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Papers In Press, published online ahead of print November 1, 2001
J. Biol. Chem, 10.1074/jbc.M109503200
Submitted on October 2, 2001
Revised on November 1, 2001
Accepted on November 1, 2001
Department of Life Science, Aalborg University, Aalborg DK-9000
Corresponding Author: kdg{at}bio.auc.dk
The high mobility group (HMG) proteins of the HMGB family are architectural factors in eukaryotic chromatin, which are involved in the regulation of various DNA-dependent processes. We have examined the post-translational modifications of five HMGB proteins from maize suspension cultured cells, revealing that HMGB1 and HMGB2/3, but not HMGB4 and HMGB5, are phosphorylated by protein kinase CK2. The phosphorylation sites have been mapped to the acidic C-terminal domains by analysis of tryptic peptides derived from HMGB1 and HMGB2/3 using nanospray ion trap mass spectrometry. In native HMGB1, Ser149 is constitutively phosphorylated, while Ser133 and Ser136 are differentially phosphorylated. The functional significance of the CK2-mediated phosphorylation of HMGB proteins was analysed by circular dichroism measurements showing that the phosphorylation increases the thermal stability of the HMGB proteins. Electrophoretic mobility shift assays demonstrate that the phosphorylation reduces the affinity of the HMGB proteins for linear DNA. The specific recognition of DNA minicircles is not affected by the phosphorylation, but a different pattern of protein/DNA complexes is formed. Collectively, these findings show that phosphorylation of residues within the acidic C-terminal domain of the HMGB proteins can modulate protein stability and the DNA binding properties of the HMGB proteins.
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