The p66 and p12 subunits of DNA polymerase δ are modified by ubiquitin and ubiquitin-like proteins

Geng Liu, Emma Warbrick

    Research output: Contribution to journalArticle

    28 Citations (Scopus)

    Abstract

    Modification by ubiquitin-like proteins is now known to be important for the functions of many proteins involved in DNA replication and repair. We have investigated the modification of human DNA polymerase d by ubiquitin and SUMO proteins. We find that while the p125 and p50 subunits were not modified, the p12 subunit is ubiquitinated and the p66 subunit can be modified by ubiquitin and SUMO3. We show that levels of p12 are regulated by the proteasome, either directly or indirectly, through a mechanism that is not dependent upon p12 ubiquitination. We have mapped two sites of SUMO3-specific modification on the p66 subunit. SUMOylation by SUMO3 but not SUMO2 is unusual: their level of homology is so high that they are normally classified as variants of the same protein. However, our findings show that these two proteins can be distinguished in vivo and may have specific functions.
    Original languageEnglish
    Pages (from-to)360-366
    Number of pages7
    JournalBiochemical and Biophysical Research Communications
    Volume349
    Issue number1
    DOIs
    Publication statusPublished - 2006

    Keywords

    • DNA polymerase delta
    • Ubiquitin
    • SUMO
    • DNA replication
    • PCNA

    Fingerprint Dive into the research topics of 'The p66 and p12 subunits of DNA polymerase δ are modified by ubiquitin and ubiquitin-like proteins'. Together they form a unique fingerprint.

  • Cite this