pubmed-article:7667096 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0805018 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C1442824 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0181586 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:7667096 | lifeskim:mentions | umls-concept:C1627358 | lld:lifeskim |
pubmed-article:7667096 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:7667096 | pubmed:dateCreated | 1995-10-11 | lld:pubmed |
pubmed-article:7667096 | pubmed:abstractText | To assess which residues of Oct-1 POU-specific (POUs) are important for DNA recognition and stimulation of adenovirus DNA replication we have mutated 10 residues of the POUs helix-turn-helix motif implicated in DNA contact. Seven of these turned out to have reduced DNA binding affinity. Of these, three alanine substituted proteins were found to have a changed specificity using a binding site selection procedure. Mutation of the first residue in the recognition helix, Gln44, to alanine led to a loss of specificity for the first two bases, TA, of the wild-type recognition site TATGC(A/T)AAT. Instead of the A, a T was selected, suggesting a new contact and a novel specificity. A change in specificity was also observed for the T45A mutant, which could bind to TATAC(A/T)AAT, a site hardly recognized by the wild-type protein. Mutation of residue Arg49 led to a relaxed specificity for three consecutive bases, TGC. This residue, which is critical for high affinity binding, is absent from the structurally homologous lambdoid helix-turn-helix motifs. Employing a reconstituted system all but two mutants could stimulate adenovirus DNA replication upon saturation. Mutation of residues Gln27 and Arg49 impairs the ability of the Oct-1 POU domain protein to enhance replication, with a concomitant loss of DNA contacts. Since the POU domain binds the precursor terminal protein-DNA polymerase complex and guides it to the origin, lack of stimulation may be caused by incorrect targetting of the DNA polymerase due to loss of specificity. | lld:pubmed |
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pubmed-article:7667096 | pubmed:language | eng | lld:pubmed |
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pubmed-article:7667096 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7667096 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7667096 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7667096 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7667096 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:7667096 | pubmed:author | pubmed-author:van der... | lld:pubmed |
pubmed-article:7667096 | pubmed:author | pubmed-author:KapteinRR | lld:pubmed |
pubmed-article:7667096 | pubmed:author | pubmed-author:CoxMM | lld:pubmed |
pubmed-article:7667096 | pubmed:author | pubmed-author:StratingM JMJ | lld:pubmed |
pubmed-article:7667096 | pubmed:author | pubmed-author:van... | lld:pubmed |
pubmed-article:7667096 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7667096 | pubmed:day | 25 | lld:pubmed |
pubmed-article:7667096 | pubmed:volume | 23 | lld:pubmed |
pubmed-article:7667096 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7667096 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7667096 | pubmed:pagination | 3189-97 | lld:pubmed |
pubmed-article:7667096 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:7667096 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7667096 | pubmed:articleTitle | Mutation of the Oct-1 POU-specific recognition helix leads to altered DNA binding and influences enhancement of adenovirus DNA replication. | lld:pubmed |
pubmed-article:7667096 | pubmed:affiliation | Laboratory for Physiological Chemistry, Utrecht University, Stratenum, The Netherlands. | lld:pubmed |
pubmed-article:7667096 | pubmed:publicationType | Journal Article | lld:pubmed |