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dc.contributor.authorSouthgate, Christopher D.
dc.contributor.authorGreen, Michael R.
dc.date2022-08-11T08:09:34.000
dc.date.accessioned2022-08-23T16:36:02Z
dc.date.available2022-08-23T16:36:02Z
dc.date.issued1995-04-01
dc.date.submitted2009-03-26
dc.identifier.citationJ Virol. 1995 Apr;69(4):2605-10.
dc.identifier.issn0022-538X (Print)
dc.identifier.pmid7884911
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38696
dc.description.abstractLentivirus Tat proteins comprise a novel class of RNA-binding transcriptional activators that are essential for viral replication. In this study, we performed a series of protein fusion experiments to delineate the minimal protein domains and promoter elements required for Tat action. We show that a 15-amino-acid region of equine infectious anemia virus (EIAV) Tat protein, when fused to the GAL4 or LexA DNA binding domain, can activate transcription in appropriate promoter contexts. In the natural human immunodeficiency virus type 1 long terminal repeat, activation by Tat is dependent on multiple binding sites for the cellular transcription factor SP1. We delineate a 114-amino-acid region of the SP1 glutamine-rich activation domain that when fused to the GAL4 DNA binding domain can support transcription activation by Tat. Using these Tat and SP1 derivatives, we show that Tat activation can be reconstructed on a completely synthetic promoter lacking all cis-acting elements unique to the human immunodeficiency virus long terminal repeat. Our results indicate that lentivirus Tat proteins have essential properties of typical cellular transcriptional activators and define useful reagents for studying the detailed mechanism of Tat action.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7884911&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAnimals
dc.subjectCricetinae
dc.subjectFungal Proteins
dc.subjectGene Products, tat
dc.subjectHIV Long Terminal Repeat
dc.subjectHIV-1
dc.subjectHela Cells
dc.subjectHumans
dc.subjectInfectious Anemia Virus, Equine
dc.subjectLentivirus
dc.subject*Promoter Regions (Genetics)
dc.subject*Saccharomyces cerevisiae Proteins
dc.subject*Trans-Activation (Genetics)
dc.subjectTranscription Factors
dc.subjecttat Gene Products, Human Immunodeficiency Virus
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleDelineating minimal protein domains and promoter elements for transcriptional activation by lentivirus Tat proteins
dc.typeJournal Article
dc.source.journaltitleJournal of virology
dc.source.volume69
dc.source.issue4
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2549&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1550
dc.identifier.contextkey798527
refterms.dateFOA2022-08-23T16:36:02Z
html.description.abstract<p>Lentivirus Tat proteins comprise a novel class of RNA-binding transcriptional activators that are essential for viral replication. In this study, we performed a series of protein fusion experiments to delineate the minimal protein domains and promoter elements required for Tat action. We show that a 15-amino-acid region of equine infectious anemia virus (EIAV) Tat protein, when fused to the GAL4 or LexA DNA binding domain, can activate transcription in appropriate promoter contexts. In the natural human immunodeficiency virus type 1 long terminal repeat, activation by Tat is dependent on multiple binding sites for the cellular transcription factor SP1. We delineate a 114-amino-acid region of the SP1 glutamine-rich activation domain that when fused to the GAL4 DNA binding domain can support transcription activation by Tat. Using these Tat and SP1 derivatives, we show that Tat activation can be reconstructed on a completely synthetic promoter lacking all cis-acting elements unique to the human immunodeficiency virus long terminal repeat. Our results indicate that lentivirus Tat proteins have essential properties of typical cellular transcriptional activators and define useful reagents for studying the detailed mechanism of Tat action.</p>
dc.identifier.submissionpathoapubs/1550
dc.contributor.departmentProgram in Gene Function and Expression
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentHoward Hughes Medical Institute
dc.source.pages2605-10


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