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CDYL1-dependent decrease in lysine crotonylation at DNA double-strand break sites functionally uncouples

Enas R Abu-Zhayia1, Laila A Bishara1, Feras E Machour1

  • 1Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.

Molecular Cell
|April 21, 2022
PubMed

Insights

CDYL1

Area of Science:

  • Molecular Biology
  • Epigenetics
  • DNA Repair

Background:

  • CDYL1 protein is known to be recruited to DNA double-strand breaks (DSBs).
  • CDYL1 promotes homologous recombination (HR) repair and transcriptional silencing at DSBs.
  • The precise mechanism by which CDYL1 induces silencing remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of CDYL1-mediated transcriptional silencing at DSBs.
  • To investigate the role of CDYL1's enzymatic activity in DSB-induced silencing.
  • To determine the relationship between CDYL1's repair and silencing functions.

Main Methods:

  • Analysis of histone lysine crotonylation (Kcr) and H3K9cr at DSBs.
  • Assessing the impact of CDYL1 on transcription elongation factor ENL.
  • Utilizing genetic inhibition of CDYL1's hydratase activity.
  • Evaluating homologous recombination (HR) efficiency.

Main Results:

  • CDYL1 recruitment to DSBs leads to decreased H3K9cr, correlating with transcriptional silencing.
  • CDYL1's crotonyl-CoA hydratase activity removes H3K9cr, causing ENL eviction and silencing.
  • Inhibiting CDYL1's hydratase activity prevents H3K9cr reduction and alleviates silencing.
  • HR efficiency is unaffected by the inhibition of CDYL1's hydratase activity.

Conclusions:

  • CDYL1's functions in DNA repair and transcriptional silencing at DSBs are separable.
  • CDYL1's enzymatic activity is crucial for DSB-induced silencing, but not for HR.
  • Homologous recombination repair and DSB-induced silencing may operate independently.
Keywords:
CDYL1ENLH3K9crNHEJdouble-strand breakhomologous recombinationlysine acetylationlysine crotonylationtranscriptional repression

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