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Hat1-Dependent Lysine Acetylation Targets Diverse Cellular Functions.

Paula A Agudelo Garcia1, Prabakaran Nagarajan1, Mark R Parthun1

  • 1Department of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, Ohio 43210, United States.

Journal of Proteome Research
|February 22, 2020
PubMed
Summary

The study reveals that Hat1 (histone acetyltransferase 1) regulates numerous proteins beyond histones, impacting cellular metabolism and transcriptional regulation. Loss of Hat1 significantly alters the mammalian acetylome, affecting key proteins like CBP and p53.

Keywords:
CBPHat1acetylationacetylomeacetyltransferasechromatinglycolysismitochondriap53proteomics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Lysine acetylation is a crucial post-translational modification regulating diverse biological processes.
  • The specific roles and targets of lysine acetyltransferases, such as Hat1 (histone acetyltransferase 1), are not fully elucidated.
  • Hat1 is known to acetylate histones, but its broader impact on the cellular acetylome requires investigation.

Purpose of the Study:

  • To comprehensively analyze the impact of Hat1 on the mammalian acetylome using an unbiased proteomics approach.
  • To identify Hat1-dependent acetylation targets and understand carbon source-dependent regulation of acetylation.
  • To investigate the role of Hat1 in regulating proteins involved in metabolism, transcription, and mitochondrial function.

Main Methods:

  • Utilized label-free quantitative proteomics to compare acetylomes of Hat1-proficient (Hat1+/+) and Hat1-deficient (Hat1-/-) mouse embryonic fibroblast cell lines.
  • Enriched acetylated peptides using acetyllysine affinity purification after trypsin digestion of whole cell extracts.
  • Cultured cells in glucose- and galactose-containing media to assess carbon source-dependent acetylation changes.

Main Results:

  • Identified significant carbon source-dependent alterations in the acetylome, particularly affecting enzymes in glycolysis.
  • Discovered 65 proteins with at least 2.5-fold decreased acetylation in Hat1-/- cells compared to Hat1+/+ cells.
  • Observed a substantial decrease (up to 20-fold) in the acetylation of CREB-binding protein (CBP) autoregulatory loop in Hat1-deficient cells, alongside affected acetylation of p53 and mitochondrial proteins.

Conclusions:

  • Hat1 plays a significant role in regulating the acetylation of a broad range of proteins, extending beyond histones.
  • Hat1-dependent acetylation is critical for metabolic regulation, transcriptional control, and potentially mitochondrial function.
  • The findings highlight Hat1 as a key regulator of the mammalian acetylome with implications for various cellular processes.