Interaction of p21(CDKN1A) with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair. (Articolo in rivista)

Type
Label
  • Interaction of p21(CDKN1A) with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/nar/gkn014 (literal)
Alternative label
  • Cazzalini O, Perucca P, Savio M, Necchi D, Bianchi L, Stivala LA, Ducommun B, Scovassi AI, Prosperi E. (2008)
    Interaction of p21(CDKN1A) with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair.
    in Nucleic acids research
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cazzalini O, Perucca P, Savio M, Necchi D, Bianchi L, Stivala LA, Ducommun B, Scovassi AI, Prosperi E. (literal)
Pagina inizio
  • 1713 (literal)
Pagina fine
  • 1722 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Corresponding author: Ennio Prosperi (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 36 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Cazzalini O., Perucca P., Savio M., Bianchi L., Stivala L.A. Dipartimento di Medicina Sperimentale, Università di Pavia, Italy; Necchi D., Dipartimento di Biologia Animale, Università di Pavia, Italy. Ducommun B., LBCMCP Universite P. Sabatier, Toulouse, France; IGM-CNR, Pavia, Italy (literal)
Titolo
  • Interaction of p21(CDKN1A) with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair. (literal)
Abstract
  • The cell-cycle inhibitor p21(CDKN1A) has been suggested to directly participate in DNA repair, thanks to the interaction with PCNA. Yet, its role has remained unclear. Among proteins interacting with both p21 and PCNA, the histone acetyltransferase (HAT) p300 has been shown to participate in DNA repair. Here we report evidence indicating that p21 protein localizes and interacts with both p300 and PCNA at UV-induced DNA damage sites. The interaction between p300 and PCNA is regulated in vivo by p21. Indeed, loss of p21, or its inability to bind PCNA, results in a prolonged binding to chromatin and an increased association of p300 with PCNA, in UV-irradiated cells. Concomitantly, HAT activity of p300 is reduced after DNA damage. In vitro experiments show that inhibition of p300 HAT activity induced by PCNA is relieved by p21, which disrupts the association between recombinant p300 and PCNA. These results indicate that p21 is required during DNA repair to regulate p300 HAT activity by disrupting its interaction with PCNA. (literal)
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