Functional domain structure of human centromere protein B. Implication of the internal and C-terminal self-association domains in centromeric heterochromatin condensation.

@article{Sugimoto1994FunctionalDS,
  title={Functional domain structure of human centromere protein B. Implication of the internal and C-terminal self-association domains in centromeric heterochromatin condensation.},
  author={Kenji Sugimoto and Y Hagishita and Michio Himeno},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 39},
  pages={24271-6}
}
Centromere protein B (CENP-B) is a common centromere DNA-binding protein among mammalian centromeres. CENP-B possesses the specific DNA binding activity to the 17-base pair sequence dispersed in centromeric repetitive DNA sequences. In the previous study, we have shown that its DNA-binding domain exists within the N-terminal 134 amino acid residues. Here, to clarify the whole domain structure, another functional unit required for CENP-B self-association was examined. Recombinant CENP-B was… CONTINUE READING