ArticleThe Journal of biological chemistry2019
A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 9 citations in OpenAlex.
- Deletion ofFrontiers in microbiology · 2022Article
- Targeting the SAGA and ATAC Transcriptional Coactivator Complexes in MYC-Driven Cancers.Cancer research · 2020Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
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Abstract
Gcn5 and sirtuins are highly conserved histone acetyltransferase (HAT) and histone deacetylase (HDAC) enzymes that were first characterized as regulators of gene expression. Although histone tails are important substrates of these enzymes, they also target many nonhistone proteins that function in diverse biological processes. However, the mechanisms used by these enzymes to choose their nonhistone substrates are unknown. Previously, we used SILAC-based MS to identify novel nonhistone substrates of Gcn5 and sirtuins in yeast and found a shared target consensus sequence. Here, we use a synthetic biology approach to demonstrate that this consensus sequence can direct acetylation and deacetylation targeting by these enzymes
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