Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli.
about
Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsRole of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasisSsq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins.Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly.A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscSFatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding.Reconstructing genome-wide regulatory network of E. coli using transcriptome data and predicted transcription factor activities.Diversifying selection and host adaptation in two endosymbiont genomes.The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiaeThe specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.RNA-Seq analysis of isolate- and growth phase-specific differences in the global transcriptomes of enteropathogenic Escherichia coli prototype isolatesControlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems.Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU).Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscUMammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20Xenorhabdus nematophila requires an intact iscRSUA-hscBA-fdx operon to colonize Steinernema carpocapsae nematodes.The human escort protein Hep binds to the ATPase domain of mitochondrial hsp70 and regulates ATP hydrolysis.Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli.A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly.The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR.X-ray diffraction analysis of a crystal of HscA from Escherichia coli.Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.Identity and function of a large gene network underlying mutagenic repair of DNA breaks.The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli.Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system.Preferential substrate binding orientation by the molecular chaperone HscA.Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.Functional implications of the interaction between HscB and IscU in the biosynthesis of FeS clusters.Regulation of human Nfu activity in Fe-S cluster delivery-characterization of the interaction between Nfu and the HSPA9/Hsc20 chaperone complex.Selenate reductase activity in Escherichia coli requires Isc iron-sulfur cluster biosynthesis genes.Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.
P2860
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P2860
Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli.
description
1997 nî lūn-bûn
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1997年の論文
@ja
1997年学术文章
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1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@ast
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@en
type
label
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@ast
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@en
prefLabel
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@ast
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@en
P2093
P2860
P356
P1433
P1476
Hsc66 and Hsc20, a new heat sh ...... system from Escherichia coli.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560060511
P577
1997-05-01T00:00:00Z