Results 41 to 50 of about 7,556 (201)

Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain [PDF]

, 2013
Mitochondrial maintenance crucially depends on the quality control of proteins by various chaperones, proteases and repair enzymes. While most of the involved components have been studied in some detail, little is known on the biological role of the ...
Fischer, Fabian, Hamann, Andrea, Osiewacz, Heinz D., Weil, Andrea   +3 more
core   +1 more source

AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ [PDF]

Journal of Biological Chemistry, 2010
AAA(+) chaperone ClpX has been suggested to be a modulator of prokaryotic cytoskeletal protein FtsZ, but the details of recognition and remodeling of FtsZ by ClpX are largely unknown. In this study, we have extensively investigated the nature of FtsZ polymers and mechanisms of ClpX-regulated FtsZ polymer dynamics.
Shinya, Sugimoto, Kunitoshi, Yamanaka, Shingo, Nishikori, Atsushi, Miyagi, Toshio, Ando, Teru, Ogura   +5 more
openaire   +2 more sources

Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system. [PDF]

, 2018
Protein degradation is a fundamental process in all living cells and is essential to remove both damaged proteins and intact proteins that are no longer needed by the cell.
Joseph, Simpson, K Devaraj, Neal, M Cole, Christian, Shi, Xinying, Wu, Ti   +4 more
core   +2 more sources

Control of substrate gating and translocation into ClpP by channel residues and ClpX binding [PDF]

, 2010
ClpP is a self-compartmentalized protease, which has very limited degradation activity unless it associates with ClpX to form ClpXP or with ClpA to form ClpAP.
Barkow, Bewley, Bewley, Bogyo, Breusing, Brotz-Oesterhelt, Burton, Burton, Farrell, Flynn, Goldberg, Gottesman, Gottesman, Gottesman, Gribun, Grimaud, Groll, Hersch, Ingvarsson, Jenal, Jennings, Joshi, Kang, Kenniston, Kessel, Kim, Kim, Kim, Kirstein, Kwon, Levchenko, Liu, Martin, Martin, Martin, Mary E. Lee, Maurizi, Maurizi, Ortega, Powers, Rabl, Reinstein, Robert T. Sauer, Sauer, Siddiqui, Singh, Singh, Smith, Smith, Song, Sousa, Sousa, Striebel, Szyk, Tania A. Baker, Thompson, Thompson, Wang, Whitby, Yoo, Yu   +60 more
core   +1 more source

CLPX regulates mitochondrial fatty acid β-oxidation in liver cells

Journal of Biological Chemistry, 2023
Mitochondrial fatty acid oxidation (β-oxidation) is an essential metabolic process for energy production in eukaryotic cells, but the regulatory mechanisms of this pathway are largely unknown. In the present study, we found that several enzymes involved in β-oxidation are associated with CLPX, the AAA+ unfoldase that is a component of the mitochondrial
Ko Suzuki, Yoshiko Kubota, Kiriko Kaneko, Costantine Chasama Kamata, Kazumichi Furuyama   +4 more
openaire   +2 more sources

Latent ClpX-recognition signals ensure LexA destruction after DNA damage [PDF]

Genes & Development, 2003
The DNA-damage response genes in bacteria are up-regulated when LexA repressor undergoes autocatalytic cleavage stimulated by activated RecA protein. Intact LexA is stable to intracellular degradation but its auto-cleavage fragments are degraded rapidly. Here, both fragments of LexA are shown to be substrates for the ClpXP protease.
Saskia B, Neher, Julia M, Flynn, Robert T, Sauer, Tania A, Baker   +3 more
openaire   +2 more sources

Observations of snowpack properties to evaluate ground-based microwave remote sensing [PDF]

, 2013
Active microwave radar has been shown to have great potential for estimating snow water equivalent (SWE) globally from space. To help evaluate optimal active microwave sensor configurations to observe SWE, we evaluated ground-based Frequency Modulated ...
Emad Tajkhorshid (243146), Günther H. Peters (1517515), Jesper J. Madsen (1517524), Johan H. Faber (146290), Ole H. Olsen (1517518), Y. Zenmei Ohkubo (1517521)   +5 more
core   +2 more sources

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

eLife, 2020
ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E.
Xue Fei, Tristan A Bell, Simon Jenni, Benjamin M Stinson, Tania A Baker, Stephen C Harrison, Robert T Sauer   +6 more
doaj   +1 more source

A Staphylococcus aureus clpX Mutant Used as a Unique Screening Tool to Identify Cell Wall Synthesis Inhibitors that Reverse β-Lactam Resistance in MRSA

Frontiers in Molecular Biosciences, 2021
Staphylococcus aureus is a leading cause of bacterial infections world-wide. Staphylococcal infections are preferentially treated with β-lactam antibiotics, however, methicillin-resistant S. aureus (MRSA) strains have acquired resistance to this superior
Kristoffer T. Bæk, Camilla Jensen, Maya A. Farha, Tobias K. Nielsen, Ervin Paknejadi, Viktor H. Mebus, Martin Vestergaard, Eric D. Brown, Dorte Frees   +8 more
doaj   +1 more source

The ClpX chaperone controls autolytic splitting of Staphylococcus aureus daughter cells, but is bypassed by β-lactam antibiotics or inhibitors of WTA biosynthesis.

PLoS Pathogens, 2019
β-lactam antibiotics interfere with cross-linking of the bacterial cell wall, but the killing mechanism of this important class of antibiotics is not fully understood.
Camilla Jensen, Kristoffer T Bæk, Clement Gallay, Ida Thalsø-Madsen, Lijuan Xu, Ambre Jousselin, Fernando Ruiz Torrubia, Wilhelm Paulander, Ana R Pereira, Jan-Willem Veening, Mariana G Pinho, Dorte Frees   +11 more
doaj   +1 more source