Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain.

@article{Hger1991InteractionOX,
  title={Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain.},
  author={Thomas H. H{\"o}ger and Georg Krohne and J{\"u}rgen A. Kleinschmidt},
  journal={Experimental cell research},
  year={1991},
  volume={197 2},
  pages={280-9}
}
Morphological data suggest an interaction of the nuclear lamina with chromatin which markedly changes during the cell cycle. To study the molecular basis of this interaction we developed a novel lamin/chromatin binding assay that quantitated the binding of soluble, radiolabeled lamins to minichromosomes assembled in Xenopus laevis oocyte nuclear extracts. Lamins were derived from couple in vitro transcription and translation of the corresponding cDNAs. Chromatin binding was detected by… CONTINUE READING

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