Adenosine Diphosphoribosylation of Certain Basic Chromosomal Proteins in Isolated Trout Testis Nuclei

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Abstract
Isolated trout testis nuclei rapidly incorporate [.alpha.-32P]NAD+ into chromosomal proteins. Three proteins, very-lysine-rich histone (H1), a specific trout chromosomal protein (H6) and the spermspecific protamines incorporate the label as adenosine diphosphoribosyl (ADP-Rib) residues. No significant labeling of the nucleosomal core histones H2A, H2B, H3 and H4 was observed. The linkage of the [32P](ADP-Rib) residues to each proteins was very labile at pH values > 7.0, but by working at acidic pH and low temperatures the ADP-Rib label could be covalently bound to protein by gel electrophoresis and ion-exchange chromatography. The [32P]ADP-Rib chains could be removed by digestion with snake venom phosphodiesterase with the formation of AMP and phosphoribosyl-AMP.