Mitochondrial quality control proteases and their modulation for cancer therapy

J Zhang, W Qiao, Y Luo - Medicinal Research Reviews, 2023 - Wiley Online Library
Mitochondria, the main provider of energy in eukaryotic cells, contains more than 1000
different proteins and is closely related to the development of cells. However, damaged …

Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules

MF Mabanglo, WA Houry - Journal of Biological Chemistry, 2022 - ASBMB
ClpP is a highly conserved serine protease that is a critical enzyme in maintaining protein
homeostasis and is an important drug target in pathogenic bacteria and various cancers. In …

Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications

Nitika, B Zheng, L Ruan, JT Kline, S Omkar… - PLoS …, 2022 - journals.plos.org
Hsp70 interactions are critical for cellular viability and the response to stress. Previous
attempts to characterize Hsp70 interactions have been limited by their transient nature and …

Non-canonical amino acids in analyses of protease structure and function

P Goettig, NG Koch, N Budisa - International Journal of Molecular …, 2023 - mdpi.com
All known organisms encode 20 canonical amino acids by base triplets in the genetic code.
The cellular translational machinery produces proteins consisting mainly of these amino …

Translation fidelity and respiration deficits in CLPP-deficient tissues: mechanistic insights from mitochondrial complexome profiling

J Key, S Gispert, G Koepf, J Steinhoff-Wagner… - International journal of …, 2023 - mdpi.com
The mitochondrial matrix peptidase CLPP is crucial during cell stress. Its loss causes
Perrault syndrome type 3 (PRLTS3) with infertility, neurodegeneration, and a growth deficit …

Structure and the mode of activity of Lon proteases from diverse organisms

A Wlodawer, B Sekula, A Gustchina… - Journal of molecular …, 2022 - Elsevier
Lon proteases, members of the AAA+ superfamily of enzymes, are key components of the
protein quality control system in bacterial cells, as well as in the mitochondria and other …

[PDF][PDF] Protein model refinement for cryo-EM maps using AlphaFold2 and the DAQ score

G Terashi, X Wang, D Kihara - Acta Crystallographica Section D …, 2023 - journals.iucr.org
As more protein structure models have been determined from cryogenic electron microscopy
(cryo-EM) density maps, establishing how to evaluate the model accuracy and how to …

AAA+ protease-adaptor structures reveal altered conformations and ring specialization

S Kim, X Fei, RT Sauer, TA Baker - Nature structural & molecular …, 2022 - nature.com
ClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor.
Here we present high-resolution cryo-EM structures of Escherichia coli ClpAPS complexes …

Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex

S Li, KY Hsieh, CI Kuo, SC Su, KF Huang, K Zhang… - Science …, 2021 - science.org
The Lon protease is the prototype of a family of proteolytic machines with adenosine
triphosphatase modules built into a substrate degradation chamber. Lon is known to …

Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate

M Rüttermann, M Koci, P Lill, ED Geladas… - Nature …, 2023 - nature.com
The double-ring AAA+ ATPase Pex1/Pex6 is required for peroxisomal receptor recycling
and is essential for peroxisome formation. Pex1/Pex6 mutations cause severe peroxisome …