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Intrinsic disorder of human Yin Yang 1 protein

Andrzej Górecki1, Piotr Bonarek1, Adam Kazimierz Górka1

  • 1Department of Physical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland.

Proteins
|May 13, 2015
PubMed

Insights

Yin Yang 1 (YY1) is an intrinsically disordered protein (IDP). Our study reveals YY1

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Yin Yang 1 (YY1) is a crucial zinc finger protein regulating diverse cellular processes.
  • YY1's extensive interactions suggest intrinsically disordered regions.
  • Understanding YY1's structure is key to its function in development and disease.

Purpose of the Study:

  • To investigate the structural properties of human YY1.
  • To determine if YY1 exhibits characteristics of intrinsically disordered proteins (IDPs).

Main Methods:

  • Biochemical and biophysical techniques including fluorescence, circular dichroism, and gel filtration chromatography.
  • Proteolytic susceptibility assays.
  • Bioinformatics approaches applied to full-length YY1 and its fragments.

Main Results:

  • The N-terminal region of YY1 (residues 1-295) lacks defined tertiary structure and exhibits minimal secondary structure.
  • YY1 demonstrates characteristics consistent with intrinsically disordered proteins (IDPs).
  • The protein exists natively in a partially unfolded conformation.

Conclusions:

  • Human YY1 is classified as an intrinsically disordered protein (IDP).
  • The disordered nature of YY1 facilitates its diverse protein-protein and DNA interactions.
  • This finding provides structural insights into YY1's regulatory roles in cellular processes.
Keywords:
CDIDPSECTFEYY1carcinogenesisdenaturationfluorescencehydrodynamicstranscription factor

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