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Poly synthetase nuclear matrix association

ADP-Ribosylation of Nuclear Matrix Proteins. Association of Poly(ADP-Ribose) Synthetase with the Nuclear Matrix... [Pg.222]

The present experiments show that a number of ADP-ribosylated proteins in the range of 40,000-300,000 kD exist in nuclear matrices isolated from HeLa cells, and that the lamins A and B are probably modified. Furthermore, it was observed that a portion (approx. 1%) of the nuclear poly(ADP-ribose) synthetase is tightly associated with the isolated nuclear matrix. [Pg.222]

The present results demonstrate that a portion of the nuclear poly(ADP-ribose) synthetase is found in tight association with the isolated nuclear matrix. The question is whether the enzyme, if present at this site in vivo, is required to maintain reactions proceeding in association with the nuclear matrix. These may, for example, be reactions involving DNA in the vicinity of the DNA attachment sites. In view of various indications that transcription of active genes occurs in association with the nuclear matrix [6-9], the results of Slattery et al. [27] are also of interest. The authors observed that poly(ADP-ribose) synthetase is identical with the factor TFIIC which, by inhibiting nick-induced transcription, eliminates random transcription by polymerase II. [Pg.227]


See other pages where Poly synthetase nuclear matrix association is mentioned: [Pg.226]    [Pg.170]    [Pg.47]   
See also in sourсe #XX -- [ Pg.225 , Pg.226 ]




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