ArticleACS chemical biology2010
Peptide arrays identify isoform-selective substrates for profiling endogenous lysine deacetylase activity.
Article in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 89 citations in OpenAlex.
- Lysine Deacetylase Substrate Selectivity: Distinct Interaction Surfaces Drive Positive and Negative Selection for Residues Following Acetyllysine.Biochemistry · 2023Article
- 9-Cyano-10-telluriumpyronin Derivatives as Red-light-activatable Raman Probes.Chemistry, an Asian journal · 2023Article
- Advances in high-throughput mass spectrometry in drug discovery.EMBO molecular medicine · 2023Review
- Endogenous expression of inactive lysine deacetylases reveals deacetylation-dependent cellular mechanisms.PloS one · 2023Article
- NADH inhibition of SIRT1 links energy state to transcription during time-restricted feeding.Nature metabolism · 2021Article
- Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8.Biochemistry · 2021Article
- Label-Free Screening of SARS-CoV-2 NSP14 Exonuclease Activity Using SAMDI Mass Spectrometry.SLAS discovery : advancing life sciences R & D · 2021Article
- Hydroxamic acid-modified peptide microarrays for profiling isozyme-selective interactions and inhibition of histone deacetylases.Nature communications · 2021Article
- HDAC3 deacetylates the DNA mismatch repair factor MutSβ to stimulate triplet repeat expansions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Temporal Sampling of Enzymes from Live Cells by Localized Electroporation and Quantification of Activity by SAMDI Mass Spectrometry.Small (Weinheim an der Bergstrasse, Germany) · 2020Article
- Article
- Profiling Protein Tyrosine Phosphatase Specificity with Self-Assembled Monolayers for Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry and Peptide Arrays.ACS combinatorial science · 2019Article
- Label-Free Assay of Protein Tyrosine Phosphatase Activity in Single Cells.Analytical chemistry · 2019Article
- Joker de Bruijn: Covering k-Mers Using Joker Characters.Journal of computational biology : a journal of computational molecular cell biology · 2018Article
- Traceless Immobilization of Analytes for High-Throughput Experiments with SAMDI Mass Spectrometry.Journal of the American Chemical Society · 2018Article
- Purification of metal-dependent lysine deacetylases with consistently high activity.Protein expression and purification · 2018Article
- Chelatable trace zinc causes low, irreproducible KDAC8 activity.Analytical biochemistry · 2018Article
- Combining SAMDI Mass Spectrometry and Peptide Arrays to Profile Phosphatase Activities.Methods in enzymology · 2018Article
- HDAC8 substrate selectivity is determined by long- and short-range interactions leading to enhanced reactivity for full-length histone substrates compared with peptides.The Journal of biological chemistry · 2017Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
This paper reports the development of a class of isoform-selective peptide substrates for measuring endogenous lysine deacetylase (KDAC) activities in cell culture. The peptides were first identified by comparing the substrate specificity profiles of the four KDAC isoforms KDAC2, KDAC3, KDAC8, and sirtuin 1 (SIRT1) on a 361-member hexapeptide array wherein the two C-terminal residues to the acetylated lysine were varied. The arrays were prepared by immobilizing the peptides to a self-assembled monolayer of alkanethiolates on gold and could therefore be analyzed by a mass spectrometry technique termed SAMDI (self-assembled monolayers for matrix assisted laser desorption/ionization time-of-flight mass spectrometry). Arrays presenting the selective substrates were treated with nuclear extracts from HeLa, Jurkat, and smooth muscle cells and analyzed to measure endogenous deacetylase activities. We then use the arrays to profile KDAC activity through the HeLa cell cycle. We find that the activity profile of the KDAC3 selective peptide closely mirrors the changing acetylation state of the H4 histone, suggesting a role for this enzyme in cell cycle regulation. This work is significant because it describes a general route for identifying selective substrates that can be used to understand the differential roles of members of the deacetylase enzyme family in complex biological processes and further because the label-free approach avoids perturbation of enzyme activity that has plagued fluorescence-based assays.
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