Poly(ADP-ribosyl)ation of proteins associated with nuclear matrix in rat testis.
We have previously demonstrated that a significant percentage of poly(ADPR) polymerase is present, as a tightly-bound form, at the third level of chromatin organisation defined by chromosomal loops and nuclear matrix. The present work is focused on the study of poly(ADP-ribosyl)ation of proteins present in these nuclear subfractions. It has been shown that, due to the action of poly(ADPR) polymerase, the ADP-ribose moiety of [14C]NAD is transferred to both loosely-bound and tightly-bound chromosomal proteins, which in consequence are modified by chain polymers of ADP-ribose of different lengths. Moreover, histone-like proteins seem to be ADP-ribosylated in chromosomal loops and nuclear matrix associated regions of DNA loops (MARS). A hypothesis can be put forward that the ADP-ribosylation system is functionally related to the nuclear processes, actively coordinated by the nuclear matrix.
Quesada
P
P
Dipartimento di Chimica Organica e Biologica, Università Federico II, Naples, Italy.
d'Erme
M
M
Atorino
L
L
Faraone-Mennella
M R
MR
Caiafa
P
P
Farina
B
B
D000818:Animals; D034961:Antigens, Nuclear; D008297:Male; D008954:Models, Biological; D009687:Nuclear Proteins / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D013737:Testis / Q000378:metabolism*
D034961:Antigens, Nuclear; D009687:Nuclear Proteins; D011065:Poly(ADP-ribose) Polymerases