Results 51 to 60 of about 7,556 (201)
mBio, 2020 Chlamydia trachomatis is an obligate intracellular bacterium that undergoes a complex developmental cycle in which the bacterium differentiates between two functionally and morphologically distinct forms, the elementary body (EB) and reticulate body (RB),
Nicholas A. Wood +5 more
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Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria [PDF]
, 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
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Nature Communications, 2023 AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently translocated
Alireza Ghanbarpour +8 more
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Clp ATPases differentially affect natural competence development in Streptococcus mutans
MicrobiologyOpen, 2022 In naturally competent bacteria, DNA transformation through horizontal gene transfer is an evolutionary mechanism to receive extracellular DNA. Bacteria need to maintain a state of competence to accept foreign DNA, and this is an energy‐driven phenomenon
Satya D. Pandey, Indranil Biswas
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Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle [PDF]
, 2016 The ClpXP protease assembles in a reaction in which an ATP-bound ring hexamer of ClpX binds to one or both heptameric rings of the ClpP peptidase. Contacts between ClpX IGF-loops and clefts on a ClpP ring stabilize the complex.
Amor, Alvaro Jorge +4 more
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Elucidating The Specificity Determinants Responsible For ClpX-Adaptor Interaction [PDF]
Biophysical Journal, 2009 The ClpXP proteolytic machinery in bacteria consists of the AAA+ ATPase protein ClpX and the serine peptidase ClpP. ClpX recognizes, unfolds, and translocates substrates into the protease chamber where hydrolysis of the polypeptide occurs. To control substrate-specificity, the cell uses adaptor proteins, such as SspB, to modulate substrate selection ...
Chowdhury, Tahmeena +3 more
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Insight into the RssB-Mediated Recognition and Delivery of σs to the AAA+ Protease, ClpXP
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.
Dimce Micevski +6 more
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Frontiers 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
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Frontiers in Bioengineering and Biotechnology, 2021 Motility is finely regulated and is crucial to bacterial processes including colonization and biofilm formation. There is a trade-off between motility and growth in bacteria with molecular mechanisms not fully understood.
Bingyu Li +11 more
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The Journal of Cell Biology, 2005 ![Graphic][1] The ClpX hexamer can operate on one cylinder. SAUER/MACMILLANClpXP is an ATP-powered eating machine. Its ring of six ClpX ATPase modules feeds substrates to the ClpP protease.
openaire +2 more sources