Results 51 to 60 of about 9,876 (190)

Structural insights into the Clp protein degradation machinery

mBio
The Clp protease system is important for maintaining proteostasis in bacteria. It consists of ClpP serine proteases and an AAA+ Clp-ATPase such as ClpC1.
Xiaolong Xu, Yanhui Wang, Wei Huang, Danyang Li, Zixin Deng, Feng Long   +5 more
doaj   +1 more source

ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP

eLife, 2020
AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase.
Sora Kim, Kristin L Zuromski, Tristan A Bell, Robert T Sauer, Tania A Baker   +4 more
doaj   +1 more source

Reprogramming of the Caseinolytic Protease by ADEP Antibiotics: Molecular Mechanism, Cellular Consequences, Therapeutic Potential

Frontiers in Molecular Biosciences, 2021
Rising antibiotic resistance urgently calls for the discovery and evaluation of novel antibiotic classes and unique antibiotic targets. The caseinolytic protease Clp emerged as an unprecedented target for antibiotic therapy 15 years ago when it was ...
Heike Brötz-Oesterhelt, Heike Brötz-Oesterhelt, Andreas Vorbach   +2 more
doaj   +1 more source

The ClpXP protease and the ClpX unfoldase control virulence, cell division, and autolysis in Streptococcus pneumoniae

Microbiology Spectrum
In all living cells, molecular chaperones and ATP-dependent proteases are essential for protein homeostasis. The ClpXP protease is a chaperone-protease complex conserved between bacteria and mitochondria.
Viktor H. Mebus, Supradipta De, Larissa M. Busch, Manuela Gesell Salazar, Rabea Schlüter, Uwe Völker, Sven Hammerschmidt, Dorte Frees   +7 more
doaj   +1 more source

The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1. [PDF]

PLoS ONE, 2015
Clp chaperone-proteases are cylindrical complexes built from ATP-dependent chaperonerings that stack onto a proteolytic ClpP double-ring core to carry out substrate protein degradation.Interaction of the ClpP particle with the chaperone is mediated by an
Julia Leodolter, Jannis Warweg, Eilika Weber-Ban   +2 more
doaj   +1 more source

Segregation of molecules at cell division reveals native protein localization [PDF]

, 2014
We introduce a non-intrusive method exploiting post-division single-cell variability to validate protein localization. The results show that Clp proteases, widely reported to form biologically relevant foci, are in fact uniformly distributed inside ...
Baker, Tania A., Chien, Peter, Landgraf, Dirk, Okumus, Burak, Paulsson, Johan   +4 more
core   +1 more source

Mechanochemical basis of protein degradation by a double-ring AAA+ machine [PDF]

, 2014
Molecular machines containing double or single AAA+ rings power energy-dependent protein degradation and other critical cellular processes, including disaggregation and remodeling of macromolecular complexes.
A Martin, A Martin, A Roll-Mecak, Adrian O Olivares, AF Neuwald, Andrew R Nager, AR Nager, BM Stinson, C Zhao, CM Farrell, DA Dougan, DH Wolf, DM Smith, E Gur, E Gur, EM De La Cruz, EU Weber-Ban, F Guo, F Wang, J Hinnerwisch, J Liu, JA Kenniston, JC Cordova, JM Flynn, JM Miller, JW Kerssemakers, M Carrion-Vazquez, M Sen, MC Bewley, ME Aubin-Tam, ME Aubin-Tam, MR Maurizi, ND Werbeck, Ohad Iosefson, P Koodathingal, R Grimaud, RA Maillard, Robert T Sauer, RT Sauer, S Cranz-Mileva, SD Moore, SE Glynn, SM Doyle, T Ogura, Tania A Baker, W Kress, Y Katayama, YI Kim, Z Maglica   +48 more
core   +1 more source

Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria [PDF]

, 2017
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 ...
Baker, Tania, Bergonia, Hector A., Ducamp, Sarah, Gouya, Laurent, Kafina, Martin D., Kannengiesser, Caroline, Kardon, Julia R., Karim, Zoubida, Manceau, Hana, Nicolas, Gaël, Paw, Barry H., Phillips, John D., Puy, Hervé, van der Vorm, Lisa N., Yien, Yvette Y.   +14 more
core   +3 more sources

α-Amino Diphenyl Phosphonates as Novel Inhibitors of Escherichia coli ClpP Protease [PDF]

Journal of Medicinal Chemistry, 2018
Increased Gram-negative bacteria resistance to antibiotics is becoming a global problem, and new classes of antibiotics with novel mechanisms of action are required. The caseinolytic protease subunit P (ClpP) is a serine protease conserved among bacteria that is considered as an interesting drug target. ClpP function is involved in protein turnover and
Carlos Moreno-Cinos, Elisa Sassetti, Irene G. Salado, Gesa Witt, Siham Benramdane, Laura Reinhardt, Cristina D. Cruz, Jurgen Joossens, Pieter Van der Veken, Heike Brötz-Oesterhelt, Päivi Tammela, Mathias Winterhalter, Philip Gribbon, Björn Windshügel, Koen Augustyns   +14 more
openaire   +3 more sources

A LON-ClpP Proteolytic Axis Degrades Complex I to Extinguish ROS Production in Depolarized Mitochondria [PDF]

, 2016
Mitochondrial dysfunction is implicated in numerous neurodegenerative disorders and in Parkinson’s disease (PD) in particular. PINK1 and Parkin gene mutations are causes of autosomal recessive PD, and these respective proteins function cooperatively to ...
Pryde, KR, Schapira, AH, Taanman, JW
core   +1 more source