A tightly-bound form of poly(ADP-ribose)polymerase is present, within the third level of rat testis chromatin structure, both in the loops and in chromatin matrix. When chromatin matrix was extensively digested with DNAaseI, only little residual enzymatic activity remained in the insoluble fraction, the extent of DNA hydrolysis being well correlated to the progressive loss of the poly(ADP-ribose)polymerase activity. These findings suggest that the tightly-bound form of the enzyme is not an intrinsic protein component of chromatin matrix but is only indirectly located in this structure, being rather associated to the attachment points of loop DNA on the matrix.
Tightly-bound form of poly(ADP-ribose)polymerase in the higher order of chromatin organization / D'Erme, Maria; M., Malanga; P., Quesada; M. R., Faraone Mennella; B., Farina; Caiafa, Paola. - In: BIOCHEMISTRY INTERNATIONAL. - ISSN 0158-5231. - STAMPA. - 20:5(1990), pp. 887-895.
Tightly-bound form of poly(ADP-ribose)polymerase in the higher order of chromatin organization
D'ERME, Maria;CAIAFA, Paola
1990
Abstract
A tightly-bound form of poly(ADP-ribose)polymerase is present, within the third level of rat testis chromatin structure, both in the loops and in chromatin matrix. When chromatin matrix was extensively digested with DNAaseI, only little residual enzymatic activity remained in the insoluble fraction, the extent of DNA hydrolysis being well correlated to the progressive loss of the poly(ADP-ribose)polymerase activity. These findings suggest that the tightly-bound form of the enzyme is not an intrinsic protein component of chromatin matrix but is only indirectly located in this structure, being rather associated to the attachment points of loop DNA on the matrix.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.