Angrisano, Tiziana (2006) TACC3 mediates the association of MBD2 with histone acetyltransferases: a novel mechanism for reactivation of methylated promoters. [Tesi di dottorato] (Unpublished)


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Item Type: Tesi di dottorato
Lingua: English
Title: TACC3 mediates the association of MBD2 with histone acetyltransferases: a novel mechanism for reactivation of methylated promoters
Angrisano, TizianaUNSPECIFIED
Date: 2006
Date Type: Publication
Number of Pages: 82
Institution: Università degli Studi di Napoli Federico II
Department: Biologia e patologia cellullare e molecolare "L. Califano"
Dottorato: Genetica e medicina molecolare
Ciclo di dottorato: 15
Coordinatore del Corso di dottorato:
Bruni, Carmelo BrunoUNSPECIFIED
Bruni, Carmelo BrunoUNSPECIFIED
Date: 2006
Number of Pages: 82
Uncontrolled Keywords: 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
Date Deposited: 28 Jul 2008
Last Modified: 30 Apr 2014 19:24
DOI: 10.6092/UNINA/FEDOA/895


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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