Mechanism of chromatin assembly in Xenopus oocytes (Articolo in rivista)

Type
Label
  • Mechanism of chromatin assembly in Xenopus oocytes (Articolo in rivista) (literal)
Anno
  • 1986-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/0022-2836(86)90317-7 (literal)
Alternative label
  • Ruberti I.; Worcel A. (1986)
    Mechanism of chromatin assembly in Xenopus oocytes
    in Journal of Molecular Biology; Academic Press, London (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ruberti I.; Worcel A. (literal)
Pagina inizio
  • 457 (literal)
Pagina fine
  • 476 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.scopus.com/inward/record.url?eid=2-s2.0-0022476944&partnerID=q2rCbXpz (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 189 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biology University of Rochester, Rochester, NY 14627, United States (literal)
Titolo
  • Mechanism of chromatin assembly in Xenopus oocytes (literal)
Abstract
  • We have analyzed the chromatin assembly reaction catalyzed by the Xenopus oocyte extract (S-150). A 50 S complex is formed upon mixing the 17 S pUC DNA and the S-150. Mature histones are not detected in this complex, which contains relaxed DNA and protein, and generates subnucleosomal 7 S particles upon digestion with micrococcal nuclease. The relaxed nucleoprotein is gradually supercoiled into nucleosomal chromatin in the S-150, via a pathway that requires ATP and is blocked by novobiocin, and this process is accompanied by the appearance of mature histones H3 and H4. Isolated complexes also supercoil in vitro, which implies the complex is a kit that contains histone precursors, as well as topoisomerases and other enzymes required for assembly. We discuss the biological implications of these findings. © 1986. (literal)
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