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http://purl.uniprot.org/citations/15292447http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15292447http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15292447http://www.w3.org/2000/01/rdf-schema#comment"The transcription termination factor (TTF)-I is a multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. TTF-I plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. The N-terminal part of TTF-I contains a negative regulatory domain (NRD) that inhibits DNA binding. Here we show that interactions between the NRD and the C-terminal part of TTF-I mask the DNA-binding domain of TTF-I. However, interaction with TIP5, a subunit of the nucleolar chromatin remodeling complex, NoRC, recovers DNA-binding activity. We have mapped the protein domains that mediate the interaction between TTF-I and TIP5. The association of TIP5 with the NRD facilitates DNA binding of TTF-I and leads to the recruitment of NoRC to the rDNA promoter. Thus, TTF-I and NoRC act in concert to silence rDNA transcription."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh732"xsd:string
http://purl.uniprot.org/citations/15292447http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkh732"xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Nemeth A."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Nemeth A."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Grummt I."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Grummt I."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Laengst G."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Laengst G."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Strohner R."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/author"Strohner R."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/pages"4091-4099"xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/pages"4091-4099"xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/title"The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/title"The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo."xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/15292447http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/15292447http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15292447
http://purl.uniprot.org/citations/15292447http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15292447