Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU
Open Access
- 1 December 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (52) , 53924-53931
- https://doi.org/10.1074/jbc.m410117200
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Preferential Substrate Binding Orientation by the Molecular Chaperone HscAPublished by Elsevier ,2004
- Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone SystemJournal of Biological Chemistry, 2003
- Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscUJournal of Biological Chemistry, 2002
- The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coliJournal of Biological Chemistry, 2001
- Interaction of the iron–sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coliProceedings of the National Academy of Sciences, 2000
- IscU as a Scaffold for Iron−Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscUBiochemistry, 2000
- Kinetic Characterization of the ATPase Cycle of the Molecular Chaperone Hsc66 from Escherichia coliPublished by Elsevier ,2000
- The Hsc66-Hsc20 Chaperone System in Escherichia coli : Chaperone Activity and Interactions with the DnaK-DnaJ-GrpE SystemJournal of Bacteriology, 1998
- Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coliProtein Science, 1997
- Structural Analysis of Substrate Binding by the Molecular Chaperone DnaKScience, 1996