Angrisano, Tiziana (2006) TACC3 mediates the association of MBD2 with histone acetyltransferases: a novel mechanism for reactivation of methylated promoters. [Tesi di dottorato] (Inedito)
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| Tipologia del documento: | Tesi di dottorato |
|---|---|
| Lingua: | English |
| Titolo: | TACC3 mediates the association of MBD2 with histone acetyltransferases: a novel mechanism for reactivation of methylated promoters |
| Autori: | Autore Email Angrisano, Tiziana [non definito] |
| Data: | 2006 |
| Tipo di data: | Pubblicazione |
| Numero di pagine: | 82 |
| Istituzione: | Università degli Studi di Napoli Federico II |
| Dipartimento: | Biologia e patologia cellullare e molecolare "L. Califano" |
| Dottorato: | Genetica e medicina molecolare |
| Ciclo di dottorato: | 15 |
| Coordinatore del Corso di dottorato: | nome email Bruni, Carmelo Bruno [non definito] |
| Tutor: | nome email Bruni, Carmelo Bruno [non definito] |
| Data: | 2006 |
| Numero di pagine: | 82 |
| Parole chiave: | MBD2, TACC3, Methylation |
| Settori scientifico-disciplinari del MIUR: | Area 05 - Scienze biologiche > BIO/11 - Biologia molecolare Area 06 - Scienze mediche > MED/03 - Genetica medica Area 05 - Scienze biologiche > BIO/13 - Biologia applicata Area 06 - Scienze mediche > MED/07 - Microbiologia e microbiologia clinica Area 05 - Scienze biologiche > BIO/12 - Biochimica clinica e biologia molecolare clinica Area 05 - Scienze biologiche > BIO/18 - Genetica |
| Depositato il: | 28 Lug 2008 |
| Ultima modifica: | 30 Apr 2014 19:24 |
| URI: | http://www.fedoa.unina.it/id/eprint/895 |
| DOI: | 10.6092/UNINA/FEDOA/895 |
Abstract
We have recently reported that a novel MBD2 interactor (MBDin) has the capacity to reactivate transcription from MBD2-repressed methylated promoters even in the absence of demethylation events. Here we show that another unrelated protein, TACC3, displays a similar activity on methylated genes. In addition the data reported here provide possible molecular mechanisms for the observed phenomenon. Immunoprecipitation experiments showed that MBD2/TACC3 form a complex in vivo with the histone acetyltransferase pCAF. MBD2 could also associate with HDAC2, a component of MeCP1 repression complex. However, we found that the complexes formed by MBD2 with TACC3/pCAF and with HDAC2 were mutually exclusive. Moreover, HAT enzymatic assays demonstrated that HAT activity associates with MBD2 in vivo and that such association significantly increased when TACC3 was overexpressed. Overall our findings suggest that TACC3 can be recruited by MBD2 on methylated promoters and is able to reactivate transcription possibly by favoring the formation of an HAT-containing MBD2 complex and, thus, switching the repression potential of MBD2 in activation even prior to eventual demethylation.
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