pubmed-article:11818337 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11818337 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:11818337 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
pubmed-article:11818337 | lifeskim:mentions | umls-concept:C0597600 | lld:lifeskim |
pubmed-article:11818337 | lifeskim:mentions | umls-concept:C0599944 | lld:lifeskim |
pubmed-article:11818337 | lifeskim:mentions | umls-concept:C0015272 | lld:lifeskim |
pubmed-article:11818337 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:11818337 | pubmed:dateCreated | 2002-3-6 | lld:pubmed |
pubmed-article:11818337 | pubmed:abstractText | In mammals, sequence-specific termination of DNA replication within the ribosomal RNA genes is catalyzed by a defined DNA-protein complex that includes transcription termination factor I (TTF-I). Here we show that TTF-I acts as a polar contrahelicase contrary to the intrinsic 3' -->5' helicase activity of SV40 large T antigen. The contrahelicase activity requires binding of TTF-I to its cognate recognition site and the presence of an auxiliary GC-rich sequence, which is able to form a specific secondary structure. Mutations in the GC-rich sequence lead to a loss of folding into correct secondary structure and abrogate contrahelicase activity. The finding suggests that a specific interaction between the Sal box-bound TTF-I and the GC-rich sequence is essential for the inhibition of T antigen helicase. Analyses of N-terminally truncated mutants of TTF-I showed inhibition of helicase by the same domain of TTF-I, which is also responsible for replication fork arrest. | lld:pubmed |
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pubmed-article:11818337 | pubmed:language | eng | lld:pubmed |
pubmed-article:11818337 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11818337 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11818337 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11818337 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11818337 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11818337 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11818337 | pubmed:issn | 1469-221X | lld:pubmed |
pubmed-article:11818337 | pubmed:author | pubmed-author:PutterVeraV | lld:pubmed |
pubmed-article:11818337 | pubmed:author | pubmed-author:GrummtFriedri... | lld:pubmed |
pubmed-article:11818337 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11818337 | pubmed:volume | 3 | lld:pubmed |
pubmed-article:11818337 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11818337 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11818337 | pubmed:pagination | 147-52 | lld:pubmed |
pubmed-article:11818337 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:11818337 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11818337 | pubmed:articleTitle | Transcription termination factor TTF-I exhibits contrahelicase activity during DNA replication. | lld:pubmed |
pubmed-article:11818337 | pubmed:affiliation | Institute of Biochemistry, University of Würzburg, D-97074 Würzburg, Germany. | lld:pubmed |
pubmed-article:11818337 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11818337 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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