Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly*
- Hugo D. Urbina, J. Silberg, K. Hoff, L. Vickery
- Biology, ChemistryJournal of Biological Chemistry
- 30 November 2001
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.
Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.
- K. Hoff, J. Silberg, L. Vickery
- BiologyProceedings of the National Academy of Sciences…
- 5 July 2000
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.
Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly.
- S. Garland, K. Hoff, L. Vickery, V. Culotta
- BiologyJournal of Molecular Biology
- 10 December 1999
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.
Reprogramming Cellular Behavior with RNA Controllers Responsive to Endogenous Proteins
- Stephanie J. Culler, K. Hoff, C. Smolke
- BiologyScience
- 26 November 2010
This work engineered RNA devices that detect signaling through the nuclear factor κB and Wnt signaling pathways in human cells and rewire these pathways to produce new behaviors, thereby linking disease markers to noninvasive sensing and reprogrammed cellular fates.
Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide.
- K. Hoff, J. Avalos, K. Sens, C. Wolberger
- Biology, ChemistryStructure
- 1 August 2006
Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU*
- K. Hoff, D. Ta, Tim L. Tapley, J. Silberg, L. Vickery
- BiologyJournal of Biological Chemistry
- 26 July 2002
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.
Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System*
- K. Hoff, J. Cupp-Vickery, L. Vickery
- BiologyJournal of Biological Chemistry
- 26 September 2003
Results indicate that residues in the LPPVK motif are important for IscU interactions with Hsc66 but not for the ability of Hsc20 to target Isc U to H sc66.
Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU*
- J. Silberg, Tim L. Tapley, K. Hoff, L. Vickery
- BiologyJournal of Biological Chemistry
- 24 December 2004
The overall rate of the chaperone cycle in vivo will be determined by the availability of the IscU-HscB substrate-co-chaperone complex.
Structural insights into intermediate steps in the Sir2 deacetylation reaction.
- W. Hawse, K. Hoff, C. Wolberger
- Chemistry, BiologyStructure
- 10 September 2008
The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coli *
- J. Silberg, K. Hoff, Tim L. Tapley, L. Vickery
- Biology, ChemistryJournal of Biological Chemistry
- 19 January 2001
Results support a role for IscU as a substrate for Hsc66 and suggest a specialized function for H sc66 in the assembly, stabilization, or transfer of Fe/S clusters formed on Isc U.
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