Lon protease

Lon pro·te·ase

(lohn),
an enzyme that degrades a bacterial protein and stops cell division until chromosomal repair is completed.
References in periodicals archive ?
A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation.
There are (a) the ATP-dependent proteases, namely, the LON protease and the Clp Protease Proteolytic subunit (CLPP) and the mitochondrial AAA (ATPases Associated with diverse cellular Activities) proteases of the inner mitochondrial membrane and matrix; (b) the two ATP independent proteases, the ATP23 and HtrA2; and (c) two oligopeptidases, namely, the presequence protease (PITRM1, also known as PreP) and the mitochondrial oligopeptidase M (MEP, also known as neurolysin) [53] (Figure 1).
LON Protease. The LON protease, firstly identified in bacteria as La protein [54], is conserved among prokaryotes and eukaryotes.
Finally, LON protease has been associated with mitochondrial DNA regulation.
Under normal conditions, ATFS-1 is imported in mitochondria and degraded by the LON protease [150].
On the other hand, mitophagy is enhanced by accumulation of unfolded proteins in the mitochondrial matrix or down-regulation of the LONP1 peptidase (Human LON protease homolog) [227, 228].
HIF1[alpha] binds to genomic hypoxia-responsive elements promoting the expression of a large number of genes including glycolytic enzymes and pyruvate dehydrogenase kinase-1 (PDK1 inhibits conversion of pyruvate to acetyl CoA) and it also inhibits LON protease that (among others) degrades COX4-1 subunit [62, 290, 291].
Lee et al., "Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber," The EMBO Journal, vol.
coli Lon protease at 1.9 A resolution," Journal of Structural Biology, vol.
Wang, "Oxygen-sensitive mitochondrial accumulation of cystathionine [beta]-synthase mediated by Lon protease," Proceedings of the National Academy of Sciences of the United States of America, vol.
Washington, August 31 (ANI): The availability of an enzyme, known as the Lon protease, that protects cells from oxidative damage, declines as the body ages, a new study has found.
ATP dependent proteases include the Lon proteases (Piml in yeast) and caseinolytic peptidases (ClpP) in the matrix, and the AAA+ family of proteases which are mostly present on the inner membrane.