VirD2 protein of Agrobacterium tumefaciens very tightly linked to the 5' end of T-strand DNA
The T-strand, a probable intermediate of Agrobacterium plant transformation, is bound by a nondenaturable linkage to a protein moiety at its 5' end. The protein is shown to be the polypeptide VirD2, previously identified as a component of the T-DNA border endonuclease that initiates T-strand pr...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1988-11, Vol.242 (4880), p.927-930 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Ward, E.R Barnes, W.M |
| description | The T-strand, a probable intermediate of Agrobacterium plant transformation, is bound by a nondenaturable linkage to a protein moiety at its 5' end. The protein is shown to be the polypeptide VirD2, previously identified as a component of the T-DNA border endonuclease that initiates T-strand production. T-strands from an Agrobacterium strain expressing a virD2-lacZ fusion are bound to a protein of larger size than the wild-type protein and are immunoprecipitable by antibody to beta-galactosidase |
| doi_str_mv | 10.1126/science.242.4880.927 |
| format | Article |
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The protein is shown to be the polypeptide VirD2, previously identified as a component of the T-DNA border endonuclease that initiates T-strand production. T-strands from an Agrobacterium strain expressing a virD2-lacZ fusion are bound to a protein of larger size than the wild-type protein and are immunoprecipitable by antibody to beta-galactosidase</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.242.4880.927</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: The American Association for the Advancement of Science</publisher><subject>ADN ; AGALLAS ; AGROBACTERIUM ; Agrobacterium tumefaciens ; Antibodies ; Bacterial plant pathogens ; Bacteriology ; Biochemistry ; Biological and medical sciences ; Crown gall disease ; DNA ; DNA binding proteins ; DNA probes ; Fundamental and applied biological sciences. Psychology ; GALLE ; Gels ; Genetic aspects ; Genetics ; GENOMAS ; GENOME ; Microbiology ; Oligonucleotide probes ; Phenols ; Phytopathology. Animal pests. Plant and forest protection ; Plant cells ; Plant tumor inducing plasmids ; Plasmids ; PROTEINAS ; PROTEINE ; Proteins ; Systematics. Structure, properties and multiplication. 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The protein is shown to be the polypeptide VirD2, previously identified as a component of the T-DNA border endonuclease that initiates T-strand production. T-strands from an Agrobacterium strain expressing a virD2-lacZ fusion are bound to a protein of larger size than the wild-type protein and are immunoprecipitable by antibody to beta-galactosidase</description><subject>ADN</subject><subject>AGALLAS</subject><subject>AGROBACTERIUM</subject><subject>Agrobacterium tumefaciens</subject><subject>Antibodies</subject><subject>Bacterial plant pathogens</subject><subject>Bacteriology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Crown gall disease</subject><subject>DNA</subject><subject>DNA binding proteins</subject><subject>DNA probes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GALLE</subject><subject>Gels</subject><subject>Genetic aspects</subject><subject>Genetics</subject><subject>GENOMAS</subject><subject>GENOME</subject><subject>Microbiology</subject><subject>Oligonucleotide probes</subject><subject>Phenols</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Plant cells</subject><subject>Plant tumor inducing plasmids</subject><subject>Plasmids</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Proteins</subject><subject>Systematics. Structure, properties and multiplication. 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Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1988-11-11</date><risdate>1988</risdate><volume>242</volume><issue>4880</issue><spage>927</spage><epage>930</epage><pages>927-930</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The T-strand, a probable intermediate of Agrobacterium plant transformation, is bound by a nondenaturable linkage to a protein moiety at its 5' end. The protein is shown to be the polypeptide VirD2, previously identified as a component of the T-DNA border endonuclease that initiates T-strand production. T-strands from an Agrobacterium strain expressing a virD2-lacZ fusion are bound to a protein of larger size than the wild-type protein and are immunoprecipitable by antibody to beta-galactosidase</abstract><cop>Washington, DC</cop><pub>The American Association for the Advancement of Science</pub><doi>10.1126/science.242.4880.927</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1988-11, Vol.242 (4880), p.927-930 |
| issn | 0036-8075 1095-9203 |
| language | eng |
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| source | JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | ADN AGALLAS AGROBACTERIUM Agrobacterium tumefaciens Antibodies Bacterial plant pathogens Bacteriology Biochemistry Biological and medical sciences Crown gall disease DNA DNA binding proteins DNA probes Fundamental and applied biological sciences. Psychology GALLE Gels Genetic aspects Genetics GENOMAS GENOME Microbiology Oligonucleotide probes Phenols Phytopathology. Animal pests. Plant and forest protection Plant cells Plant tumor inducing plasmids Plasmids PROTEINAS PROTEINE Proteins Systematics. Structure, properties and multiplication. Genetics |
| title | VirD2 protein of Agrobacterium tumefaciens very tightly linked to the 5' end of T-strand DNA |
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