High-Affinity Binding of Tumor-Suppressor Protein p53 and HMGB1 to Hemicatenated DNA Loops

We have recently observed that chromatin architectural protein HMGB1 (previously reported to be involved in numerous biological processes such as DNA replication, recombination, repair, tumor growth, and metastasis) could bind with extremely high affinity (K d < 1 pM) to a novel DNA structure tha...

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Veröffentlicht in:	Biochemistry (Easton) 2004-06, Vol.43 (22), p.7215-7225
Hauptverfasser:	Štros, Michal, Muselíková-Polanská, Eva, Pospíšilová, Šárka, Strauss, François
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Cattle DNA, Catenated - chemistry DNA, Catenated - metabolism Electrophoretic Mobility Shift Assay Glutathione Transferase - genetics Glutathione Transferase - metabolism HMGB1 Protein - chemistry HMGB1 Protein - metabolism Humans Nucleic Acid Conformation Promoter Regions, Genetic - genetics Protein Binding - physiology Protein Structure, Tertiary - physiology Rats Substrate Specificity Thymus Gland - cytology Transcriptional Activation Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - metabolism Tumor Suppressor Proteins - metabolism
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