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Papers In Press, published online ahead of print February 4, 2003
Department of Biotechnology, Aalborg University, Aalborg DK-9000
Corresponding Author: kdg{at}bio.auc.dk
The structure-specific recognition protein SSRP1 plays a role in transcription and replication in the chromatin context. Mediated by its C-terminal HMG-box domain, SSRP1 binds DNA non-sequence-specifically, but recognises 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
J. Biol. Chem, 10.1074/jbc.M300250200
Submitted on January 9, 2003
Revised on February 4, 2003
Accepted on February 4, 2003
Protein kinase CK2 phosphorylates the HMG domain protein SSRP1 inducing the recognition of UV-damaged DNA
. The kinase phosphorylated several amino acid residues in the C-terminal part of the SSRP1 protein. Two phosphorylation sites were mapped in the very C-terminal region next to the HMG-box domain and about seven sites are localised within the acidic domain. Circular dichroism showed that the phosphorylation of the two C-terminal sites by CK2 resulted in a structural change in the region of HMG-box domain, since the negative peak of the CD spectrum at 222 nm was decreased by ~10%. In parallel, the phosphorylation induced the recognition of UV-damaged DNA, whereas the non-phosphorylated protein does not discriminate UV-damaged DNA and control DNA. The affinity of CK2-phosphorylated SSRP1 for the DNA correlates with the degree of UV-induced DNA damage. Moreover, maize SSRP1 can restore the increased UV-sensitivity of a yeast strain lacking the NHP6A/B HMG-domain proteins to levels of the control strain. Collectively, these findings indicate a role for SSRP1 in the UV response of eukaryotic cells.
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