Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region |
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| Affiliation: | 1. Department of Physical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Kraków, Poland;2. Dipartimento di Scienze e Tecnologie Agro-Alimentari, Alma Mater Studiorum — Università di Bologna, Piazza Goidanich 60, 47521 Cesena, Italy;3. Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine — CIRMMP, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy;4. Magnetic Resonance Center — CERM, University of Florence, 50019, Florence, Italy;1. Martin-Luther-University Halle-Wittenberg, Institute for Physiological Chemistry, 06114 Halle, Germany;2. Martin-Luther-University Halle-Wittenberg, Institute of Human Genetics, 06114 Halle, Germany;3. Department of Medicine, Health and Medical University, 14471 Potsdam, Germany;1. Special Centre for Molecular Medicine, Jawaharlal Nehru University, New Delhi 110067, India;2. Special Centre for Systems Medicine (Concurrent Faculty), Jawaharlal Nehru University, New Delhi 110067, India;3. National Centre for Disease Control, New Delhi, India;1. Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Sk?odowska University, Lublin, Poland;2. Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw 02-106, Poland;3. Polish-Japanese Academy of Information Technology, Warsaw 02-008, Poland;4. Department of Biochemistry and Molecular Biology, Medical University of Lublin, 21-093 Lublin, Poland |
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| Abstract: | Human protein Yin Yang 1 (YY1) controls the transcription of hundreds of genes both positively and negatively through interactions with a wide range of partner proteins. Results presented here from proteolytic sensitivity, calorimetry, circular dichroism, fluorescence, NMR, size-exclusion chromatography, SELEX, and EMSA show that purified YY1 forms dimers via its disordered N-terminal region with strong zinc-ion concentration dependence. The YY1 dimer is shown to bind tandem repeats of a canonical recognition DNA sequence with high affinity, and analysis of human YY1 regulatory sites shows that many contain repeats of its recognition elements. YY1 dimerization may compete with partner protein interactions, making control by zinc ion concentration a previously unrecognized factor affecting YY1 gene regulation. Indeed, YY1 is known to be important in many pathogenic processes, including neoplasia, in which zinc ion concentrations are altered. The present results incentivize studies in vivo or in vitro that explore the role of zinc ion concentration in YY1-mediated gene expression. |
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