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J. Biol. Chem., Vol. 278, Issue 15, 12710-12715, April 11, 2003
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,§,,
From the 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 Institute of Life Sciences, Aalborg
University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark and
¶ Agilent Technologies, Hewlett-Packardstrasse,
D-76337 Waldbronn, Germany
. 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 localized 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, because 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 between 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.
To whom correspondence should be addressed. Tel.:
45-9635-9126; Fax: 45-9814-1808; E-mail: kdg@bio.auc.dk.
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