title: Poly(ADP-ribosyl)ation of proteins associated with nuclear matrix in rat testis.
abstract: 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.
authors.affiliation: Dipartimento di Chimica Organica e Biologica, Università Federico II, Naples, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Quesada
authors.forename: M
authors.initials: M
authors.lastname: d'Erme
authors.forename: L
authors.initials: L
authors.lastname: Atorino
authors.forename: M R
authors.initials: MR
authors.lastname: Faraone-Mennella
authors.forename: P
authors.initials: P
authors.lastname: Caiafa
authors.forename: B
authors.initials: B
authors.lastname: Farina
mesh_terms: 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*
chemical_list: D034961:Antigens, Nuclear; D009687:Nuclear Proteins; D011065:Poly(ADP-ribose) Polymerases