Phosphorylation of linker histones by a protein kinase A-like activity in mitotic nuclei.

@article{Sweet1997PhosphorylationOL,
  title={Phosphorylation of linker histones by a protein kinase A-like activity in mitotic nuclei.},
  author={Melody T. Sweet and Gary Carlson and Richard G. Cook and Dominic Nelson and C David Allis},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 2},
  pages={916-23}
}
Micronuclear linker histones of the ciliated protozoan, Tetrahymena thermophila, are extensively phosphorylated in vivo. Each of these polypeptides, alpha, beta, gamma, and delta, contains sites for phosphorylation by cyclic-AMP dependent protein kinase (PKA) but not Cdc2 kinase, and some data have been presented implicating PKA kinase in their phosphorylation in vitro and in vivo (Sweet, M. T., and Allis, C. D. (1993) Chromosoma 102, 637-647; Sweet, M. T., Jones, K., and Allis, C. D. (1996) J… CONTINUE READING

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