T hermotomaculum

Abstract

Ther.mo.to.ma'cu.lum. Gr. fem. n. thermê heat; L. neut. n. tomaculum , a kind of sausage; N.L. neut. n. Thermotomaculum , a sausage‐shaped thermophile. Acidobacteria / Holophagae / Thermotomaculales / Thermotomaculaceae / Thermotomaculum Gram‐stain‐negative, strictly anaerobic, long rods. Cells occur singly, as a group of 3–4 cells in a chain‐like structure, or as aggregates of up to 40–50 cells. Nonmotile. Strictly heterotrophic. Capable of fermentative growth on complex organic substrates such as yeast extract and tryptone peptone. Thermophilic and neutrophilic. The major fatty acids are iso‐C 15 :0 and iso‐C 17 :0 . The major quinones are menaquinone‐7 and ‐8. A member of the phylum Acidobacteria , the class Holophagae , the order Thermotomaculales , and the family Thermotomaculaceae . The known habitat is deep‐sea hydrothermal fields. DNA G + C content (mol%) : 51.6 (HPLC). Type species : Thermotomaculum hydrothermale Izumi, Nunoura, Miyazaki, Mino, Toki, Takai, et al. 2017, 4292 VP (Effective publication: Izumi, Nunoura, Miyazaki, Mino, Toki, Takai, et al. 2012, 251).

THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: Ion channels

“…Receptor heterogeneity within each class arises from the homo-oligomeric, or hetero-oligomeric, assembly of distinct subunits into cation-selective tetramers. Each subunit of the tetrameric complex comprises an extracellular amino terminal domain (ATD), an extracellular ligand binding domain (LBD), three transmembrane domains composed of three membrane spans (M1, M3 and M4), a channel lining re-entrant 'p-loop' (M2) located between M1 and M3 and an intracellular carboxy-terminal domain (CTD) [458,523,639,691,997]. The X-ray structure of a homomeric ionotropic glutamate receptor (GluA2 -see below) has recently been solved at 3.6Å resolution [919] and although providing the most complete structural information current available may not representative of the subunit arrangement of, for example, the heteromeric NMDA receptors [466].…”

Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism

“…[35][36] This competitive dynamic is regulated, in part, by the removal of acetyl and succinyl groups from lysine residues by the activity of sirtuins, which deacylate lysine residues throughout the cell. 37 The quantitation of lysine acetyl and succinyl competition has yet to be performed for either dietary (starvation or ethanol) or genetic (sirtuin knockout) in vivo models at the same time.…”

“…Sirtuins are a highly conserved family of nicotinamide adenine dinucleotide (NAD+)dependent deacylases with homology to the yeast Sir2 protein. 37 Sirtuin 3 (SIRT3) is the predominant regulator of mitochondrial lysine acetylation, while sirtuin 5 (SIRT5) is the major regulator of lysine succinylation. [38][39] Each are known to be involved in a variety of pathologies, including nonalcoholic fatty liver disease (NAFLD), diabetes, cardiovascular disease, cancer, neurodegeneration, and aging.…”