Comparison of ADP-ribosylation of chromosomal proteins between intact and broken cells.
ADP-ribosylation of nonhistone high mobility group (HMG) proteins and histone H1 in intact cells was markedly different from that in the broken cell systems using isolated nuclei and chromatin. (i) The amounts of (ADP-ribose)n on these proteins in intact cells were less 10(-2) - 10(-3) of those in the broken cell systems. (ii) The modified protein molecules in intact cells were about 2 orders of magnitude less extent than those in the broken cells. (iii) The (ADP-ribose)n chains synthesized in intact cells, nuclei and chromatin were mainly mono, oligo and poly, respectively. (iv) The principal acceptor molecules in intact cells were concentrated in HMG 1, 2, 14 and 17, and histone H1, whereas the four HMG proteins were minor acceptors in nuclei, and HMG 1 and 2 and histone H1 were major acceptors in chromatin.
Tanuma
S
S
Kawashima
K
K
Endo
H
H
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000378:metabolism*; D002843:Chromatin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D043264:Phosphodiesterase I; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism
D002843:Chromatin; D006609:High Mobility Group Proteins; D006657:Histones; D009702:Nucleoside Diphosphate Sugars; D000246:Adenosine Diphosphate Ribose; D010727:Phosphoric Diester Hydrolases; D043264:Phosphodiesterase I