ArticleProceedings of the National Academy of Sciences of the United States of America2013
mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed.
- Maize unstable factor for orange1 encodes a nuclear protein that affects redox accumulation during kernel development.The Plant cell · 2024Article
- Uncovering the Role of the Yeast Lysine Acetyltransferase NuA4 in the Regulation of Nuclear Shape and Lipid Metabolism.Molecular and cellular biology · 2024Article
- Perturbed fatty-acid metabolism is linked to localized chromatin hyperacetylation, increased stress-response gene expression and resistance to oxidative stress.PLoS genetics · 2023Article
- A balancing act: interactions within NuA4/TIP60 regulate picNuA4 function in Saccharomyces cerevisiae and humans.Genetics · 2022Article
- Article
- Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism.Toxins · 2022Review
- Gds1 Interacts with NuA4 To Promote H4 Acetylation at Ribosomal Protein Genes.Molecular and cellular biology · 2022Article
- The SAGA and NuA4 component Tra1 regulates Candida albicans drug resistance and pathogenesis.Genetics · 2021Article
- Phenomic screen identifies a role for the yeast lysine acetyltransferase NuA4 in the control of Bcy1 subcellular localization, glycogen biosynthesis, and mitochondrial morphology.PLoS genetics · 2020Article
- NuA4 acetyltransferase is required for efficient nucleotide excision repair in yeast.DNA repair · 2019Article
- The Pseudokinase Domain ofG3 (Bethesda, Md.) · 2018Article
- Molecular Architecture of the Essential Yeast Histone Acetyltransferase Complex NuA4 Redefines Its Multimodularity.Molecular and cellular biology · 2018Article
- Architecture of the Saccharomyces cerevisiae NuA4/TIP60 complex.Nature communications · 2018Article
- Critical genomic regulation mediated by Enhancer of Polycomb.Current genetics · 2018Review
- YHMI: a web tool to identify histone modifications and histone/chromatin regulators from a gene list in yeast.Database : the journal of biological databases and curation · 2018Article
- Budding yeast Wee1 distinguishes spindle pole bodies to guide their pattern of age-dependent segregation.Nature cell biology · 2017Article
- Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes.BMC genomics · 2017Article
- Article
- Lysine acetyltransferase NuA4 and acetyl-CoA regulate glucose-deprived stress granule formation in Saccharomyces cerevisiae.PLoS genetics · 2017Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
13 authors.
Funding
Abstract
Recent global proteomic and genomic studies have determined that lysine acetylation is a highly abundant posttranslational modification. The next challenge is connecting lysine acetyltransferases (KATs) to their cellular targets. We hypothesize that proteins that physically interact with KATs may not only predict the cellular function of the KATs but may be acetylation targets. We have developed a mass spectrometry-based method that generates a KAT protein interaction network from which we simultaneously identify both in vivo acetylation sites and in vitro acetylation sites. This modified chromatin-immunopurification coupled to an in vitro KAT assay with mass spectrometry (mChIP-KAT-MS) was applied to the Saccharomyces cerevisiae KAT nucleosome acetyltransferase of histone H4 (NuA4). Using mChIP-KAT-MS, we define the NuA4 interactome and in vitro-enriched acetylome, identifying over 70 previously undescribed physical interaction partners for the complex and over 150 acetyl lysine residues, of which 108 are NuA4-specific in vitro sites. Through this method we determine NuA4 acetylation of its own subunit Epl1 is a means of self-regulation and identify a unique link between NuA4 and the spindle pole body. Our work demonstrates that this methodology may serve as a valuable tool in connecting KATs with their cellular targets.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.