Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.
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Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesisStructure of Human J-type Co-chaperone HscB Reveals a Tetracysteine Metal-binding DomainThe unique regulation of iron-sulfur cluster biogenesis in a Gram-positive bacteriumStructural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron CofactorsGenome-wide screen of Salmonella genes expressed during infection in pigs, using in vivo expression technologyStructural studies of the Enterococcus faecalis SufU [Fe-S] cluster proteinIscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli.The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandiiTangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Controlled 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).Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural changeMetamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds.HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.Fe-S cluster assembly pathways in bacteria.Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB.Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors.The OxyR regulon in nontypeable Haemophilus influenzae.The human escort protein Hep binds to the ATPase domain of mitochondrial hsp70 and regulates ATP hydrolysis.Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium occurs in two principally distinct pathways.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.The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.X-ray diffraction analysis of a crystal of HscA from Escherichia coli.Identification and characterization of genes differentially expressed in X and Y sperm using suppression subtractive hybridization and cDNA microarray.Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly.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.Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure.Repair of oxidized iron-sulfur clusters in Escherichia coli.Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold isu.Regulation of human Nfu activity in Fe-S cluster delivery-characterization of the interaction between Nfu and the HSPA9/Hsc20 chaperone complex.Molecular chaperones involved in mitochondrial iron-sulfur protein biogenesis.Directed evolution of SecB chaperones toward toxin-antitoxin systems.Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function.
P2860
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P2860
Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Hsc66 substrate specificity is ...... cluster template protein IscU.
@en
Hsc66 substrate specificity is ...... cluster template protein IscU.
@nl
type
label
Hsc66 substrate specificity is ...... cluster template protein IscU.
@en
Hsc66 substrate specificity is ...... cluster template protein IscU.
@nl
prefLabel
Hsc66 substrate specificity is ...... cluster template protein IscU.
@en
Hsc66 substrate specificity is ...... cluster template protein IscU.
@nl
P2093
P2860
P356
P1476
Hsc66 substrate specificity is ...... cluster template protein IscU.
@en
P2093
Dennis T Ta
Jonathan J Silberg
Kevin G Hoff
Larry E Vickery
Tim L Tapley
P2860
P304
27353-27359
P356
10.1074/JBC.M202814200
P407
P577
2002-05-06T00:00:00Z