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Poly[ADP-ribosyl]ation of proteins associated with nuclear matrix in rat testis

100%

Quesada P., d'Erme M., Atorino L., Faraone-Mennella M. R., Caiafa P., Farina B.

Acta Biochimica Polonica

1995

tom 42

nr 2

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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Atorino L.

1 Caiafa P.

1 Faraone-Mennella M. R.

1 Farina B.

1 Quesada P.

1 d'Erme M.

1 1995

Wyniki wyszukiwania

Poly[ADP-ribosyl]ation of proteins associated with nuclear matrix in rat testis