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The BCL11A transcription factor stimulates the enzymatic activities of the OGG1 DNA glycosylase

  • Tetiana Petrachkova , Olha Soldatkina , Lam Leduy and Alain Nepveu ORCID logo EMAIL logo
Published/Copyright: September 16, 2024
Biological Chemistry
From the journal Biological Chemistry Volume 405 Issue 11-12

Abstract

The BCL11A transcription factor has previously been shown to interact with and stimulate the enzymatic activities of the NTHL1 DNA glycosylase and Pol β polymerase. Here we show that BCL11A and a smaller peptide encompassing amino acids 160 to 520 can interact with the 8-oxoguanine DNA glycosylase, OGG1, increase the binding of OGG1 to DNA that contains an 8-oxoguanine base and stimulate the glycosylase activity of OGG1. Following BCL11A knockdown, we observed an increase in oxidized purines in the genome using comet assays, while immunoassays reveal an increase in 8-oxoG bases. Structure-function analysis indicates that the stimulation of OGG1 by BCL11A requires the zinc fingers 1, 2 and 3 as well as the proline-rich region between the first and second zing finger, but a glutamate-rich region downstream of zinc finger 3 is dispensable. Ectopic expression of a small peptide that contains the three zinc fingers can rescue the increase in 8-oxoguanine caused by BCL11A knockdown. These findings, together with previous results showing that BCL11A stimulates the enzymatic activities of NTHL1 and the Pol β polymerase, suggest that high expression of BCL11A is important to protect cancer cells against oxidative DNA damage.

Keywords: 8-oxoguanine glycosylase (OGG1); base excision repair; BCL11A; breast cancer; reactive oxygen species (ROS); transcription factor
Corresponding author: Alain Nepveu, Goodman Cancer Institute, McGill University, 1160 Pine Avenue West, Montreal, QC, H3A 1A3, Canada; and Departments of Oncology, Biochemistry, and Medicine, McGill University, 1160 Pine Avenue West, Montreal, QC, H3A 1A3, Canada, E-mail:

Funding source: Canadian Institutes of Health Research

Award Identifier / Grant number: CIHR, MOP-391532

  1. Research ethics: Not applicable.

  2. Author contributions: The authors have accepted responsibility for the entire content of this manuscript and approved its submission. Tetiana Petrachkova: investigation, methodology, validation, formal analysis, visualization, writing-reviewing and editing. Olga Soldatkina: resources. Lam Leduy: investigation, methodology, supervision. Alain Nepveu: conceptualization, methodology, writing – original draft, writing – review and editing, supervision, project administration, funding acquisition.

  3. Competing interests: The authors state no conflict of interest.

  4. Research funding: This work was supported by the Canadian Institutes of Health Research (CIHR, MOP- 391532) to A.N. T.P. and O.S. were supported by Fonds de recherche du Québec-Santé (FRQS).

  5. Data availability: The raw data can be obtained on request from the corresponding author.

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Received: 2024-06-10
Accepted: 2024-08-26
Published Online: 2024-09-16
Published in Print: 2024-12-17

© 2024 Walter de Gruyter GmbH, Berlin/Boston

Articles in the same Issue

  1. Frontmatter
  2. Review
  3. Structure, function, and recombinant production of EGFL7
  4. Research Articles/Short Communications
  5. Protein Structure and Function
  6. Zinc and copper effect mechanical cell adhesion properties of the amyloid precursor protein
  7. The BCL11A transcription factor stimulates the enzymatic activities of the OGG1 DNA glycosylase
  8. Cell Biology and Signaling
  9. Bioprospecting hydroxylated chalcones in in vitro model of ischemia-reoxygenation and probing NOX4 interactions via molecular docking
  10. Carnosic acid prevents heat stress-induced oxidative damage by regulating heat-shock proteins and apoptotic proteins in mouse testis
  11. Novel Techniques
  12. Simultaneous spectral illumination of microplates for high-throughput optogenetics and photobiology
  13. A platform for the early selection of non-competitive antibody-fragments from yeast surface display libraries
https://doi.org/10.1515/hsz-2024-0088
Keywords for this article
8-oxoguanine glycosylase (OGG1); base excision repair; BCL11A; breast cancer; reactive oxygen species (ROS); transcription factor

Articles in the same Issue

  1. Frontmatter
  2. Review
  3. Structure, function, and recombinant production of EGFL7
  4. Research Articles/Short Communications
  5. Protein Structure and Function
  6. Zinc and copper effect mechanical cell adhesion properties of the amyloid precursor protein
  7. The BCL11A transcription factor stimulates the enzymatic activities of the OGG1 DNA glycosylase
  8. Cell Biology and Signaling
  9. Bioprospecting hydroxylated chalcones in in vitro model of ischemia-reoxygenation and probing NOX4 interactions via molecular docking
  10. Carnosic acid prevents heat stress-induced oxidative damage by regulating heat-shock proteins and apoptotic proteins in mouse testis
  11. Novel Techniques
  12. Simultaneous spectral illumination of microplates for high-throughput optogenetics and photobiology
  13. A platform for the early selection of non-competitive antibody-fragments from yeast surface display libraries
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