Results 101 to 110 of about 4,851 (193)

Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine. [PDF]

Biomolecules
AAA+ ATPases are ring-shaped hexameric protein complexes that operate as elaborate macromolecular motors, driving a variety of ATP-dependent cellular processes. AAA+ ATPases undergo large-scale conformational changes that lead to the conversion of chemical energy from ATP into mechanical work to perform a wide range of functions, such as unfolding and ...
Audibert A, Boisbouvier J, Vermot A.
europepmc   +3 more sources

Systematic Engineering of Proteases in Saccharopolyspora Spinosa Reveals Synergistic Enhancement of Spinosad Biosynthesis via Substrate Flux Optimization

Advanced Science, Volume 13, Issue 20, 9 April 2026.
ARTP mutagenesis yielded Saccharopolyspora spinosa mutant D184 with improved extracellular nitrogen utilization. An integrated workflow of protease genetic manipulation, multi‐omics, and rational synergy design pinpointed a pepP‐clpP‐htpX synergistic triangular combination.
Duo Jin, Wangqiong Chen, Danlu Yang, Qing Liu, Baolong Bai, Zirui Dai, Xirong Liu, Zirong Zhu, Jie Rang, Liqiu Xia   +9 more
wiley   +1 more source

Identification of the ClpX Regulon in Staphylococcus aureus

, 2006
Staphyloccous aureus is a major human pathogen capable of causing a wide spectrum of infections ranging from superficial wound infections to life-threatening endocarditis and toxic shock syndrome. Essential for S.
Jelsbak, Lotte, Ingmer, Hanne, Donat, Stefanie, Frees, Dorte, Ohlsen, Knut, Thomsen, Line Elnif   +5 more
core   +1 more source

Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding

eLife, 2019
Most AAA+ remodeling motors denature proteins by pulling on the peptide termini of folded substrates, but it is not well-understood how motors produce grip when resisting a folded domain.
Tristan A Bell, Tania A Baker, Robert T Sauer   +2 more
doaj   +1 more source

Of Commensals and Opportunists: Genomics of Coagulase‐Negative Staphylococci During Sequential Ear and Eye Infections in a Healthy Adult

MicrobiologyOpen, Volume 15, Issue 2, April 2026.
The genomes of coagulase‐negative staphylococci (CoNS) isolated during sequential ear and eye infections in a healthy adult are analyzed. We highlight the identification of a community‐acquired S. capitis subsp. urealyticus ST1 lineage carrying a mosaic SCCmec IV element, linking common skin commensals to multidrug‐resistant strains associated with ...
Soo Sum Lean, Chew Chieng Yeo, Zain Illyaaseen, Sargit Kaur, Yun Fong Ngeow, Stuart C. Clarke, Hien Fuh Ng   +6 more
wiley   +1 more source

CLPP-Null Eukaryotes with Excess Heme Biosynthesis Show Reduced L-arginine Levels, Probably via CLPX-Mediated OAT Activation

Biomolecules
The serine peptidase CLPP is conserved among bacteria, chloroplasts, and mitochondria. In humans and mice, its loss causes Perrault syndrome, which presents with growth deficits, infertility, deafness, and ataxia.
Jana Key, Suzana Gispert, Arvind Reddy Kandi, Daniela Heinz, Andrea Hamann, Heinz D. Osiewacz, David Meierhofer, Georg Auburger   +7 more
doaj   +1 more source

Towards understanding the functions of the GroEL and ClpX chaperone systems in Escherichia coli [PDF]

, 2004
Molecular chaperones are proteins that assist in folding, refolding, disaggregation, or degradation of other proteins in the cell. This thesis includes studies of two bacterial chaperones, GroEL, which mediates protein folding, and ClpX, which mediates ...
Davidson, Toni
core   +1 more source

A mitochondrial insertion directs substrate selection and engagement by ClpX

ABSTRACT The force-generating AAA+ ATPase domain of protein unfoldases is specified for many substrates and other functional partners through elaboration with accessory domains. Mitochondrial homologs of the unfoldase ClpX contain an insertion within the AAA+ domain that is absent in bacterial homologs.
Adam DeCosta, Rebecca Barrick, Julia R. Kardon   +2 more
openaire   +2 more sources

The function of ClpX chaperone in bacteria [PDF]

, 2020
Intracellular proteolysis is an essential regulatory process that affects cellular physiology. Since proteolysis destroys proteins irreversibly, this process must be strictly controlled.
Kýr, Jan
core  

delta_clpX czcD::clpX grown at 37 C on pH 7.0 C+Y + 1 % agarose

Depleted ClpX strain of delta_clpX czcD::clpX grown at 37 C on pH 7.0 C+Y with 1 % agarose for at least 76 hours. Images acquired every 5 minutes. FPS is 3.
Viktor Hundtofte Mebus (18096871)
core   +1 more source