| pubmed-article:12134028 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C1564874 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C2753500 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C1413292 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C1423526 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C0525037 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:12134028 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:12134028 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:12134028 | pubmed:dateCreated | 2002-7-22 | lld:pubmed |
| pubmed-article:12134028 | pubmed:abstractText | During adeno-associated virus (AAV) type 2 productive infections, the p19 promoter of AAV is activated by the AAV Rep78 and Rep68 proteins. Rep-induced activation of p19 depends on the presence of one of several redundant Rep binding elements (RBEs) within the p5 promoter or within the terminal repeats (TR). In the absence of the TR, the p5 RBE and the p19 Sp1 site at position -50 are essential for p19 transactivation. To determine how a Rep complex bound at p5 induces transcription at p19, we made a series of p19 promoter chloramphenicol acetyltransferase constructs in which the p5 RBE was inserted at different locations upstream or downstream of the p19 mRNA start site. The RBE acted like a repressor element at most positions in the presence of both Rep and adenovirus (Ad), and the level of repression increased dramatically as the RBE was inserted closer to the p19 promoter. We concluded that the RBE by itself was not a conventional upstream activation signal and instead behaved like a repressor. To understand how the Rep-RBE complex within p5 activated p19, we considered the possibility that its role was to function as an architectural protein whose purpose was to bring other p5 transcriptional elements to the p19 promoter. In order to address this possibility, we replaced both the p5 RBE and the p19 Sp1 site with GAL4 binding sites. The modified GAL4-containing constructs were cotransfected with plasmids that expressed GAL4 fusion proteins capable of interacting through p53 and T-antigen (T-ag) protein domains. In the presence of Ad and the GAL4 fusion proteins, the p19 promoter exhibited strong transcriptional activation that was dependent on both the GAL4 fusion proteins and Ad infection. This suggested that the primary role of the p5 RBE and the p19 Sp1 sites was to act as a scaffold for bringing transcription complexes in the p5 promoter into close proximity with the p19 promoter. Since Rep and Sp1 themselves were not essential for transactivation, we tested mutants within the other p5 transcriptional elements in the context of GAL4-induced looping to determine which of the other p5 elements was necessary for p19 induction. Mutation of the p5 major late-transcription factor site reduced p19 activity but did not eliminate induction in the presence of the GAL4 fusion proteins. However, mutation of the p5 YY1 site at position -60 (YY1-60) eliminated GAL4-induced transactivation. This implicated the YY1-60 protein complexes in p19 induction by Rep. In addition, both basal p19 activity and activity in the presence of Ad increased when the YY1-60 site was mutated even in the absence of Rep or GAL4 fusion proteins. Therefore, there are likely to be alternative p5-p19 interactions that are Rep independent in which the YY1-60 complex inhibits p19 transcription. We concluded that transcriptional control of the p19 promoter was dependent on the formation of complexes between the p5 and p19 promoters and that activation of the p19 promoter depends largely on the ability of Rep and Sp1 to form a scaffold that positions the p5 YY1 complex near the p19 promoter. | lld:pubmed |
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| pubmed-article:12134028 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12134028 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12134028 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12134028 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12134028 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12134028 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12134028 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:12134028 | pubmed:author | pubmed-author:MuzyczkaNicho... | lld:pubmed |
| pubmed-article:12134028 | pubmed:author | pubmed-author:LacknerDaniel... | lld:pubmed |
| pubmed-article:12134028 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12134028 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:12134028 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12134028 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12134028 | pubmed:pagination | 8225-35 | lld:pubmed |
| pubmed-article:12134028 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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