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MetabolomicsLysine acetyltransferase Rv0998 coordinates transcriptional and metabolic adaptation of Mycobacterium tuberculosis to acidic pH

Mycobacterium tuberculosis (Mtb) survives host defences by adapting to host conditions, including acid stress, during infection. A critical survival strategy involves pH homeostasis, mediated by complex signalling systems that regulate metabolic reprogramming and stress responses. While ...

2026-09-03 | MTBLS15171 | MetaboLights
TranscriptomicsToxoplasma gondii lysine acetyltransferase GCN5-A functions in the cellular response to alkaline stress and expression of cyst genes
Parasitic protozoa such as the apicomplexan Toxoplasma gondii progress through their life cycle in response to stimuli in the environment or host organism. Very little is known about how proliferating tachyzoites reprogram their expressed genome in response to stresses that prompt development into ...
ORGANISM(S): Toxoplasma gondii 
2011-05-25 | E-GEOD-22100 | biostudies-arrayexpress
ProteomicsChemical proteomics profiling of N-terminal and lysine acetyltransferases
Acetylation of amino groups is a prevalent protein modification in all kingdoms of life. Acetyl groups are transferred from Coenzyme A (CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA ...
ORGANISM(S): Homo Sapiens (human) 
2021-04-14 | PXD018544 | JPOST Repository
ProteomicsGlobal profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis
Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them sha...
ORGANISM(S): Escherichia Coli 
2020-07-07 | PXD015875 | JPOST Repository
ProteomicsInvestigating peptide-Coenzyme A-conjugates as chemical probes for proteomic profiling of N-terminal and lysine acetyltransferases
Acetyl groups are transferred from Acetyl-Coenzyme A (Ac-CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA conjugates as KAT probes, we have synthesized peptide probes with CoA conjugate...
ORGANISM(S): Homo Sapiens (human) 
2022-05-02 | PXD032957 | JPOST Repository
GenomicsLoss of PHF20 does not negatively affect deposition of H4K16 acetylation, but does impact the expression of MOF targets
Protein post-translational modifications transmit signals in part by creating binding sites for effector molecules. This is especially true in epigenetic pathways where histone tails are heavily modified, resulting in the recruitment of molecules that can affect transcription. One such molecule, pla...
ORGANISM(S): Mus musculus 
2012-02-27 | E-GEOD-29306 | biostudies-arrayexpress
ProteomicsParalogue-selective degradation of the lysine acetyltransferase EP300
This contains the raw data for global proteomic profiling described in the paper "Paralogue-selective degradation of the lysine acetyltransferase EP300"
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-05-30 | MSV000094896 | MassIVE
TranscriptomicsInhibition of p300 Lysine Acetyltransferase activity by Luteolin reduces tumor growth in head and neck squamous cell carcinoma (HNSCC) xenograft mouse model [mRNA]
Chromatin acetylation is attributed with distinct functional relevance with respect to gene expression in normal and diseased conditions thereby leading to a topical interest in the concept of epigenetic modulators and therapy. We report here the identification and characterization of the acetylatio...
ORGANISM(S): Homo sapiens 
2016-07-05 | E-GEOD-75029 | biostudies-arrayexpress
ProteomicsTargeted degradation of the enhancer lysine acetyltransferases CBP and p300
The enhancer factors CBP/p300 maintain gene expression programs through lysine acetylation of chromatin and transcriptional regulators and by scaffolding functions mediated by several protein-protein interaction domains. We have designed dCBP-1, a compound that induces degradation of CBP/p300, and ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-11-15 | MSV000086457 | MassIVE
ProteomicsThe state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes
The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the t...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD044167 | JPOST Repository
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