Activation mechanism of the nuclear chaperone nucleoplasmin: role of the core domain.

@article{Bauelos2003ActivationMO,
  title={Activation mechanism of the nuclear chaperone nucleoplasmin: role of the core domain.},
  author={Sonia Ba{\~n}uelos and Aitor Hierro and Jesus M. Arizmendi and Guillermo Montoya and Adelina Prado and Arturo Muga},
  journal={Journal of molecular biology},
  year={2003},
  volume={334 3},
  pages={585-93}
}
Nucleoplasmin (NP) mediates nucleosome assembly by removing basic proteins from sperm chromatin and exchanging them with histones. This function is modulated by phosphorylation of NP at multiple sites. NP is pentameric, each monomer consisting of two domains: a core, which forms a stable ring-like pentamer, and a tail, that holds a polyglutamic tract and the nuclear localization signal. In the present study, we have explored the role of the core domain in the functionality of NP. Despite… CONTINUE READING