Phosphorylation by protein kinase CK2 changes the DNA binding properties of the human chromatin protein DEK.

Journal Article (Journal Article)

We have examined the posttranslational modification of the human chromatin protein DEK and found that DEK is phosphorylated by the protein kinase CK2 in vitro and in vivo. Phosphorylation sites were mapped by quadrupole ion trap mass spectrometry and found to be clustered in the C-terminal region of the DEK protein. Phosphorylation fluctuates during the cell cycle with a moderate peak during G(1) phase. Filter binding assays, as well as Southwestern analysis, demonstrate that phosphorylation weakens the binding of DEK to DNA. In vivo, however, phosphorylated DEK remains on chromatin. We present evidence that phosphorylated DEK is tethered to chromatin throughout the cell cycle by the un- or underphosphorylated form of DEK.

Full Text

Duke Authors

Cited Authors

  • Kappes, F; Damoc, C; Knippers, R; Przybylski, M; Pinna, LA; Gruss, C

Published Date

  • July 1, 2004

Published In

Volume / Issue

  • 24 / 13

Start / End Page

  • 6011 - 6020

PubMed ID

  • 15199154

Pubmed Central ID

  • PMC480878

Electronic International Standard Serial Number (EISSN)

  • 1098-5549

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.24.13.6011-6020.2004


  • eng