Results 21 to 30 of about 5,302 (190)

Virulence Regulation and Lifestyle Transitions: The Role of c-di-GMP and Two-Component Systems in Erwinia amylovora and Their Evolutionary Context Within Enterobacterales. [PDF]

Mol Plant Pathol
Erwinia amylovora infects apple blossoms by activating the T3SS, then spreads systemically via amylovoran‐mediated biofilms. Transitions between motile and sessile states are regulated by key two‐component systems and c‐di‐GMP. This review summarises infection biology, virulence factors, regulatory networks and evolutionary insights underlying fire ...
Niroula D, Bhandari K, Sundin GW, Joshi JR.   +3 more
europepmc   +2 more sources

Structural insights into the Pseudomonas aeruginosa ClpP1•ClpP2 heterocomplex and its interactions with the AAA+ ClpX unfoldase. [PDF]

Protein Sci
Abstract ClpXP and other AAA+ proteases play central roles in bacterial proteostasis by degrading misfolded and regulatory proteins. In Pseudomonas aeruginosa, ClpXP consists of the ClpX unfoldase and ClpP peptidase, which influence critical adaptive processes contributing to stress resistance. P.
Ghanbarpour A, Zhang JJ, Davis JH, Baker TA, Sauer RT.   +4 more
europepmc   +2 more sources

Proteolytic Queues at ClpXP Increase Antibiotic Tolerance [PDF]

ACS Synthetic Biology, 2019
AbstractAntibiotic tolerance is a widespread phenomenon that renders antibiotic treatments less effective and facilitates antibiotic resistance. Here we explore the role of proteases in antibiotic tolerance, short-term population survival of antibiotics, using queueing theory (i.e.
Heather S. Deter, Alawiah H. Abualrahi, Prajakta Jadhav, Elise K. Schweer, Curtis T. Ogle, Nicholas C. Butzin   +5 more
openaire   +2 more sources

Cellular functions of the ClpP protease impacting bacterial virulence

Frontiers in Molecular Biosciences, 2022
Proteostasis mechanisms significantly contribute to the sculpting of the proteomes of all living organisms. ClpXP is a central AAA+ chaperone-protease complex present in both prokaryotes and eukaryotes that facilitates the unfolding and subsequent ...
Mazen E. Aljghami, Marim M. Barghash, Emily Majaesic, Vaibhav Bhandari, Walid A. Houry, Walid A. Houry   +5 more
doaj   +1 more source

Multistep substrate binding and engagement by the AAA+ ClpXP protease [PDF]

Proceedings of the National Academy of Sciences, 2020
Significance AAA+ proteases play key regulatory and quality control roles in all domains of life. These destructive enzymes recognize damaged, unneeded, or regulatory proteins via specific degrons and unfold them prior to processive degradation. Here, we show that Escherichia coli
Reuben A. Saunders, Benjamin M. Stinson, Tania A. Baker, Robert T. Sauer   +3 more
openaire   +2 more sources

Small molecule inhibitors of the mitochondrial ClpXP protease possess cytostatic potential and re-sensitize chemo-resistant cancers

Scientific Reports, 2021
The human mitochondrial ClpXP protease complex (HsClpXP) has recently attracted major attention as a target for novel anti-cancer therapies. Despite its important role in disease progression, the cellular role of HsClpXP is poorly characterized and only ...
Martina Meßner, Melanie M. Mandl, Mathias W. Hackl, Till Reinhardt, Maximilian A. Ardelt, Karolina Szczepanowska, Julian E. Frädrich, Jens Waschke, Irmela Jeremias, Anja Fux, Matthias Stahl, Angelika M. Vollmar, Stephan A. Sieber, Johanna Pachmayr   +13 more
doaj   +1 more source

Chance, Destiny, and the Inner Workings of ClpXP [PDF]

Cell, 2014
AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of
Russell, Rick, Matouschek, Andreas
openaire   +2 more sources

Proteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli. [PDF]

PLoS ONE, 2017
During bacterial cell division a dynamic protein structure called the Z-ring assembles at the septum. The major protein in the Z-ring in Escherichia coli is FtsZ, a tubulin homolog that polymerizes with GTP.
Marissa G Viola, Christopher J LaBreck, Joseph Conti, Jodi L Camberg   +3 more
doaj   +1 more source

ClpXP Degrades SsrA-Tagged Proteins inStreptococcus pneumoniae [PDF]

Journal of Bacteriology, 2009
ABSTRACTBacterial proteins that are abnormally truncated due to incomplete mRNA or the presence of rare codons are extended by an SsrA tag during ribosome rescue in atrans-translation process important for maintaining protein quality. InEscherichia coli, the SsrA-tagged proteins become the target of the Tsp, Lon, FtsH, ClpXP, and ClpAP proteases.
Sarita, Ahlawat, Donald A, Morrison
openaire   +2 more sources

Engineering Synthetic Adaptors and Substrates for Controlled ClpXP Degradation [PDF]

Journal of Biological Chemistry, 2009
Facile control of targeted intracellular protein degradation has many potential uses in basic science and biotechnology. One promising approach to this goal is to redesign adaptor proteins, which can regulate proteolytic specificity by tethering substrates to energy-dependent AAA+ proteases.
Joseph H, Davis, Tania A, Baker, Robert T, Sauer   +2 more
openaire   +2 more sources