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Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly*
The cysteine desulfurase enzymes NifS and IscS provide sulfur for the biosynthesis of Fe/S proteins. NifU and IscU have been proposed to serve as template or scaffold proteins in the initial Fe/SExpand
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Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.
The iscU gene in bacteria is located in a gene cluster encoding proteins implicated in iron-sulfur cluster assembly and an hsc70-type (heat shock cognate) molecular chaperone system, iscSUA-hscBA. ToExpand
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Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU*
Hsc66 and Hsc20 comprise a specialized chaperone system important for the assembly of iron-sulfur clusters in Escherchia coli. Only a single substrate, the Fe/S template protein IscU, has beenExpand
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Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly.
Recent studies in bacteria and eukaryotes have led to the identification of several new genes implicated in the biogenesis of iron-sulfur (Fe/S) cluster-containing proteins. This report focuses onExpand
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Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide.
Sirtuin proteins comprise a unique class of NAD+-dependent protein deacetylases. Although several structures of sirtuins have been determined, the mechanism by which NAD+ cleavage occurs has remainedExpand
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Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System*
Hsc66 (HscA) and Hsc20 (HscB) from Escherichia coli comprise a specialized chaperone system that selectively binds the iron-sulfur cluster template protein IscU. Hsc66 interacts with peptidesExpand
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Structural insights into intermediate steps in the Sir2 deacetylation reaction.
Sirtuin enzymes comprise a unique class of NAD(+)-dependent protein deacetylases. Although structures of many sirtuin complexes have been determined, structural resolution of intermediate chemicalExpand
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The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.
Hsc66, a stress-70 protein, and Hsc20, a J-type accessory protein, comprise a newly described Hsp70-type chaperone system in addition to DnaK-DnaJ-GrpE in Escherichia coli. Because endogenousExpand
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Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU*
The ATPase activity of HscA, a specialized hsp70 molecular chaperone from Escherichia coli, is regulated by the iron-sulfur cluster assembly protein IscU and the J-type co-chaperone HscB. IscUExpand
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A conserved histidine in human DNLZ/HEP is required for stimulation of HSPA9 ATPase activity.
The DNL-type zinc-finger protein DNLZ regulates the activity and solubility of the human mitochondrial chaperone HSPA9. To identify DNLZ residues that are critical for chaperone regulation, weExpand
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