THE NCoR CO-REPRESSOR INTERACTS WITH THE KAISO TRANSCRIPTION FACTOR THROUGH A MECHANISM DIFFERENT FROM THAT OF BCL6 INTERACTION

K. I. Balagurov; Балагуров К. И.; P. G. Georgiev; Георгиев П. Г.; A. N. Bonchuk; Бончук А. Н.

doi:10.31857/S2686738922600777

THE NCoR CO-REPRESSOR INTERACTS WITH THE KAISO TRANSCRIPTION FACTOR THROUGH A MECHANISM DIFFERENT FROM THAT OF BCL6 INTERACTION

Authors: Balagurov K.I.¹, Georgiev P.G.¹, Bonchuk A.N.¹
Affiliations:
1. Institute of Gene Biology, Russian Academy of Sciences
Issue: Vol 508, No 1 (2023)
Pages: 91-94
Section: Articles
URL: https://vestnik.nvsu.ru/2686-7389/article/view/651159
DOI: https://doi.org/10.31857/S2686738922600777
EDN: https://elibrary.ru/MPYLIL
ID: 651159

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Abstract

The vertebrate transcription factor Kaiso binds specifically to methylated DNA sequences using C2H2-type zinc fingers. In addition to C2H2-domains, the BTB/POZ domain, which forms homodimers, is located at the N-terminus of Kaiso. Kaiso, like several other well-studied BTB/POZ proteins, including BCL6, interacts with the NCoR (nuclear co-repressor) protein, which determines the landing of transcriptional repressive complexes on chromatin. Using the yeast two-hybrid system, we have shown that the N-terminal domain of NCoR interacts with the C-terminal zinc fingers of Kaiso, and not with its BTB/POZ domain, as previously assumed. The results obtained demonstrate that NCoR interacts with various transcription factor domains, which can increase the efficiency of attracting NCoR-dependent repressor complexes to regulatory regions of the genome.

Keywords

co-repressors, zinc-finger proteins, C2H2-domains, transcription factors, transcriptional repression

References

Prokhortchouk A., Hendrich B., Jorgensen H., et al. // Genes and Development. 2001. V. 15,13. P. 1613–1618.
Yoon H., Chan D., Reynolds A., et al. // Molecular Cell. 2003. V. 12,3. P. 723–734.
Mottis A., Mouchiroud L., Auwerx J. // Genes and Development. 2013. V. 27,8. P. 819–835.
Yu J., Li Y., Ishizuka T., et al. // EMBO Journal. 2003. V. 22,13. P. 3403–3410.
Guenther M.G., Barak O., Lazar M. A. // Molecular and Cellular biology. 2001. V. 21,18. P. 6091–6101.
Horlein A.J., Naar A.M., Heinzel T., et al. // Nature. 1995. V. 377. P. 397–404.
Park D.M., Li J., Okamoto H., et al. // Cell Cycle. 2007. V. 6,4. P. 467–470.
Ahmad K., Melnick A., Lax S., et al. // Molecular Cell. 2003. V. 12,6. P. 1551–1564.
Bilic I., Koesters C., Unger B., et al. // Nature Immunology. 2006. V. 7,4. P. 392–400.
Huynh K.D., Bardwell V.J. // Oncogene. 1998. V. 17. P. 2473–2484.
Zacharchenko T., Wright S. // IUCrJ. 2021. V. 8. P. 154–160.
Buck-Koehntop B.A., Stanfield R.L., Ekiert D.C., et al. // PNAS. 2012. V. 109,38. P. 15229–15234.
Jumper J., Evans R., Pritzel A., et al. // Nature. 2021. V. 596,7873. P. 583–589.