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Author Notes:

Elizabeth V. Minten, eminten@hms.harvard.edu

David S. Yu, dsyu@emory.edu

E.V.M. and D.S.Y. wrote the draft of the manuscript and contributed to editing.

We thank members of the Yu lab for their helpful discussion and technical expertise. This work was supported by the National Institute of General Medical Sciences of the National Institutes of Health (NIH) (5T32GM008367-29), the National Cancer Institute (NCI) of the NIH (F31CA225124 to E.V.M. and R01CA178999 and R01CA254403 to D.S.Y.), the U.S. Department of Defense (BC180883 and OC160540 to D.S.Y.), the Basser Center for BRCA (32356 to D.S.Y.), and the Winship Cancer Institute/Brenda Nease Breast Cancer Research Fund (53237 to D.S.Y.). Research reported in this publication was supported in part by the Emory Integrated Genomics Core (EIGC) Shared Resource of Winship Cancer Institute of Emory University and the NIH/NCI under award number P30CA138292. The content is solely the responsibility of the authors and does not necessarily represent the official

The authors declare no competing interests.

Subject:

Keywords:

  • Cancer
  • Cell-based Assays
  • Protein Biochemistry
  • Protein expression and purification
  • Acetylation
  • Acetyltransferases
  • Histones
  • Lysine
  • Protein Processing, Post-Translational

Protocol for in vitro lysine deacetylation to test putative substrates of class III deacetylases

Tools:

Journal Title:

STAR Protocols

Volume:

Volume 3, Number 2

Publisher:

, Pages 101313-101313

Type of Work:

Article | Final Publisher PDF

Abstract:

Lysine acetylation is an important post-translational modification that is used in multiple cellular pathways, such as the regulation of gene expression at the histone level. The purpose of this assay is to test for putative substrates of class III deacetylases using an in vitro method. The in vitro analysis helps circumvent confounding variables when assessing for a direct relationship between deacetylase and substrate, such as the effects of other cellular deacetylases or acetyltransferases that modify the substrate in vivo. For complete details on the use and execution of this protocol, please refer to Minten et al. (2021).

Copyright information:

© 2022 The Author(s)

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/rdf).
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