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Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK

Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin... Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK Ferdinand Kappes 1 , * , Catalina Damoc 2 , Rolf Knippers 1 , Michael Przybylski 2 , Lorenzo A. Pinna 3 and Claudia Gruss 1 1 Department of Biology 2 Department of Chemistry, University of Konstanz, 78457 Konstanz, Federal Republic of Germany 3 Department of Biological Chemistry, University of Padua, Padua, Italy ABSTRACT 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular and Cellular Biology American Society For Microbiology

Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK

Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK

Molecular and Cellular Biology , Volume 24 (13): 6011 – Jul 1, 2004

Abstract

Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK Ferdinand Kappes 1 , * , Catalina Damoc 2 , Rolf Knippers 1 , Michael Przybylski 2 , Lorenzo A. Pinna 3 and Claudia Gruss 1 1 Department of Biology 2 Department of Chemistry, University of Konstanz, 78457 Konstanz, Federal Republic of Germany 3 Department of Biological Chemistry, University of Padua, Padua, Italy ABSTRACT 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.

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Publisher
American Society For Microbiology
Copyright
Copyright © 2004 by the American society for Microbiology.
ISSN
0270-7306
eISSN
1098-5549
DOI
10.1128/MCB.24.13.6011-6020.2004
pmid
15199154
Publisher site
See Article on Publisher Site

Abstract

Phosphorylation by Protein Kinase CK2 Changes the DNA Binding Properties of the Human Chromatin Protein DEK Ferdinand Kappes 1 , * , Catalina Damoc 2 , Rolf Knippers 1 , Michael Przybylski 2 , Lorenzo A. Pinna 3 and Claudia Gruss 1 1 Department of Biology 2 Department of Chemistry, University of Konstanz, 78457 Konstanz, Federal Republic of Germany 3 Department of Biological Chemistry, University of Padua, Padua, Italy ABSTRACT 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.

Journal

Molecular and Cellular BiologyAmerican Society For Microbiology

Published: Jul 1, 2004

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