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Molecular Biology

, Volume 53, Issue 3, pp 379–383 | Cite as

Multiple Interactions of the Oct-1 (POU2F1) Transcription Factor with PORE and MORE Sites

  • A. G. StepchenkoEmail author
  • S. G. Georgieva
  • E. V. Pankratova
GENOMICS. TRANSCRIPTOMICS
  • 6 Downloads

Abstract

The Oct-1 (POU2F1) transcription factor is one of the most important regulatory proteins in humans and other mammals. An increase in Oct-1 aids the resistance to oxidative and cytotoxic stresses and radiation exposure. A high level of Oct-1 is found in many human tumors and correlates with low survival. Oct-1 interacts with its binding sites as a monomer, a homodimer, or a multimer. The nucleotide sequence of the Oct-1 binding site determines the character of interaction and the conformation of Oct-1 on target DNA, thus influencing the binding of Oct-1 co-repressors and co-activators. Nucleotide substitutions were introduced in all positions of the PORE and MORE sequences and tested for effect on the Oct-1 capability of forming monomeric and dimeric DNA–protein complexes. The position and nature of nucleotide substitutions were found to affect the type of Oct-1 binding to DNA. Several substitutions suppressed the formation of dimers, while others stimulated the process. Certain nucleotide substitutions completely prevented the binding of both monomers and dimers. The Oct-1 concentration in the cell is another factor that affects the character of DNA–protein interactions. Based on the results, the nature and affinity of interaction with Oct-1 is possible to predict from the nucleotide sequence for PORE and MORE sites of the human genome.

Keywords:

Oct-1 (POU2F1 ) transcription factor DNA–protein interaction transcription regulation 

Notes

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Copyright information

© Pleiades Publishing, Inc. 2019

Authors and Affiliations

  • A. G. Stepchenko
    • 1
    Email author
  • S. G. Georgieva
    • 1
  • E. V. Pankratova
    • 1
  1. 1.Engelhardt Institute of Molecular Biology, Russian Academy of SciencesMoscowRussia

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