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Histone Modification

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...

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Simultaneous Measurement of HDAC1 and HDAC6 Activity in HeLa Cells Using UHPLC-MS

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Structure-Based Identification of HDAC8 Non-histone Substrates.

Nawsad Alam¹, Lior Zimmerman¹, Noah A Wolfson²

¹Department of Microbiology and Molecular Genetics, Institute for Medical Research Israel-Canada, Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel.

Structure (London, England : 1993)

|March 3, 2016

Summary

Researchers identified new protein substrates for Histone Deacetylase 8 (HDAC8) using a structure-based computational approach. This expands the known functions of HDAC8 in regulating cellular processes and the broader acetylome.

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Published on: January 14, 2016

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Histone deacetylases (HDACs) regulate cellular functions by removing acetyl groups from proteins.
HDAC8, a specific HDAC, has recently been found to target non-histone proteins, suggesting a broader role beyond histones.
Understanding HDAC8's full substrate repertoire is crucial for elucidating its role in cellular homeostasis.

Purpose of the Study:

To discover novel protein substrates of HDAC8.
To expand the understanding of the cellular acetylome and its regulation.
To explore the functional complexity of HDAC8.

Main Methods:

Development and application of a structure-based computational approach using Rosetta FlexPepBind.
Evaluation of peptide-binding ability to HDAC8 based on structural models.
Identification of substrates using peptide sequences from known acetylated proteins.

Main Results:

Identification of numerous new in vitro peptide substrates for HDAC8.
Validation of a structure-based method for predicting HDAC8 substrates.
Suggests a significantly larger number of cellular proteins are regulated by HDAC8 than previously known.

Conclusions:

HDAC8 regulates a wider range of cellular proteins than previously appreciated.
The findings expand the known landscape of the acetylome and HDAC8-mediated regulation.
The computational approach provides a powerful tool for future substrate discovery.