Phosphorylation alters the affinity of high mobility group protein HMG 14 for single-stranded DNA |
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| Affiliation: | 1. Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden;2. Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Göteborg, Sweden;3. Department of Psychiatry and Neurochemistry, University of Gothenburg, 405 30 Göteborg, Sweden;1. Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg 405 30, Sweden;2. Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK;3. Wellcome Centre for Mitochondrial Research, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK;4. Department of Clinical Neurosciences, School of Clinical Medicine, University of Cambridge, Cambridge, UK;1. Skirball Institute of Biomolecular Medicine, Cell Biology Department, NYU School of Medicine, New York, NY 10016, USA;2. Molecular Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA;3. Proteomics Laboratory, NYU School of Medicine, New York, NY 10016, USA;4. Biochemistry and Molecular Pharmacology, NYU School of Medicine, New York, NY 10016, USA;5. Department of Neurology, NYU School of Medicine, New York, NY 10016, USA;6. Perlmutter Cancer Center, NYU School of Medicine, New York, NY 10016, USA |
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| Abstract: | The effect of phosphorylation on the affinity of HMG 14 from calf thymus for single-stranded DNA (ssDNA) was studied, using a cyclic GMP-dependent protein kinase from bovine lung and a nuclear protein kinase II from rat liver. When phosphorylated by G-kinase, HMG 14 eluted at 0.27 M NaCl from the ssDNA-column, whereas the native protein eluted at 0.30 M salt concentration. In contrast, phosphorylation by nuclear protein kinase II did not alter dissociation of HMG 14 from ssDNA and the phosphoprotein consequently coeluted with the native HMG 14. Thus, addition of a negative charge by phosphorylation of the Ser-6 residue by G-kinase presumably weakens the interaction between the DNA-binding amino acids of HMG 14 and the negatively charged phosphate groups of DNA. |
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