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.

Figiel M., Szubert F., Luchinat E., Bonarek P., Baranowska A., Wajda-Nikiel K., et al. (2023). Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region. BIOCHIMICA ET BIOPHYSICA ACTA. GENE REGULATORY MECHANISMS, 1866(1), 1-13 [10.1016/j.bbagrm.2022.194905].

Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region

Luchinat E.;
2023

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.
2023
Figiel M., Szubert F., Luchinat E., Bonarek P., Baranowska A., Wajda-Nikiel K., et al. (2023). Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region. BIOCHIMICA ET BIOPHYSICA ACTA. GENE REGULATORY MECHANISMS, 1866(1), 1-13 [10.1016/j.bbagrm.2022.194905].
Figiel M.; Szubert F.; Luchinat E.; Bonarek P.; Baranowska A.; Wajda-Nikiel K.; Wilamowski M.; Milek P.; Dziedzicka-Wasylewska M.; Banci L.; Gorecki A.
File in questo prodotto:
Eventuali allegati, non sono esposti

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/912944
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 1
  • Scopus 1
  • ???jsp.display-item.citation.isi??? 1
social impact