Induction of a subnuclear structure by the simultaneous expression of baculovirus proteins, IE1, LEF3, and P143 in the presence of hr
Baculoviruses elicit the formation of a nuclear domain, called the virogenic stroma, in which viral DNA replication and nucleocapsid assembly occur. We had previously reported that nuclear focus formation of a transcriptional activator, IE1, is triggered by its binding to a viral DNA element, hr, an...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2006-09, Vol.352 (2), p.400-407 |
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| creator | Nagamine, Toshihiro Kawasaki, Yu Matsumoto, Shogo |
| description | Baculoviruses elicit the formation of a nuclear domain, called the virogenic stroma, in which viral DNA replication and nucleocapsid assembly occur. We had previously reported that nuclear focus formation of a transcriptional activator, IE1, is triggered by its binding to a viral DNA element,
hr, and predicted that this
hr-induced IE1 focus is an initial scaffold for the virogenic stroma. However, LEF3, a component of the virogenic stroma, did not localize to the IE1 foci. In exploring a mediator for its localization, we found that a baculovirus DNA helicase (P143), in combination with IE1 and
hr, induced a subnuclear structure to which LEF3 localized and also that another component of the virogenic stroma, DBP, is able to localize to this structure. These results reveal that only four viral molecules are necessary to establish a nuclear domain which possesses a recruiting ability for a component of the virogenic stroma. |
| doi_str_mv | 10.1016/j.virol.2006.04.034 |
| format | Article |
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hr, and predicted that this
hr-induced IE1 focus is an initial scaffold for the virogenic stroma. However, LEF3, a component of the virogenic stroma, did not localize to the IE1 foci. In exploring a mediator for its localization, we found that a baculovirus DNA helicase (P143), in combination with IE1 and
hr, induced a subnuclear structure to which LEF3 localized and also that another component of the virogenic stroma, DBP, is able to localize to this structure. These results reveal that only four viral molecules are necessary to establish a nuclear domain which possesses a recruiting ability for a component of the virogenic stroma.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2006.04.034</identifier><identifier>PMID: 16780915</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Baculovirus ; Base Sequence ; BmNPV ; Bombyx ; Bombyx mori ; Bombyx mori nucleopolyhedrovirus ; Cell Line ; Cell Nucleus - virology ; DBP ; DNA helicases ; DNA, Viral - genetics ; DNA, Viral - metabolism ; DNA-binding proteins ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - physiology ; Genes, Viral ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; IE1/LEF3/P143-associated structure ; Immediate-Early Proteins - genetics ; Immediate-Early Proteins - physiology ; Nuclear structure ; Nucleopolyhedrovirus - genetics ; Nucleopolyhedrovirus - pathogenicity ; Nucleopolyhedrovirus - physiology ; Plasmids - genetics ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Replication compartment ; Trans-Activators - genetics ; Trans-Activators - physiology ; transcription factors ; Transfection ; viral proteins ; Viral Proteins - genetics ; Viral Proteins - physiology ; Virogenic stroma</subject><ispartof>Virology (New York, N.Y.), 2006-09, Vol.352 (2), p.400-407</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-d2bf3ec6b68e827a37eafb2353dda8796bde080bbeb6df53d601b1465c0ddec3</citedby><cites>FETCH-LOGICAL-c523t-d2bf3ec6b68e827a37eafb2353dda8796bde080bbeb6df53d601b1465c0ddec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2006.04.034$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16780915$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagamine, Toshihiro</creatorcontrib><creatorcontrib>Kawasaki, Yu</creatorcontrib><creatorcontrib>Matsumoto, Shogo</creatorcontrib><title>Induction of a subnuclear structure by the simultaneous expression of baculovirus proteins, IE1, LEF3, and P143 in the presence of hr</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Baculoviruses elicit the formation of a nuclear domain, called the virogenic stroma, in which viral DNA replication and nucleocapsid assembly occur. We had previously reported that nuclear focus formation of a transcriptional activator, IE1, is triggered by its binding to a viral DNA element,
hr, and predicted that this
hr-induced IE1 focus is an initial scaffold for the virogenic stroma. However, LEF3, a component of the virogenic stroma, did not localize to the IE1 foci. In exploring a mediator for its localization, we found that a baculovirus DNA helicase (P143), in combination with IE1 and
hr, induced a subnuclear structure to which LEF3 localized and also that another component of the virogenic stroma, DBP, is able to localize to this structure. These results reveal that only four viral molecules are necessary to establish a nuclear domain which possesses a recruiting ability for a component of the virogenic stroma.</description><subject>Animals</subject><subject>Baculovirus</subject><subject>Base Sequence</subject><subject>BmNPV</subject><subject>Bombyx</subject><subject>Bombyx mori</subject><subject>Bombyx mori nucleopolyhedrovirus</subject><subject>Cell Line</subject><subject>Cell Nucleus - virology</subject><subject>DBP</subject><subject>DNA helicases</subject><subject>DNA, Viral - genetics</subject><subject>DNA, Viral - metabolism</subject><subject>DNA-binding proteins</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - physiology</subject><subject>Genes, Viral</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>IE1/LEF3/P143-associated structure</subject><subject>Immediate-Early Proteins - genetics</subject><subject>Immediate-Early Proteins - physiology</subject><subject>Nuclear structure</subject><subject>Nucleopolyhedrovirus - genetics</subject><subject>Nucleopolyhedrovirus - pathogenicity</subject><subject>Nucleopolyhedrovirus - physiology</subject><subject>Plasmids - genetics</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Replication compartment</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - physiology</subject><subject>transcription factors</subject><subject>Transfection</subject><subject>viral proteins</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - physiology</subject><subject>Virogenic stroma</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUc1u1DAYtBAVXQpPgAQ-cdqEz3FiJwcOqNrCSiu1EuVs-ecL9SqbLHZS0QfgvXE2K3GjJ_98M-PxDCHvGOQMmPi0zx99GLq8ABA5lDnw8gVZMWhElrbsJVkBlEUm6qK4JK9j3EM6SwmvyCUTsoaGVSvyZ9u7yY5-6OnQUk3jZPrJdqgDjWNIkykgNU90fEAa_WHqRt3jMEWKv48BYzwTjbZTNyQ_aXIMw4i-j2u63bA13W1u-Jrq3tE7VnLq-5PWTMbe4kx-CG_IRau7iG_P6xW5v9ncX3_Ldrdft9dfdpmtCj5mrjAtRyuMqLEupOYSdWsKXnHndC0bYRxCDcagEa5NtwKYYaWoLDiHll-Rj4tssvhrwjiqg48Wu275kxK1FKxsqmeBrEkBV5IlIF-ANgwxBmzVMfiDDk-KgZpbUnt1aknNLSkoVaomsd6f5SdzQPePc64lAT4sgFYPSv8MPqof3wtgHEDWjJ8e_rwgMMX16DGoaP0cqPMB7ajc4P9r4S88aq8H</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Nagamine, Toshihiro</creator><creator>Kawasaki, Yu</creator><creator>Matsumoto, Shogo</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20060901</creationdate><title>Induction of a subnuclear structure by the simultaneous expression of baculovirus proteins, IE1, LEF3, and P143 in the presence of hr</title><author>Nagamine, Toshihiro ; Kawasaki, Yu ; Matsumoto, Shogo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-d2bf3ec6b68e827a37eafb2353dda8796bde080bbeb6df53d601b1465c0ddec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Baculovirus</topic><topic>Base Sequence</topic><topic>BmNPV</topic><topic>Bombyx</topic><topic>Bombyx mori</topic><topic>Bombyx mori nucleopolyhedrovirus</topic><topic>Cell Line</topic><topic>Cell Nucleus - virology</topic><topic>DBP</topic><topic>DNA helicases</topic><topic>DNA, Viral - genetics</topic><topic>DNA, Viral - metabolism</topic><topic>DNA-binding proteins</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - physiology</topic><topic>Genes, Viral</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>IE1/LEF3/P143-associated structure</topic><topic>Immediate-Early Proteins - genetics</topic><topic>Immediate-Early Proteins - physiology</topic><topic>Nuclear structure</topic><topic>Nucleopolyhedrovirus - genetics</topic><topic>Nucleopolyhedrovirus - pathogenicity</topic><topic>Nucleopolyhedrovirus - physiology</topic><topic>Plasmids - genetics</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Replication compartment</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - physiology</topic><topic>transcription factors</topic><topic>Transfection</topic><topic>viral proteins</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - physiology</topic><topic>Virogenic stroma</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagamine, Toshihiro</creatorcontrib><creatorcontrib>Kawasaki, Yu</creatorcontrib><creatorcontrib>Matsumoto, Shogo</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagamine, Toshihiro</au><au>Kawasaki, Yu</au><au>Matsumoto, Shogo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Induction of a subnuclear structure by the simultaneous expression of baculovirus proteins, IE1, LEF3, and P143 in the presence of hr</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>352</volume><issue>2</issue><spage>400</spage><epage>407</epage><pages>400-407</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Baculoviruses elicit the formation of a nuclear domain, called the virogenic stroma, in which viral DNA replication and nucleocapsid assembly occur. We had previously reported that nuclear focus formation of a transcriptional activator, IE1, is triggered by its binding to a viral DNA element,
hr, and predicted that this
hr-induced IE1 focus is an initial scaffold for the virogenic stroma. However, LEF3, a component of the virogenic stroma, did not localize to the IE1 foci. In exploring a mediator for its localization, we found that a baculovirus DNA helicase (P143), in combination with IE1 and
hr, induced a subnuclear structure to which LEF3 localized and also that another component of the virogenic stroma, DBP, is able to localize to this structure. These results reveal that only four viral molecules are necessary to establish a nuclear domain which possesses a recruiting ability for a component of the virogenic stroma.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16780915</pmid><doi>10.1016/j.virol.2006.04.034</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Baculovirus Base Sequence BmNPV Bombyx Bombyx mori Bombyx mori nucleopolyhedrovirus Cell Line Cell Nucleus - virology DBP DNA helicases DNA, Viral - genetics DNA, Viral - metabolism DNA-binding proteins DNA-Binding Proteins - genetics DNA-Binding Proteins - physiology Genes, Viral Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism IE1/LEF3/P143-associated structure Immediate-Early Proteins - genetics Immediate-Early Proteins - physiology Nuclear structure Nucleopolyhedrovirus - genetics Nucleopolyhedrovirus - pathogenicity Nucleopolyhedrovirus - physiology Plasmids - genetics Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Replication compartment Trans-Activators - genetics Trans-Activators - physiology transcription factors Transfection viral proteins Viral Proteins - genetics Viral Proteins - physiology Virogenic stroma |
| title | Induction of a subnuclear structure by the simultaneous expression of baculovirus proteins, IE1, LEF3, and P143 in the presence of hr |
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