Results 61 to 70 of about 5,302 (190)

Mechanochemical basis of protein degradation by a double-ring AAA+ machine [PDF]

open access: yes, 2014
Molecular machines containing double or single AAA+ rings power energy-dependent protein degradation and other critical cellular processes, including disaggregation and remodeling of macromolecular complexes.
A Martin   +48 more
core   +1 more source

A Uniform Benchmark for Testing SsrA-Derived Degrons in the Escherichia coli ClpXP Degradation Pathway

open access: yesMolecules, 2021
The ssrA degron is commonly used in fusion proteins to control protein stability in bacteria or as an interaction module. These applications often rely on the modular activities of the ssrA tag in binding to the SspB adaptor and in engaging the ClpXP ...
Maria Magdalena Klimecka   +6 more
doaj   +1 more source

Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria [PDF]

open access: yes, 2017
Loss-of-function mutations in genes for heme biosynthetic enzymes can give rise to congenital porphyrias, eight forms of which have been described. The genetic penetrance of the porphyrias is clinically variable, underscoring the role of additional ...
Baker, Tania   +14 more
core   +3 more sources

A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells

open access: yesCommunications Biology, 2021
Wang et al. developed a fluorescence-assisted single-cell methodology (split protease-E. coli ClpXP (SPEC)) to characterise protein-protein interactions for both eukaryotic and prokaryotic species in E. coli cells.
Shengchen Wang   +7 more
doaj   +1 more source

Proteolysis in the Escherichia coli heat shock response: a player at many levels [PDF]

open access: yes, 2011
Proteolysis is a fundamental process used by all forms of life to maintain homeostasis, as well as to remodel the proteome following environmental changes.
Baker, Tania, Meyer, Anne S.
core   +1 more source

Communication of ClpXP protease hypersensitivity to bacteriophage mu repressor isoforms

open access: yesJournal of Molecular Biology, 1997
The immunity repressor (Rep) of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. Although Rep is stable in vivo, an altered immunity repressor (Vir) encoded by virulent, trans-dominant Mu mutants is rapidly degraded by Escherichia coli ClpXP protease. Rep and Vir are degraded
D J, Welty, J M, Jones, H, Nakai
openaire   +2 more sources

Dynamics of Substrate Denaturation and Translocation by the ClpXP Degradation Machine [PDF]

open access: yesMolecular Cell, 2000
ClpXP is a protein machine composed of the ClpX ATPase, a member of the Clp/Hsp100 family of remodeling enzymes, and the ClpP peptidase. Here, ClpX and ClpXP are shown to catalyze denaturation of GFP modified with an ssrA degradation tag. ClpX translocates this denatured protein into the proteolytic chamber of ClpP and, when proteolysis is blocked ...
Kim, Yong-In   +4 more
openaire   +2 more sources

The Mouse Heart Mitochondria N Terminome Provides Insights into ClpXP-Mediated Proteolysis [PDF]

open access: yesMolecular & Cellular Proteomics, 2020
The mammalian mitochondrial proteome consists of more than 1100 annotated proteins and their proteostasis is regulated by only a few ATP-dependent protease complexes. Technical advances in protein mass spectrometry allowed for detailed description of the mitoproteome from different species and tissues and their changes under specific conditions ...
Hofsetz, Eduard   +6 more
openaire   +3 more sources

The Essential Role of ClpXP in Caulobacter crescentus Requires Species Constrained Substrate Specificity

open access: yesFrontiers in Molecular Biosciences, 2017
The ClpXP protease is a highly conserved AAA+ degradation machine that is present throughout bacteria and in eukaryotic organelles. ClpXP is essential in some bacteria, such as Caulobacter crescentus, but dispensible in others, such as Escherichia coli ...
Robert H. Vass   +3 more
doaj   +1 more source

ClpXP controls the expression of LEE genes in enterohaemorrhagic Escherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 2005
Enterohaemorrhagic Escherichia coli (EHEC) contains a 36-kb pathogenicity island termed the locus of enterocyte effacement (LEE), which encodes a type III secretion system (TTSS) and virulence proteins. In this paper, we show that the O157:H7 Sakai clpPX mutant strongly impaired the secretion of virulence proteins by TTSS and repressed transcription ...
Toshifumi, Tomoyasu   +4 more
openaire   +2 more sources

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