Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease. [PDF]
Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape. The dysregulation of these mitochondrial proteins is linked to a range of human metabolic disorders.
Rowland EA, Snowden CK, Cristea IM.
europepmc +6 more sources
Protein lipoylation in mitochondria requires Fe-S cluster assembly factors NFU4 and NFU5. [PDF]
Abstract Plants have evolutionarily conserved NifU (NFU)-domain proteins that are targeted to plastids or mitochondria. “Plastid-type” NFU1, NFU2, and NFU3 in Arabidopsis (Arabidopsis thaliana) play a role in iron–sulfur (Fe–S) cluster assembly in this organelle, whereas the type-II NFU4 and NFU5 proteins have not been subjected to ...
Przybyla-Toscano J +7 more
europepmc +10 more sources
Genetic dissection of the mitochondrial lipoylation pathway in yeast [PDF]
Background Lipoylation of 2-ketoacid dehydrogenases is essential for mitochondrial function in eukaryotes. While the basic principles of the lipoylation processes have been worked out, we still lack a thorough understanding of the details of this ...
Laura P. Pietikäinen +4 more
doaj +3 more sources
Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum. [PDF]
Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways.
Svenja Günther +8 more
doaj +2 more sources
Mitochondrial Protein Lipoylation and the 2-Oxoglutarate Dehydrogenase Complex Controls HIF1α Stability in Aerobic Conditions. [PDF]
Hypoxia-inducible transcription factors (HIFs) control adaptation to low oxygen environments by activating genes involved in metabolism, angiogenesis, and redox homeostasis. The finding that HIFs are also regulated by small molecule metabolites highlights the need to understand the complexity of their cellular regulation.
Burr SP +10 more
europepmc +4 more sources
LipoFNT: Lipoylation Sites Identification with Flexible Neural Tree
Lysine lipoylation is a special type of posttranslational modification in both prokaryotes’ and eukaryotes’ proteomics researches. Such a modification takes part in several significant biological processions and plays a key role in the cellular level. In
Wenzheng Bao +3 more
doaj +2 more sources
The amidase domain of lipoamidase specifically inactivates lipoylated proteins in vivo.
BackgroundIn the 1950s, Reed and coworkers discovered an enzyme activity in Streptococcus faecalis (Enterococcus faecalis) extracts that inactivated the Escherichia. coli and E.
Maroya D Spalding, Sean T Prigge
doaj +3 more sources
Chemical Tagging of Protein Lipoylation
AbstractProtein lipoylation is a post‐translational modification of emerging importance in both prokaryotes and eukaryotes. However, labeling and large‐scale profiling of protein lipoylation remain challenging. Here, we report the development of iLCL (iodoacetamide‐assisted lipoate‐cyclooctyne ligation), a chemoselective reaction that enables chemical ...
Qi Tang +3 more
core +4 more sources
Methionine restriction (MR) provides metabolic benefits in many organisms. However, mechanisms underlying the MR-induced effect remain incompletely understood. Here, we show in the budding yeast S.
Wen Fang +8 more
doaj +2 more sources
Ferredoxins: master regulators in mitochondrial redox homeostasis and programmed cell death [PDF]
Ferredoxins (FDXs) are evolutionarily conserved iron-sulfur (Fe–S) proteins that serve as master regulators of mitochondrial redox homeostasis, governing critical processes including electron transfer, energy metabolism, Fe–S cluster biogenesis, and ...
Yajuan Lu +13 more
doaj +2 more sources

