The acetyltranferases p300/CBP interact with, and acetylate XPG protein in nucleotide excision repair. (Comunicazione a convegno)

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  • The acetyltranferases p300/CBP interact with, and acetylate XPG protein in nucleotide excision repair. (Comunicazione a convegno) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Alternative label
  • Tillhon M, Cazzalini O, Nardo T, Necchi D, Sommatis S, Stivala LA, Scovassi AI, Prosperi E (2012)
    The acetyltranferases p300/CBP interact with, and acetylate XPG protein in nucleotide excision repair.
    in 3rd Erling Seeberg Symposium on DNA Repair, Trondheim/Orland, Norvegia, 19-24 giugno 2012
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Tillhon M, Cazzalini O, Nardo T, Necchi D, Sommatis S, Stivala LA, Scovassi AI, Prosperi E (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Genetica Molecolare, CNR (IGM-CNR); Dipartimento di Medicina Molecolare, Università di Pavia; Dipartimento di Scienze del Farmaco, Università di Pavia. (literal)
Titolo
  • The acetyltranferases p300/CBP interact with, and acetylate XPG protein in nucleotide excision repair. (literal)
Abstract
  • Following DNA damage, lysine or histone acetyltransferase (KAT or HAT) p300 associates with PCNA, which inhibits the HAT activity. However, the role of this inhibition, counteracted by p21CDKN1A during DNA repair is still unclear. To better understand the involvement of p300, and its homolog CBP, in DNA repair, we have investigated the interaction of these proteins with a specific NER factor, i.e. XPG, because it is a PCNA-interacting protein. The results have shown that both p300 and CBP proteins interact with XPG, and their association increases after DNA damage. XPG was acetylated in vitro by both enzymes, and immunoprecipitation of acetylated proteins with anti acetyl-K antibody revealed the presence of acetylated XPG in cell extracts of UV-irradiated human fibroblasts. To investigate the influence of p300/CBP on NER efficiency, expression of these proteins was knocked-down by RNAi in primary human fibroblasts. NER activity was assessed after UV irradiation by UDS, and concomitant immuno-staining for p300 or CBP, to verify efficient knock-down of protein levels. The results have indicated that silencing of either p300 or CBP, significantly reduced (by 30-40%) NER efficiency. The recruitment of XPG to sites of local UV-irradiation was not significantly affected by p300/CBP RNAi, but XPG persisted at late times after irradiation. In knocked-down cells, the levels of acetylated XPG were found to be significantly decreased. In vitro, XPG acetylation was inhibited by PCNA, and in vivo the interaction with p300 was regulated by p21, in a PCNA-dependent manner. These results suggest that p300/CBP activity is required after the initial recruitment of NER factors to DNA damage sites, and suggest that XPG acetylation might be necessary for the release of XPG protein from DNA repair sites. (literal)
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