Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. W...
Gespeichert in:
| Veröffentlicht in: | Journal of Bacteriology 1992-11, Vol.174 (21), p.7033-7039 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 7039 |
|---|---|
| container_issue | 21 |
| container_start_page | 7033 |
| container_title | Journal of Bacteriology |
| container_volume | 174 |
| creator | Chang, C.H. (Cornell University, Ithaca, NY) Winans, S.C |
| description | VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. We constructed internal deletions of virA that truncate one or more domains and tested the ability of the resulting proteins to mediate environmentally responsive vir gene activation in vivo. The periplasmic domain is required for sensing of monosaccharides (in agreement with earlier results), while the linker domain is required for sensing of phenolic compounds and acidity. The phosphoryl receiver domain of VirA plays an inhibitory role in signal transduction that may be modulated by phosphorylation. The carboxy terminus of the protein was also dispensable for tumorigenesis, while the periplasmic domain was required |
| doi_str_mv | 10.1128/JB.174.21.7033-7039.1992 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_4444628</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16408929</sourcerecordid><originalsourceid>FETCH-LOGICAL-c602t-756dcdc5db0a81911bf80269effbbbda1b4b35666a6d163fc91232a71601de6b3</originalsourceid><addsrcrecordid>eNpdkU9v1DAQxSMEKkvhCyAhWQhxahaPnTjxgcNSUf6oEgcoV2vsOLteEntrJwW-PV521UJ9GB_e782M_YqCAF0CsPbN53dLaKolg2VDOS9zkUuQkj0oFkBlW9Y1pw-LBaUMSgmSPy6epLSlFKqqZifFCVRZqvmi-HUxezO54HEgMQw2EUzJrb3tyBTItLFkZ6PbDZhGZ87I4PwPG88I-o5Ea6y7sZF0YUTnEwn9X8NqHYNGM2XfPJJpHm2PxtkMfHdxRXYxTNb5p8WjHodknx3v0-Lq4v2384_l5ZcPn85Xl6URlE1lU4vOdKbuNMUWJIDuW8qEtH2vte4QdKV5LYRA0YHgvZHAOMMGBIXOCs1Pi7eHvrtZj7Yz1k8RB7WLbsT4WwV06n_Fu41ahxvFaMPbKvtfH_0xXM82TWp0ydhhQG_DnBSIiraSyQy-vAduwxzzvybFWENr1sg6Q-0BMjGkFG1_uwhQtU9WbbXKySoGap_svki1TzZbX_z7kDvjIcqsvzrqmAwOfURvXLrFqnwEa-_W3Lj15qeLVuVo703N0PMD1GNQuI65z9VXyVlV84b_ATgYwjc</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>227052795</pqid></control><display><type>article</type><title>Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Chang, C.H. (Cornell University, Ithaca, NY) ; Winans, S.C</creator><creatorcontrib>Chang, C.H. (Cornell University, Ithaca, NY) ; Winans, S.C</creatorcontrib><description>VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. We constructed internal deletions of virA that truncate one or more domains and tested the ability of the resulting proteins to mediate environmentally responsive vir gene activation in vivo. The periplasmic domain is required for sensing of monosaccharides (in agreement with earlier results), while the linker domain is required for sensing of phenolic compounds and acidity. The phosphoryl receiver domain of VirA plays an inhibitory role in signal transduction that may be modulated by phosphorylation. The carboxy terminus of the protein was also dispensable for tumorigenesis, while the periplasmic domain was required</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/JB.174.21.7033-7039.1992</identifier><identifier>PMID: 1400253</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>AGROBACTERIUM TUMEFACIENS ; Agrobacterium tumefaciens - genetics ; Agrobacterium tumefaciens - pathogenicity ; Alleles ; Aspartic Acid ; Bacteria ; Bacterial Proteins - genetics ; Bacteriology ; Base Sequence ; Biological and medical sciences ; COMPOSE PHENOLIQUE ; COMPUESTOS FENOLICOS ; DNA Mutational Analysis ; DNA-Binding Proteins ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. Psychology ; Genetics ; Membrane Transport Proteins ; Microbiology ; Molecular Sequence Data ; MONOSACARIDOS ; MONOSACCHARIDE ; Mutagenesis ; Periplasmic Binding Proteins ; Plants - microbiology ; Protein Structure, Tertiary ; PROTEINAS ; PROTEINE ; Proteins ; Signal Transduction - genetics ; Transcription Factors ; Virulence ; Virulence Factors</subject><ispartof>Journal of Bacteriology, 1992-11, Vol.174 (21), p.7033-7039</ispartof><rights>1993 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Nov 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-756dcdc5db0a81911bf80269effbbbda1b4b35666a6d163fc91232a71601de6b3</citedby><cites>FETCH-LOGICAL-c602t-756dcdc5db0a81911bf80269effbbbda1b4b35666a6d163fc91232a71601de6b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC207384/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC207384/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4444628$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1400253$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chang, C.H. (Cornell University, Ithaca, NY)</creatorcontrib><creatorcontrib>Winans, S.C</creatorcontrib><title>Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. We constructed internal deletions of virA that truncate one or more domains and tested the ability of the resulting proteins to mediate environmentally responsive vir gene activation in vivo. The periplasmic domain is required for sensing of monosaccharides (in agreement with earlier results), while the linker domain is required for sensing of phenolic compounds and acidity. The phosphoryl receiver domain of VirA plays an inhibitory role in signal transduction that may be modulated by phosphorylation. The carboxy terminus of the protein was also dispensable for tumorigenesis, while the periplasmic domain was required</description><subject>AGROBACTERIUM TUMEFACIENS</subject><subject>Agrobacterium tumefaciens - genetics</subject><subject>Agrobacterium tumefaciens - pathogenicity</subject><subject>Alleles</subject><subject>Aspartic Acid</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>COMPOSE PHENOLIQUE</subject><subject>COMPUESTOS FENOLICOS</subject><subject>DNA Mutational Analysis</subject><subject>DNA-Binding Proteins</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>Membrane Transport Proteins</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>MONOSACARIDOS</subject><subject>MONOSACCHARIDE</subject><subject>Mutagenesis</subject><subject>Periplasmic Binding Proteins</subject><subject>Plants - microbiology</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Proteins</subject><subject>Signal Transduction - genetics</subject><subject>Transcription Factors</subject><subject>Virulence</subject><subject>Virulence Factors</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU9v1DAQxSMEKkvhCyAhWQhxahaPnTjxgcNSUf6oEgcoV2vsOLteEntrJwW-PV521UJ9GB_e782M_YqCAF0CsPbN53dLaKolg2VDOS9zkUuQkj0oFkBlW9Y1pw-LBaUMSgmSPy6epLSlFKqqZifFCVRZqvmi-HUxezO54HEgMQw2EUzJrb3tyBTItLFkZ6PbDZhGZ87I4PwPG88I-o5Ea6y7sZF0YUTnEwn9X8NqHYNGM2XfPJJpHm2PxtkMfHdxRXYxTNb5p8WjHodknx3v0-Lq4v2384_l5ZcPn85Xl6URlE1lU4vOdKbuNMUWJIDuW8qEtH2vte4QdKV5LYRA0YHgvZHAOMMGBIXOCs1Pi7eHvrtZj7Yz1k8RB7WLbsT4WwV06n_Fu41ahxvFaMPbKvtfH_0xXM82TWp0ydhhQG_DnBSIiraSyQy-vAduwxzzvybFWENr1sg6Q-0BMjGkFG1_uwhQtU9WbbXKySoGap_svki1TzZbX_z7kDvjIcqsvzrqmAwOfURvXLrFqnwEa-_W3Lj15qeLVuVo703N0PMD1GNQuI65z9VXyVlV84b_ATgYwjc</recordid><startdate>19921101</startdate><enddate>19921101</enddate><creator>Chang, C.H. (Cornell University, Ithaca, NY)</creator><creator>Winans, S.C</creator><general>American Society for Microbiology</general><scope>FBQ</scope><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>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19921101</creationdate><title>Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein</title><author>Chang, C.H. (Cornell University, Ithaca, NY) ; Winans, S.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-756dcdc5db0a81911bf80269effbbbda1b4b35666a6d163fc91232a71601de6b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>AGROBACTERIUM TUMEFACIENS</topic><topic>Agrobacterium tumefaciens - genetics</topic><topic>Agrobacterium tumefaciens - pathogenicity</topic><topic>Alleles</topic><topic>Aspartic Acid</topic><topic>Bacteria</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>COMPOSE PHENOLIQUE</topic><topic>COMPUESTOS FENOLICOS</topic><topic>DNA Mutational Analysis</topic><topic>DNA-Binding Proteins</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics</topic><topic>Membrane Transport Proteins</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>MONOSACARIDOS</topic><topic>MONOSACCHARIDE</topic><topic>Mutagenesis</topic><topic>Periplasmic Binding Proteins</topic><topic>Plants - microbiology</topic><topic>Protein Structure, Tertiary</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Proteins</topic><topic>Signal Transduction - genetics</topic><topic>Transcription Factors</topic><topic>Virulence</topic><topic>Virulence Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chang, C.H. (Cornell University, Ithaca, NY)</creatorcontrib><creatorcontrib>Winans, S.C</creatorcontrib><collection>AGRIS</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chang, C.H. (Cornell University, Ithaca, NY)</au><au>Winans, S.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>1992-11-01</date><risdate>1992</risdate><volume>174</volume><issue>21</issue><spage>7033</spage><epage>7039</epage><pages>7033-7039</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>VirA and VirG activate the Agrobacterium tumefaciens vir regulon in response to phenolic compounds, monosaccharides, and acidity released from plant wound sites. VirA contains an amino-terminal periplasmic domain and three cytoplasmic domains: a linker, a protein kinase, and a phosphoryl receiver. We constructed internal deletions of virA that truncate one or more domains and tested the ability of the resulting proteins to mediate environmentally responsive vir gene activation in vivo. The periplasmic domain is required for sensing of monosaccharides (in agreement with earlier results), while the linker domain is required for sensing of phenolic compounds and acidity. The phosphoryl receiver domain of VirA plays an inhibitory role in signal transduction that may be modulated by phosphorylation. The carboxy terminus of the protein was also dispensable for tumorigenesis, while the periplasmic domain was required</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>1400253</pmid><doi>10.1128/JB.174.21.7033-7039.1992</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9193 |
| ispartof | Journal of Bacteriology, 1992-11, Vol.174 (21), p.7033-7039 |
| issn | 0021-9193 1098-5530 1067-8832 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_4444628 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | AGROBACTERIUM TUMEFACIENS Agrobacterium tumefaciens - genetics Agrobacterium tumefaciens - pathogenicity Alleles Aspartic Acid Bacteria Bacterial Proteins - genetics Bacteriology Base Sequence Biological and medical sciences COMPOSE PHENOLIQUE COMPUESTOS FENOLICOS DNA Mutational Analysis DNA-Binding Proteins EXPRESION GENICA EXPRESSION DES GENES Fundamental and applied biological sciences. Psychology Genetics Membrane Transport Proteins Microbiology Molecular Sequence Data MONOSACARIDOS MONOSACCHARIDE Mutagenesis Periplasmic Binding Proteins Plants - microbiology Protein Structure, Tertiary PROTEINAS PROTEINE Proteins Signal Transduction - genetics Transcription Factors Virulence Virulence Factors |
| title | Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T19%3A54%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20roles%20assigned%20to%20the%20periplasmic,%20linker,%20and%20receiver%20domains%20of%20the%20Agrobacterium%20tumefaciens%20VirA%20protein&rft.jtitle=Journal%20of%20Bacteriology&rft.au=Chang,%20C.H.%20(Cornell%20University,%20Ithaca,%20NY)&rft.date=1992-11-01&rft.volume=174&rft.issue=21&rft.spage=7033&rft.epage=7039&rft.pages=7033-7039&rft.issn=0021-9193&rft.eissn=1098-5530&rft.coden=JOBAAY&rft_id=info:doi/10.1128/JB.174.21.7033-7039.1992&rft_dat=%3Cproquest_pasca%3E16408929%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=227052795&rft_id=info:pmid/1400253&rfr_iscdi=true |