Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins.
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.
Giancotti
V
V
Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Università di Trieste, Italy.
Bandiera
A
A
Sindici
C
C
Perissin
L
L
Crane-Robinson
C
C
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D006609:High Mobility Group Proteins / Q000378:metabolism*; D051379:Mice; D008836:Micrococcal Nuclease / Q000378:metabolism; D008969:Molecular Sequence Data; D014407:Tumor Cells, Cultured
D006609:High Mobility Group Proteins; D000246:Adenosine Diphosphate Ribose; D008836:Micrococcal Nuclease; D002118:Calcium