Results 21 to 30 of about 7,556 (201)

A proteolytic AAA+ machine poised to unfold protein substrates [PDF]

Nature Communications
AAA+ proteolytic machines unfold proteins before degrading them. Here, we present cryoEM structures of ClpXP-substrate complexes that reveal a postulated but heretofore unseen intermediate in substrate unfolding/degradation. A ClpX hexamer draws natively
Alireza Ghanbarpour, Robert T. Sauer, Joseph H. Davis   +2 more
doaj   +2 more sources

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

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   +4 more sources

Functional investigation of the two ClpPs and three ClpXs in Myxococcus xanthus DK1622 [PDF]

mSphere
ClpXP is a protease complex that plays important roles in protein quality control and cell cycle regulation, but the functions of multiple ClpXs and multiple ClpPs in M. xanthus remain unknown.
Tianyu Wan, Ying Cao, Ya-jun Lai, Zhuo Pan, Yue-zhong Li, Li Zhuo   +5 more
doaj   +2 more sources

An open axial channel of the AAA ClpXP protease enhances degradation of specific classes of protein substrates. [PDF]

Protein Sci
Abstract ClpXP and other AAA proteases maintain proteostasis and regulate cellular functions by degrading misfolded, incomplete, or regulatory proteins. ClpX recognizes substrates via unstructured degron sequences, typically located at the N‐ or C‐terminus. Although five classes of degrons are known, only recognition of the ssrA tag, a C‐motif‐1 degron,
Lyu Y, Bolstad I, Davis JH, Sauer RT, Ghanbarpour A.   +4 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

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Cells, 2021
Biallelic pathogenic variants in CLPP, encoding mitochondrial matrix peptidase ClpP, cause a rare autosomal recessive condition, Perrault syndrome type 3 (PRLTS3). It is characterized by primary ovarian insufficiency and early sensorineural hearing loss,
Jana Key, Sylvia Torres-Odio, Nina C. Bach, Suzana Gispert, Gabriele Koepf, Marina Reichlmeir, A. Phillip West, Holger Prokisch, Peter Freisinger, William G. Newman, Stavit Shalev, Stephan A. Sieber, Ilka Wittig, Georg Auburger   +13 more
doaj   +1 more source

ClpX Shifts into High Gear to Unfold Stable Proteins [PDF]

Cell, 2013
Protein degradation by the ClpXP protease requires collaboration among the six AAA+ domains of ClpX. Using single-molecule optical tweezers, Sen et al. show that ClpX uses a coordinated succession of power strokes to translocate polypeptides in ATP-tunable bursts before reloading with nucleotide.
Maurizi, Michael R., Stan, George
openaire   +2 more sources

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

eLife, 2020
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins.
Zev A Ripstein, Siavash Vahidi, Walid A Houry, John L Rubinstein, Lewis E Kay   +4 more
doaj   +1 more source

Loss of the ClpXP Protease Leads to Decreased Resistance to Cell-Envelope Targeting Antimicrobials in Bacillus anthracis Sterne

Frontiers in Microbiology, 2021
The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou, Christopher R. Evans, Vuong D. Do, Quinn P. Losefsky, Diem Q. Ngo, Shauna M. McGillivray   +5 more
doaj   +1 more source

Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori [PDF]

Journal of Biological Chemistry, 2003
ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N ...
Dong Young, Kim, Kyeong Kyu, Kim
openaire   +2 more sources