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Related Experiment Videos

Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6.

Wallace H Liu1,2, Jie Zheng3, Jessica L Feldman4

  • 1Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.

Nature Communications
|October 17, 2020
PubMed
Summary

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The protein deacetylase SIRT6 tightly binds nucleosomes, enabling efficient histone deacetylation and maintaining cellular homeostasis. This unique interaction mechanism explains SIRT6

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • SIRT6 is a protein deacetylase crucial for cellular homeostasis.
  • SIRT6 associates with chromatin and reduces global histone H3 acetylation.
  • The mechanism by which SIRT6 achieves this chromatin modification is not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanism of SIRT6 interaction with nucleosomes.
  • To understand how SIRT6 achieves efficient deacetylation of histones on chromatin.

Main Methods:

  • Biochemical analysis of SIRT6-nucleosome interactions.
  • Characterization of the 2:1 enzyme:nucleosome complex formation.
  • Investigation of the role of the SIRT6 C-terminus in binding affinity.

Related Experiment Videos

Main Results:

  • SIRT6 forms an exceptionally tight 2:1 complex with nucleosome core particles via asymmetric binding.
  • Both SIRT6 molecules bind to the nucleosome acidic patch, with the C-terminus mediating higher affinity binding through DNA recognition.
  • Multivalent interactions facilitate productive binding and efficient histone deacetylation.

Conclusions:

  • SIRT6's unique ability to tightly interact with nucleosomes is key to its efficient deacetylase activity.
  • The described binding mechanism explains how SIRT6 maintains cellular homeostasis through histone deacetylation and transcriptional repression.