Literature DB >> 8760375

Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins.

V Giancotti1, A Bandiera, C Sindici, L Perissin, C Crane-Robinson.   

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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Year:  1996        PMID: 8760375      PMCID: PMC1217565          DOI: 10.1042/bj3170865

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  67 in total

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