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://journals.rcsi.science/2686-7389/article/view/135684
DOI: https://doi.org/10.31857/S2686738922600777
EDN: https://elibrary.ru/MPYLIL
ID: 135684

Cite item

Full Text

Open Access
Restricted Access

Access granted
Restricted Access

Subscription Access

Abstract
About the authors
References
Supplementary files
Statistics

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.