In vitro poly-(ADP-ribosyl)ation of chromatin proteins in the rat tapeworm, Hymenolepis diminuta.
1. (ADP-ribose)-transferase activity in crude chromatin of H. diminuta was demonstrated. 2. Chromatin proteins were ADP-ribosylated in vitro and selectively extracted. 60, 12 and 18% of the (ADP-ribose)n of chromatin proteins was associated with total histones, histone H1 and histone H2B, respectively. 3. The extent of oligo-(ADP-ribose) compared to total (ADP-ribose)n in the chromatin fraction, in the histone fraction, the histone H1 fraction and the histone H2B fraction was 45, 60, 26 and 49%, with an average chain length of 2.8, 2.1, 1.8 and 2.6, respectively. 4. Analysis of (ADP-ribosyl)n-ated proteins by acetic acid/urea polyacrylamide gel electrophoresis demonstrated that histone H1, histone H2B and a 35 kDa non-histone protein were major (ADP-ribose)n acceptors.
Kappus
S
S
Department of Biochemistry, University of Bath, U.K.
Apweiler
R
R
White
C J
CJ
Whish
W J
WJ
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism; D006926:Hymenolepis / Q000378:metabolism*; D008297:Male; D009687:Nuclear Proteins / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar
D002843:Chromatin; D006657:Histones; D009687:Nuclear Proteins; D000246:Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases