Results 51 to 60 of about 5,302 (190)

Survival of Anaerobic Fe ²⁺ Stress Requires the ClpXP Protease [PDF]

Journal of Bacteriology, 2018
ABSTRACT Shewanella oneidensis strain MR-1 is a versatile bacterium capable of respiring extracellular, insoluble ferric oxide minerals under anaerobic conditions. The respiration of iron minerals results in the production of soluble ferrous ions, which at high concentrations are toxic to living organisms.
Brittany D, Bennett, Kaitlyn E, Redford, Jeffrey A, Gralnick   +2 more
openaire   +2 more sources

Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.

PLoS ONE, 2014
ClpXP is a two-component ATP-dependent protease that unfolds and degrades proteins bearing specific recognition signals. One substrate degraded by Escherichia coli ClpXP is FtsZ, an essential cell division protein.
Jodi L Camberg, Marissa G Viola, Leslie Rea, Joel R Hoskins, Sue Wickner   +4 more
doaj   +1 more source

ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation [PDF]

, 2014
We investigated how Escherichia coli ClpXP targets the helicase-nuclease (HsdR) subunit of the bacterial Type I restriction–modification enzyme EcoKI during restriction alleviation (RA).
Diffin, Fiona M, Simons, Michelle, Szczelkun, Mark D   +2 more
core   +2 more sources

Clpxp Degradation of Proteins Probed By Single-Molecule Fluorescence [PDF]

Biophysical Journal, 2010
ClpXP is an AAA+ protease that unfolds and degrades target proteins. ClpX, a hexameric ring-shaped ATPase, recognizes specific proteins and then powers their mechanical denaturation and translocation into the degradation chamber of ClpP where polypeptide bond cleavage occurs.
Shin, Yongdae, Davis, Joseph H., Brau, Ricardo R., Martin, Andreas, Baker, Tania A., Sauer, Robert T., Lang, Matthew J.   +6 more
openaire   +1 more source

Binding and Degradation of Heterodimeric Substrates by ClpAP and ClpXP [PDF]

Journal of Biological Chemistry, 2005
ClpA and ClpX function both as molecular chaperones and as the regulatory components of ClpAP and ClpXP proteases, respectively. ClpA and ClpX bind substrate proteins through specific recognition signals, catalyze ATP-dependent protein unfolding of the substrate, and when in complexes with ClpP translocate the unfolded polypeptide into the cavity of ...
Suveena, Sharma, Joel R, Hoskins, Sue, Wickner   +2 more
openaire   +2 more sources

Gain of Spontaneous clpX Mutations Boosting Motility via Adaption to Environments in Escherichia coli

Frontiers in Bioengineering and Biotechnology, 2021
Motility is finely regulated and is crucial to bacterial processes including colonization and biofilm formation. There is a trade-off between motility and growth in bacteria with molecular mechanisms not fully understood.
Bingyu Li, Bingyu Li, Bingyu Li, Chaofan Hou, Xian Ju, Yong Feng, Zhi-Qiang Ye, Yunzhu Xiao, Mingyao Gu, Chunxiang Fu, Chaoliang Wei, Conghui You   +11 more
doaj   +1 more source

Tailored Phenyl Esters Inhibit ClpXP and Attenuate Staphylococcus aureus α‐Hemolysin Secretion [PDF]

ChemBioChem, 2022
AbstractNovel strategies against multidrug‐resistant bacteria are urgently needed in order to overcome the current silent pandemic. Manipulation of toxin production in pathogenic species serves as a promising approach to attenuate virulence and prevent infections. In many bacteria such as Staphylococcus aureus or Listeria monocyotgenes, serine protease
Markus Schwarz, Ines Hübner, Stephan A. Sieber   +2 more
openaire   +2 more sources

Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX [PDF]

, 2015
ATP-dependent protein remodeling and unfolding enzymes are key participants in protein metabolism in all cells. How these often-destructive enzymes specifically recognize target protein complexes is poorly understood.
Baker, Tania, Ling, Lorraine, Montaño, Sherwin P., Rice, Phoebe A., Sauer, Robert T.   +4 more
core   +1 more source

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

The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP

Frontiers in Molecular Biosciences, 2017
ClpX is a member of the Clp/Hsp100 family of ATP-dependent chaperones and partners with ClpP, a compartmentalized protease, to degrade protein substrates bearing specific recognition signals.
Christopher J. LaBreck, Shannon May, Marissa G. Viola, Joseph Conti, Jodi L. Camberg   +4 more
doaj   +1 more source