Phosphorylation of the C subunit (p66) of human DNA polymerase delta.

Abstract : Of the four subunits constituting DNA polymerase delta, subunit C or p66 has been shown to mainly mediate polymerase interaction with PCNA, an auxiliary factor that greatly enhances DNA polymerase delta processivity on primed DNA templates. Here, we provide evidence that a highly conserved region located between amino acids 384 and 399 in the C-terminus of p66 is phosphorylated, most probably by Protein kinase CK2, and that another region, most probably located within the PCNA interacting domain in its extreme C-terminus, regulates its interaction with PCNA. Phosphorylation of p66 is associated with its co-localization with large subunit of DNA polymerase delta, p125, and PCNA, to the insoluble chromatin fraction at the beginning of S-phase. Taken together, the results provide evidence that concurrent phosphorylation events in p66 may positively and negatively regulate its activity and interactions with other components of the replisome during the cell cycle.
Type de document :
Article dans une revue
Biochemical and Biophysical Research Communications, Elsevier, 2008, 367 (2), pp.264-70. 〈10.1016/j.bbrc.2007.12.083〉
Liste complète des métadonnées

http://www.hal.inserm.fr/inserm-00413493
Contributeur : Claude Cochet <>
Soumis le : vendredi 4 septembre 2009 - 12:01:59
Dernière modification le : jeudi 11 janvier 2018 - 06:19:40

Identifiants

Collections

Citation

Laure Lemmens, Serge Urbach, Renaud Prudent, Claude Cochet, Giuseppe Baldacci, et al.. Phosphorylation of the C subunit (p66) of human DNA polymerase delta.. Biochemical and Biophysical Research Communications, Elsevier, 2008, 367 (2), pp.264-70. 〈10.1016/j.bbrc.2007.12.083〉. 〈inserm-00413493〉

Partager

Métriques

Consultations de la notice

241