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  • Title: Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins.
    Author: Giancotti V, Bandiera A, Sindici C, Perissin L, Crane-Robinson C.
    Journal: Biochem J; 1996 Aug 01; 317 ( Pt 3)(Pt 3):865-70. PubMed ID: 8760375.
    Abstract:
    Micrococcal nuclease digestion of nuclei from mouse Lewis lung carcinoma cells releases a protein mixture into the supernatant that lacks histone H1 and contains a full complement of high-mobility-group I (HMGI) proteins (i.e. I, Y and I-C). This implies that all three HMGI proteins are localized at the nuclease-sensitive regions of active chromatin. It is also shown that if Ca2+ ions are present in the nuclear incubation buffer (with or without exogenous nuclease), all three HMGI proteins become ADP-ribosylated. We propose that this modification of HMGI family proteins is part of the general poly(ADP-ribosyl)ation that accompanies DNA damage in apoptosis and other processes.
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