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Originally published In Press as doi:10.1074/jbc.M109503200 on November 1, 2001

J. Biol. Chem., Vol. 277, Issue 2, 1092-1098, January 11, 2002
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Protein Kinase CK2 Differentially Phosphorylates Maize Chromosomal High Mobility Group B (HMGB) Proteins Modulating Their Stability and DNA Interactions*

Christian StemmerDagger , Andrea Schwander§, Guy BauwDagger , Peter FojanDagger , and Klaus D. GrasserDagger ||

From the Dagger  Department of Life Science, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark and the § Institute for Biology III, Freiburg University, Schänzlestrasse 1, D-79104 Freiburg, Germany

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, whereas Ser133 and Ser136 are differentially phosphorylated. The functional significance of the CK2-mediated phosphorylation of HMGB proteins was analyzed 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.

* This work was supported by grants from the German Research Society (DFG) and the Danish Research Council (SNF) (to K. D. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

present address: Dept. of Molecular Cell Biology, Heinrich-Pette-Institute, Martinistr. 52, D-20251 Hamburg, Germany.

|| To whom correspondence should be addressed. Fax: 45-9814 1808; E-mail: kdg@bio.auc.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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