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Related Experiment Video

Updated: Mar 1, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Quantitative proteome-based systematic identification of SIRT7 substrates.

Chaohua Zhang1, Zichao Zhai2, Ming Tang1,3

  • 1Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, P. R. China.

Proteomics
|May 31, 2017
PubMed
Summary

Researchers identified novel substrates for the enzyme SIRT7 (Sirtuin 7) using advanced mass spectrometry. This study significantly expands the known functions of SIRT7 in cellular processes, particularly metabolism.

Keywords:
BioinformaticsQuantitative proteomicsSIRT7SubstratesSystematic

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • SIRT7 (Sirtuin 7) is a class III histone deacetylase implicated in various cellular functions.
  • The known substrates of SIRT7 are limited, hindering a full understanding of its biological roles.

Purpose of the Study:

  • To systematically identify and characterize novel substrates of SIRT7.
  • To expand the understanding of SIRT7's involvement in cellular regulatory networks.

Main Methods:

  • Utilized stable-isotope labeling with amino acids in cell culture (SILAC) combined with quantitative mass spectrometry (MS).
  • Employed SIRT7 knockout (SIRT7-/-) and wild-type (SIRT7+/+) mouse embryonic fibroblasts for comparative analysis.
  • Performed in vitro validation and bioinformatics-based prediction analyses to confirm candidate substrates.

Main Results:

  • Identified and quantified 1493 acetylation sites across 789 proteins.
  • Discovered 261 acetylation sites in 176 proteins exhibiting significant changes in acetylation state between SIRT7-/- and SIRT7+/+ cells, designated as putative SIRT7 substrates.
  • Bioinformatic analysis revealed that many putative substrates are involved in metabolic processes.
  • Validated a subset of predicted substrates through in vitro assays.

Conclusions:

  • This study presents a comprehensive list of candidate SIRT7 substrates, significantly advancing the field.
  • The findings suggest a broader role for SIRT7 in regulating cellular metabolism.
  • The developed methodology provides a robust platform for future substrate identification studies.