Results 41 to 50 of about 4,851 (193)

Degradation of a Caulobacter Soluble Cytoplasmic Chemoreceptor Is ClpX Dependent [PDF]

open access: yesJournal of Bacteriology, 2002
ABSTRACT In order to determine whether ClpXP-mediated proteolysis is a common mechanism used to regulate the chemotaxis machinery during the cell cycle of Caulobacter crescentus , we have characterized a soluble cytoplasmic chemoreceptor, McpB.
Potocka, I.   +4 more
openaire   +3 more sources

Table_1_Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.xlsx

open access: yes, 2022
Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a
Yumeng Zhang (3115050)   +6 more
core   +1 more source

Table_7_Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.xlsx

open access: yes, 2022
Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a
Yumeng Zhang (3115050)   +6 more
core   +1 more source

Disassembly of the Mu transposase tetramer by the ClpX chaperone. [PDF]

open access: yesGenes & Development, 1995
Mu transposition is promoted by an extremely stable complex containing a tetramer of the transposase (MuA) bound to the recombining DNA. Here we purify the Escherichia coli ClpX protein, a member of a family of multimeric ATPases present in prokaryotes and eukaryotes (the Clp family), on the basis of its ability to remove the transposase from the DNA ...
I, Levchenko, L, Luo, T A, Baker
openaire   +2 more sources

ClpX, a Stochastic Protein Unfolding and Translocation Machine [PDF]

open access: yesBiophysical Journal, 2014
During protein degradation by ClpXP, AAA+ ClpX hexamers grip protein substrates using GYVG pore loops and harness the energy of ATP binding and hydrolysis to the drive conformational changes necessary for the mechanical denaturation and translocation of the substrate into the ClpP chamber.
Sauer, Robert T.   +11 more
openaire   +1 more source

Table_5_Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.xlsx

open access: yes, 2022
Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a
Yumeng Zhang (3115050)   +6 more
core   +1 more source

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

open access: yesJournal of Molecular Biology, 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. Here, we use the well-studied AAA+ unfoldase-substrate pair, Escherichia coli ClpX and MuA transposase, to address how these powerful ...
Montaño, Sherwin P.   +4 more
openaire   +4 more sources

Table_8_Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.xlsx

open access: yes, 2022
Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a
Yumeng Zhang (3115050)   +6 more
core   +1 more source

The ClpX heat‐shock protein of Escherichia coli, the ATP‐dependent substrate specificity component of the ClpP‐ClpX protease, is a novel molecular chaperone.

open access: yesThe EMBO Journal, 1995
All major classes of protein chaperones, including DnaK (the Hsp70 eukaryotic equivalent) and GroEL (the Hsp60 eukaryotic equivalent) have been found in Escherichia coli. Molecular chaperones enhance the yields of correctly folded polypeptides by preventing aggregation and even by disaggregating certain protein aggregates. Previously, we identified the
Alicja Wawrzynów   +7 more
openaire   +3 more sources

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

open access: yesPLoS 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   +11 more
doaj   +1 more source

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