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Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly*
Surface plasmon resonance studies and isothermal titration calorimetry measurements revealed that IscU binds to IscS with high affinity (K d ∼2 μm) in support of a direct transfer mechanism, and suggested that the C-terminal region of IsCS may be important for binding Isc U.
Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation
In vivo and in vitro studies of yeast Ssq1 and Jac1 indicate that the chaperones are not required for [FeS]-cluster assembly on Isu, and the crystal structure of a complex of a peptide containing the IscU recognition region bound to the HscA substrate binding domain has been determined.
Inhibition of human aromatase by mammalian lignans and isoflavonoid phytoestrogens
It is suggested that the high concentration of lignans in vegetarians, by inhibiting aromatase in peripheral and/or cancer cells and lowering estrogen levels, may play a protective role as antipromotional compounds during growth of estrogen-dependent cancers.
Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.
Modeling suggests that rotation of this loop may allow movement of Cys328 to within approximately 3A of the pyridoxal phosphate cofactor, suggesting that a large conformational change must occur during catalysis in order for Cys 328 to participate in nucleophilic attack of a pyridine-bound cysteine substrate.
Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.
A direct and specific role for the Hsc66/Hsc20 chaperone system in functioning with isc gene components for the assembly of iron-sulfur cluster proteins is established.
Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae
Results suggest a role for Ssq1p, Jac2p, and Nfs1p in assembly/maturation of mitochondrial iron-sulfur proteins and that one or more of the target Fe/S proteins contribute to oxidative damage in cells lacking copper/zinc SOD.
Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU*
It is suggested that Hsc66 will not bind LPPVK motifs with high affinity in vivo unless they are in the context of native IscU and can be directed to H sc66 by Hsc20.
Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly.
Two genes of bakers yeast Saccharomyces cerevisiae, ISU1 and ISU2, which encode homologues to bacterial IscU and NifU, potential iron-binding or cluster-assembly proteins are identified, suggesting that they are regulated by the iron status of the cell.
Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC.
HscA, a specialized bacterial Hsp70-class molecular chaperone, interacts with the iron-sulfur cluster assembly protein IscU by recognizing a conserved LPPVK sequence motif. We report the crystal
Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
It is suggested that Hsc66 and Hsc20 comprise a molecular chaperone system similar to the prokaryotic DnaK/DnaJ and eukaryotic hsp70/hsp40 systems.