Results 61 to 70 of about 3,616 (191)

Insight into the RssB-Mediated Recognition and Delivery of σs to the AAA+ Protease, ClpXP [PDF]

Biomolecules, 2020
In Escherichia coli, SigmaS (σS) is the master regulator of the general stress response. The cellular levels of σS are controlled by transcription, translation and protein stability. The turnover of σS, by the AAA+ protease (ClpXP), is tightly regulated by a dedicated adaptor protein, termed RssB (Regulator of Sigma S protein B)—which is an atypical ...
Micevski, Dimce, Zeth, Kornelius, Mulhern, Terrence D, Schuenemann, Verena J, Zammit, Jessica E, Truscott, Kaye N, Dougan, David A   +6 more
openaire   +7 more sources

The polar localization hub protein PopZ restrains adaptor dependent ClpXP proteolysis inCaulobacter crescentus

, 2018
InCaulobacter crescentus, timely degradation of several proteins by the ClpXP protease is critical for proper cell cycle progression. During the cell cycle, the ClpXP protease, the substrate CtrA and many other proteins are localized to the stalked pole ...
Peter Chien, Kamal Kishore Joshi
core   +1 more source

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

Single-molecule denaturation and degradation of proteins by the AAA+ ClpXP protease [PDF]

Proceedings of the National Academy of Sciences, 2009
ClpXP is an ATP-fueled molecular machine that unfolds and degrades target proteins. ClpX, an AAA+ enzyme, recognizes specific proteins, and then uses cycles of ATP hydrolysis to denature any native structure and to translocate the unfolded polypeptide into ClpP for degradation. Here, we develop and apply single-molecule fluorescence assays to probe the
Shin, Yongdae, Brau, Ricardo R., Martin, Andreas, Kenniston, Jon A., Lang, Matthew J., Baker, Tania, Davis, Joseph Harry, Sauer, Robert T   +7 more
openaire   +4 more sources

The Cleavage Profile of Protein Substrates by ClpXP Reveals Deliberate Starts and Pauses [PDF]

Biochemistry, 2020
Cells rely on protein degradation by AAA+ proteases. A well-known example is the hexameric ClpX unfoldase, which captures ATP hydrolysis to feed substrates into the oligomeric ClpP peptidase. Recent studies show that an asymmetric ClpX spiral cycles protein translocation upon ATP hydrolysis.
Catherine Y. Tremblay, Robert H. Vass, Richard W. Vachet, Peter Chien   +3 more
openaire   +2 more sources

Molybdopterin biosynthesis pathway contributes to the regulation of SaeRS two-component system by ClpP in Staphylococcus aureus

Virulence, 2022
In Staphylococcus aureus, the SaeRS two-component system is essential for the bacterium’s hemolytic activity and virulence. The Newman strain of S. aureus contains a variant of SaeS sensor kinase, SaeS L18P.
Na Zhao, Yanan Wang, Junlan Liu, Ziyu Yang, Ying Jian, Hua Wang, Mahmoud Ahmed, Min Li, Taeok Bae, Qian Liu   +9 more
doaj   +1 more source

Optical Tweezers for Monitoring Unfolding by the Protease ClpXP

Frontiers in Optics 2013, 2013
The biological motor ClpXP pulls against a targeted protein until it mechanically unfolds and translocates the polypeptide into a chamber for degradation. We directly monitor degradation of model polyprotein substrates in dual-trap single molecule assays. Article not available.
Juan Carlos Cordova, Yongdae Shin, Stephane Calmat, Karl R. Schmitz, Marie-Eve Aubin-Tam, Adrian Olivares, Robert T. Sauer, Tania A. Baker, Matthew J. Lang   +8 more
openaire   +2 more sources

Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine [PDF]

IUBMB Life, 2011
AbstractIn the crowded environment of a cell, the protein quality control machinery, such as molecular chaperones and proteases, maintains a population of folded and hence functional proteins. The accumulation of unfolded proteins in a cell is particularly harmful as it not only reduces the concentration of active proteins but also overburdens the ...
Truscott, Kaye N., Bezawork-Geleta, Ayenachew, Dougan, David A.   +2 more
openaire   +5 more sources

The RssB response regulator directly targets ς^S for degradation by ClpXP

, 2001
The ςS subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. Control over ςS activity is exercised in part by regulated degradation of ςS.
Michael R. Maurizi, Susan Gottesman, YanNing Zhou, Joel R. Hoskins, Sue Wickner   +4 more
core   +1 more source

Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis

Frontiers in Microbiology, 2016
The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response and motility.
Noel eMoliere, Jörn eHoßmann, Heinrich eSchäfer, Kürşad eTurgay   +3 more
doaj   +1 more source