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dc.contributor.authorPersengiev, Stephan P.
dc.contributor.authorZhu, Xiaochun
dc.contributor.authorDixit, Bharat L.
dc.contributor.authorMaston, Glenn A.
dc.contributor.authorKittler, Ellen L. W.
dc.contributor.authorGreen, Michael R.
dc.date2022-08-11T08:09:36.000
dc.date.accessioned2022-08-23T16:37:05Z
dc.date.available2022-08-23T16:37:05Z
dc.date.issued2003-11-25
dc.date.submitted2009-04-02
dc.identifier.citation<p>Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14887-91. Epub 2003 Nov 21. <a href="http://dx.doi.org/10.1073/pnas.2036440100">Link to article on publisher's site</a></p>
dc.identifier.issn0027-8424 (Print)
dc.identifier.doi10.1073/pnas.2036440100
dc.identifier.pmid14634207
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38934
dc.description.abstractTATA-box-binding protein (TBP) is a highly conserved RNA polymerase II general transcription factor that binds to the core promoter and initiates assembly of the preinitiation complex. Two proteins with high homology to TBP have been found: TBP-related factor 1 (TRF1), described only in Drosophila melanogaster, and TRF2, which is broadly distributed in metazoans. Here, we report the identification and characterization of an additional TBP-related factor, TRF3. TRF3 is virtually identical to TBP in the C-terminal core domain, including all residues involved in DNA binding and interaction with other general transcription factors. Like other TBP family members, the N-terminal region of TRF3 is divergent. The TRF3 gene is present and expressed in vertebrates, from fish through humans, but absent from the genomes of the urochordate Ciona intestinalis and the lower eukaryotes D. melanogaster and Caenorhabditis elegans. TRF3 is a nuclear protein that is present in all human and mouse tissues and cell lines examined. Despite the highly homologous TBP-like C-terminal core domain, gel filtration analysis indicates that the native molecular weight of TRF3 is substantially less than that of TFIID. Interestingly, after mitosis, reimport of TRF3 into the nucleus occurs subsequent to TBP and other basal transcription factors. In summary, TRF3 is a highly conserved vertebrate-specific TRF whose phylogenetic conservation, expression pattern, and other properties are distinct from those of TBP and all other TRFs.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=14634207&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC299843/
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCaenorhabditis elegans
dc.subjectCell Line
dc.subjectCell Nucleus
dc.subjectChromatography, Gel
dc.subjectCiona intestinalis
dc.subjectComputational Biology
dc.subjectDNA
dc.subjectDrosophila melanogaster
dc.subjectFluorescent Antibody Technique, Indirect
dc.subjectHela Cells
dc.subjectHumans
dc.subjectMice
dc.subjectMitosis
dc.subjectMolecular Sequence Data
dc.subjectNuclear Proteins
dc.subjectPhylogeny
dc.subjectProtein Biosynthesis
dc.subjectProtein Structure, Tertiary
dc.subjectRNA Polymerase II
dc.subjectReverse Transcriptase Polymerase Chain Reaction
dc.subjectSequence Homology, Amino Acid
dc.subjectTATA Box Binding Protein-Like Proteins
dc.subjectTissue Distribution
dc.subjectTranscription Factor TFIID
dc.subjectTranscription Factors
dc.subjectTranscription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleTRF3, a TATA-box-binding protein-related factor, is vertebrate-specific and widely expressed
dc.typeJournal Article
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume100
dc.source.issue25
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1765
dc.identifier.contextkey808530
html.description.abstract<p>TATA-box-binding protein (TBP) is a highly conserved RNA polymerase II general transcription factor that binds to the core promoter and initiates assembly of the preinitiation complex. Two proteins with high homology to TBP have been found: TBP-related factor 1 (TRF1), described only in Drosophila melanogaster, and TRF2, which is broadly distributed in metazoans. Here, we report the identification and characterization of an additional TBP-related factor, TRF3. TRF3 is virtually identical to TBP in the C-terminal core domain, including all residues involved in DNA binding and interaction with other general transcription factors. Like other TBP family members, the N-terminal region of TRF3 is divergent. The TRF3 gene is present and expressed in vertebrates, from fish through humans, but absent from the genomes of the urochordate Ciona intestinalis and the lower eukaryotes D. melanogaster and Caenorhabditis elegans. TRF3 is a nuclear protein that is present in all human and mouse tissues and cell lines examined. Despite the highly homologous TBP-like C-terminal core domain, gel filtration analysis indicates that the native molecular weight of TRF3 is substantially less than that of TFIID. Interestingly, after mitosis, reimport of TRF3 into the nucleus occurs subsequent to TBP and other basal transcription factors. In summary, TRF3 is a highly conserved vertebrate-specific TRF whose phylogenetic conservation, expression pattern, and other properties are distinct from those of TBP and all other TRFs.</p>
dc.identifier.submissionpathoapubs/1765
dc.contributor.departmentProgram in Gene Function and Expression
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentHoward Hughes Medical Institute
dc.source.pages14887-91


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