Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding

scientific article published on 24 February 2020

Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.7554/ELIFE.54387
P932PMC publication ID7077987
P698PubMed publication ID32091391

P50authorJohn R. EngenQ50420861
Jamie A MorocoQ58774054
Tania BakerQ59748326
Julia R KardonQ89855393
P2860cites workChaperone machines for protein folding, unfolding and disaggregationQ27026110
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machineQ27658178
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Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Q27933616
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The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegansQ33757350
Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processingQ33820056
Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processingQ33974768
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Disulfide by Design 2.0: a web-based tool for disulfide engineering in proteinsQ35056453
NOA1, a novel ClpXP substrate, takes an unexpected nuclear detour prior to mitochondrial importQ35215048
Proteolysis in Bacterial Regulatory CircuitsQ35564854
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switchingQ35616366
Sequence- and species-dependence of proteasomal processivityQ36177085
Slippery substrates impair function of a bacterial protease ATPase by unbalancing translocation versus exitQ36832564
Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease.Q37087848
Critical clamp loader processing by an essential AAA+ protease in Caulobacter crescentusQ37318075
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Novel Mechanisms for Heme-dependent Degradation of ALAS1 Protein as a Component of Negative Feedback Regulation of Heme BiosynthesisQ38753511
CLPP coordinates mitoribosomal assembly through the regulation of ERAL1 levels.Q39232101
Control of substrate gating and translocation into ClpP by channel residues and ClpX binding.Q41063926
Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translationQ41436895
Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sitesQ41587676
Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco ActivaseQ41596828
Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.Q43151994
Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signalsQ44384522
An unstructured initiation site is required for efficient proteasome-mediated degradationQ45018402
Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencingQ47158873
Dynamics of substrate denaturation and translocation by the ClpXP degradation machineQ47235359
Remodeling of HIV-1 Nef Structure by Src-Family Kinase Binding.Q47273958
Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyriaQ47851870
Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.Q52650168
A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κBQ57851826
Mechanism for remodelling of the cell cycle checkpoint protein MAD2 by the ATPase TRIP13Q59086244
A new fluorometric method for the determination of pyridoxal 5′-phosphateQ69565089
The occurrence and determination of delta-amino-levulinic acid and porphobilinogen in urineQ73933517
Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX proteaseQ77726447
Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpXQ84648579
P4510describes a project that usesImageJQ1659584
P577publication date2020-02-24
P1433published ineLifeQ2000008
P1476titleMitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding
P478volume9

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cites work (P2860)
Q95933769AAA+ proteins: converging mechanisms, diverging functions
Q100512225Mitochondrial ClpP serine protease-biological function and emerging target for cancer therapy