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Updated: Jun 22, 2026
14:32
Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
Published on: February 27, 2016
SIRT1 is a circadian deacetylase for core clock components
William J Belden1, Jay C Dunlap
1Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA.
Cell
|July 30, 2008
Summary
The circadian rhythm regulator CLOCK, a histone acetyltransferase, works with the NAD(+)-dependent enzyme SIRT1, a histone deacetylase. SIRT1 counteracts CLOCK activity, impacting cellular metabolism and the circadian system.
Area of Science:
- Molecular Biology
- Chronobiology
- Biochemistry
Background:
- The transcriptional activator CLOCK is essential for the circadian expression of numerous genes.
- CLOCK possesses histone acetyltransferase activity, regulating gene transcription within the circadian system.
Discussion:
- SIRT1, a NAD(+)-dependent enzyme, acts as a histone deacetylase.
- SIRT1's deacetylase activity counteracts the acetyltransferase activity of CLOCK.
- This interaction reveals a metabolic influence on the circadian clock.
Key Insights:
- SIRT1 deacetylates histones, opposing CLOCK's acetylation function.
- The balance between SIRT1 and CLOCK activities is crucial for circadian gene regulation.
- Cellular metabolism, through NAD(+) levels influencing SIRT1, directly impacts the circadian system.
Outlook:
- Further research can elucidate the precise mechanisms of SIRT1-CLOCK interaction.
- Investigating this interplay may reveal new therapeutic targets for circadian rhythm disorders.
- Understanding the metabolic regulation of circadian clocks has broad implications for health and disease.
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