJwWjLJREWkrKuxxYxiXN0_KFbn1MNihWsuSoIlf1w8SWmHMaZrzC6KC0FxI2uxKn7fQt9GPQDywejRhQGFDo1fAW0d2nudemfRFxffoX0MI7ghITccgj-AzcE_sHUhHYccJZfmYo32zrvhz89f3n0DZMKwm-5y6wOgNMbJjFMElOdc3cXQajNCdFOPxqmHThsHQ3paPOq0T_Bs-S-L7c377fXHcvP5w6frq01pail4aaUWRoIR2BLcMNqAbnjNrGio5kZQTSil0HBmrSVtxxqJ121GtWVrYKS-LF6d2ubLvk-QRtW7ZMD7rEaYkuIs61VLnME3J9DEkFKETu2j63U8KoLVbIjaqVl1NauuZkPUYoi6z8XPlylT24M9ly4O5PzLJa-T0b7LXhiXzljNmcwHZeztCfvhPBz_YwF1c7tZC17_BRZ8rEk</recordid><startdate>199308</startdate><enddate>199308</enddate><creator>Shirasu, Ken</creator><creator>Kado, Clarence I.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7X8</scope></search><sort><creationdate>199308</creationdate><title>Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin‐like conjugative structure on Agrobacterium tumefaciens</title><author>Shirasu, Ken ; Kado, Clarence I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3987-d9a8c9ec80d105645ea5736d854a7c84a1444e576ddd1bf65902bd10ad62e613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Agrobacterium tumefaciens</topic><topic>Agrobacterium tumefaciens - genetics</topic><topic>Agrobacterium tumefaciens - metabolism</topic><topic>Agrobacterium tumefaciens - pathogenicity</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Outer Membrane Proteins - biosynthesis</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Proteins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Conjugation, Genetic</topic><topic>Fimbriae Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Plasmids</topic><topic>Protein Processing, Post-Translational</topic><topic>Sequence Homology, Amino Acid</topic><topic>Ti plasmid</topic><topic>VirB protein</topic><topic>Virulence - genetics</topic><topic>Virulence Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shirasu, Ken</creatorcontrib><creatorcontrib>Kado, Clarence I.</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>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shirasu, Ken</au><au>Kado, Clarence I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin‐like conjugative structure on Agrobacterium tumefaciens</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1993-08</date><risdate>1993</risdate><volume>111</volume><issue>2‐3</issue><spage>287</spage><epage>293</epage><pages>287-293</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>The virB operon of the Agrobacterium tumefaciens Ti plasmid encodes 11 proteins. Specific antisera to VirB2, VirB3 and VirB9 were used to locate these virulence proteins in the A. tumefaciens cell. Immunoblot analysis located VirB2 protein to the inner and outer membranes; VirB3 and VirB9 were likewise associated with both membranes, but mainly in the outer membrane. VirB2 is processed from a 12.3‐kDa protein into a 7.2‐kDa polypeptide. Such sized protein results from cleavage at residue Ala47, upstream of which two additional alanine residues Ala45‐Ala46 are contained and bearing resemblance to a signal peptide peptidase‐I cleavage sequence. VirB2 and VirB3 sequences are strikingly similar to the pilin biosynthetic proteins TraA and TraL encoded by the tra operon of F and R1‐19 plasmids. Since traA encodes a propilin that is cleaved into a 7.2‐kDa conjugative pilin product and since this cleavage site is present in both TraA and VirB2, we propose that virB2 encodes a pilin‐like protein which together with VirB3 and VirB9 as well as other VirB proteins may be used for interkingdom T‐DNA transfer between bacteria and plants.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8405938</pmid><doi>10.1111/j.1574-6968.1993.tb06400.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Agrobacterium tumefaciens Agrobacterium tumefaciens - genetics Agrobacterium tumefaciens - metabolism Agrobacterium tumefaciens - pathogenicity Amino Acid Sequence Bacterial Outer Membrane Proteins - biosynthesis Bacterial Outer Membrane Proteins - genetics Bacterial Proteins Bacteriology Biological and medical sciences Cell Membrane - metabolism Conjugation, Genetic Fimbriae Proteins Fundamental and applied biological sciences. Psychology Genes, Bacterial Microbiology Molecular Sequence Data Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Plasmids Protein Processing, Post-Translational Sequence Homology, Amino Acid Ti plasmid VirB protein Virulence - genetics Virulence Factors |
title | Membrane location of the Ti plasmid VirB proteins involved in the biosynthesis of a pilin‐like conjugative structure on Agrobacterium tumefaciens |
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