Protein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA.

@article{Krohn2003ProteinKC,
  title={Protein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA.},
  author={Nicholas M Krohn and Christian Stemmer and Peter Fojan and Rudi Grimm and Klaus D Grasser},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 15},
  pages={12710-5}
}
The structure-specific recognition protein SSRP1 plays a role in transcription and replication in the chromatin context. Mediated by its C-terminal high mobility group (HMG) box domain, SSRP1 binds DNA non-sequence specifically but recognizes certain DNA structures. Using acetic acid urea polyacrylamide gel electrophoresis and mass spectrometry, we have examined the phosphorylation of maize SSRP1 by protein kinase CK2 alpha. The kinase phosphorylated several amino acid residues in the C… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 23 extracted citations

Casein kinase 2, circadian clocks, and the flight from mutagenic light

Molecular and Cellular Biochemistry • 2005
View 13 Excerpts
Highly Influenced

Histone Displacement during Nucleotide Excision Repair

International journal of molecular sciences • 2012
View 9 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…