Results 91 to 100 of about 4,851 (193)
Emerging processing technologies can do more than inactivate microorganisms; under controlled sublethal conditions, they reprogram microbial physiology and metabolism. This review highlights the underlying mechanisms, technological opportunities, and current challenges for designing next‐generation fermented dairy products with improved functionality ...
Sepehrdad Dehghani +4 more
wiley +1 more source
Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation [PDF]
AbstractIGF‐motif loops project from the hexameric ring of ClpX and are required for docking with the self‐compartmentalized ClpP peptidase, which consists of heptameric rings stacked back‐to‐back. Here, we show that ATP or ATPγS support assembly by changing the conformation of the ClpX ring, bringing the IGF loops closer to each other and allowing ...
Amor, Alvaro J. +3 more
openaire +4 more sources
Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria [PDF]
Loss-of-function mutations in genes for heme biosynthetic enzymes can give rise to congenital porphyrias, eight forms of which have been described. The genetic penetrance of the porphyrias is clinically variable, underscoring the role of additional ...
Kardon, Julia +36 more
core +1 more source
Meiosis is the process of producing haploid gametes through a series of complex chromosomal events and the coordinated action of various proteins. The mitochondrial protease complex (ClpXP), which consists of caseinolytic mitochondrial matrix peptidase X
Hai-Wei Feng +4 more
doaj +1 more source
Aged mouse skeletal muscle exhibits greater mtUPR transcriptional initiation following repeated physical stress than young mice, coinciding with reduced mitochondrial proteostatic reserve and heightened oxidative burden. We implicate a mtROS‐JNK‐CHOP axis as a contributor to the enhanced response.
Grant R. Laskin +2 more
wiley +1 more source
Human Mitochondrial ClpP Is a Stable Heptamer That Assembles into a Tetradecamer in the Presence of ClpX [PDF]
The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a hollow-cored particle composed of two heptameric rings joined face-to-face forming an aqueous chamber containing the proteolytic active sites. We have found that isolated human mitochondrial ClpP (hClpP) is stable as a heptamer and remains a monodisperse species
Sung Gyun, Kang +4 more
openaire +2 more sources
Staphylococcus aureus ClpX localizes at the division septum and impacts transcription of genes involved in cell division, T7-secretion, and SaPI5-excision [PDF]
In all living cells, molecular chaperones are essential for facilitating folding and unfolding of proteins. ClpX is a highly conserved ATP-dependent chaperone that besides functioning as a classical chaperone can associate with ClpP to form the ClpXP ...
Frees, Dorte +4 more
core +1 more source
AAA+ protein unfoldases—the Moirai of the proteome
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley +1 more source
Extracytoplasmic function Ï factors that are stress inducible are often sequestered in an inactive complex with a membrane-associated anti-Ï factor. Mycobacterium tuberculosis membrane-associated anti-Ï factors have a small, stable RNA gene A (ssrA ...
Gopal, B +5 more
core +1 more source
Identifying Subcellular Structure Components in Escherichia Coli by Crosslinking and SEC‐MS
ABSTRACT Cells are comprised of a broad spectrum of structures that compartmentalize biochemical and signaling mechanisms. These structures can be comprised of many biomolecules, but especially lipids, proteins, and nucleic acids. Techniques are limited to quantify or discover new subcellular structures.
Rachel A. Victor +3 more
wiley +1 more source

