Annotation inferences using phylogenetic trees
Interaction network containing conserved and essential protein complexes in Escherichia coli.
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A high-throughput affinity-purification study reported CnoX interaction rows, but the cached abstract does not expose the pair-level evidence.
"An interaction network of protein complexes involved in diverse biological processes was uncovered and validated by sequential rounds of tagging and purification."
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Protein abundance profiling of the Escherichia coli cytosol.
The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase.
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CnoX interacts with GroEL and DnaK and enhances DnaK-machine protein renaturation.
"YbbN specifically interacts with DnaK and GroEL, as shown by reverse purification. It increases 4-fold the rate of protein renaturation in vitro by the DnaK chaperone machine"
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A cnoX-deficient strain is selectively sensitive to thermal stress.
"an ybbN-deficient strain displays an increased sensitivity to thermal stress but not to oxidative stress"
Escherichia coli thioredoxin-like protein YbbN contains an atypical tetratricopeptide repeat motif and is a negative regulator of GroEL.
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CnoX binds GroEL and mildly inhibits GroEL/GroES chaperonin and ATPase activity in vitro.
"A variety of proteins in E. coli interact with YbbN, including multiple ribosomal protein subunits and a strong interaction with GroEL."
DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN.
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CnoX refolds urea-unfolded DnaN in vitro, while the deletion mutant has DNA replication and cell-division defects.
"Moreover, YbbN functions as a bona fide chaperone in the refolding of the urea-unfolded β-clamp."
CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation.
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CnoX is an HOCl-activated holdase that prevents client aggregation and irreversible oxidation and cooperates with the major folding systems.
"CnoX (YbbN) as a folding factor that, when activated by bleach via chlorination, functions as an efficient holdase, protecting the substrates of the major folding systems GroEL/ES and DnaK/J/GrpE. Remarkably, CnoX uniquely combines this function with the ability to prevent the irreversible oxidation of its substrates."
A molecular device for the redox quality control of GroEL/ES substrates.
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CnoX binds stably outside the GroEL substrate-binding site, forms mixed disulfides with GroEL clients, and is released when GroES binds.
"Here, we report that the bacterial Hsp60 chaperonin GroEL forms a stable, functionally relevant complex with the chaperedoxin CnoX, a protein combining a chaperone and a redox function. Binding of GroES (Hsp10 cofactor) to GroEL induces CnoX release."
PTHR45663 PAINT annotations
Unfolded Protein Binding Annotation Review
Deep research report for E. coli CnoX