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Acyl phosphates of ATP (ATPAc) and related nucleotides have proven useful for the interrogation of known nucleotide binding sites via specific acylation of conserved lysines (K). In addition, occasional K-acylations are identified in proteins without such known sites. Here we present a robust and specific acylation of procaspase-6 by ATPAc at K133 in Jurkat cell lysates. The K133 acylation is dependent on π-π stacking interactions between the adenine moiety of ATPAc and a conserved Y198-Y198 site formed at the homodimeric interface of procaspase-6. Significantly, the Y198A mutation in procaspase-6 abolishes K133 acylation but has no effect on the proteolytic activity of the mature, active caspase-6 Y198A variant. Additional in vitro studies show that ATP can inhibit the auto-proteolytic activation of procaspase-6. These observations suggest that ATP, and possibly other nucleotides, may serve as the endogenous ligands for the allosteric site at the procaspase-6 dimer interface, a site which has persisted in "orphan" status for over a decade.
This article was published in the following journal.
The transcriptional anti-silencing and DNA-binding protein, VirB, is essential for the virulence of species and, yet, sequences required for VirB-DNA binding are poorly understood. While a 7-8 bp Vir...
The cytosolic iron sulfur cluster assembly (CIA) scaffold, comprising Nbp35 and Cfd1 in yeast, assembles iron sulfur (FeS) clusters destined for cytosolic and nuclear enzymes. ATP hydrolysis by the CI...
The cytosolic iron sulfur cluster assembly (CIA) scaffold biosynthesizes iron sulfur cluster cofactors for enzymes residing in the cytosol and the nucleus. In fungi and animals, it comprises two homol...
Malaria remains a worldwide concern in terms of morbidity and mortality. Limited understanding of Plasmodium proteome makes it challenging to control malaria. Understanding of the expression and funct...
APOBEC3s proteins (A3s), a family of human cytidine deaminases, protect the host from endogenous retro-elements and exogenous viral infections by introducing hypermutations. However, overexpressed A3s...
Ghrelin (growth hormone release inducer) is produced in the stomach. The active form of Ghrelin is Acyl-Ghrelin. Acyl-Ghrelin stimulates the Ghrelin receptors. Ghrelin receptors are detect...
Plasma histidine-rich glycoprotein (HRG) binds to platelets in the presence of zinc (1). This binding is totally blocked by a monoclonal antibody directed against platelet membrane CD36. ...
N-acyl-phosphatidylethanolamine (NAPEs) and their active metabolites, N-acyl-ethanolamides (NAEs) are lipid satiety factors that are normally biosynthesized in the intestinal tract in resp...
Compare chronic (one week) of a 'normal' meat diet with one week of mycoprotein consumption, with or without a reduced nucleotide content, on markers of metabolic health, such as uric acid...
The production of protein rich animal products is associated with a large environmental burden, and with ethical considerations. Additionally, the over-consumption of meat might be associa...
The small ribonucleoprotein component of RIBOSOMES. It contains the MESSENGER RNA binding site and two TRANSFER RNA binding sites - one for the incoming AMINO ACYL TRNA (A site) and the other (P site) for the peptidyl tRNA carrying the elongating peptide chain.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 18.104.22.168.
A group of compounds which consist of a nucleotide molecule to which an additional nucleoside is attached through the phosphate molecule(s). The nucleotide can contain any number of phosphates.
An 86-amino acid polypeptide, found in central and peripheral tissues, that displaces diazepam from the benzodiazepine recognition site on the gamma-aminobutyric acid receptor (RECEPTORS, GABA). It also binds medium- and long-chain acyl-CoA esters and serves as an acyl-CoA transporter. This peptide regulates lipid metabolism.
An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.