Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart

The results of in vivo and in organellar experiments indicate that the Hsp70 Ssq1 and the J-protein Jac1 function together to assist in the biogenesis of iron-sulfur (Fe/S) centers in the mitochondrial matrix. Here we present biochemical evidence supporting this idea. Isu, the proposed scaffold on w...

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Veröffentlicht in:	The Journal of biological chemistry 2003-08, Vol.278 (32), p.29719-29727
Hauptverfasser:	Dutkiewicz, Rafal, Schilke, Brenda, Knieszner, Helena, Walter, William, Craig, Elizabeth A, Marszalek, Jaroslaw
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Centrifugation, Density Gradient Electrophoresis, Polyacrylamide Gel Escherichia coli Proteins Glycerol - metabolism Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - metabolism Hydrolysis Iron-Sulfur Proteins - metabolism Kinetics Membrane Transport Proteins - metabolism Mitochondrial Membrane Transport Proteins Mitochondrial Proteins Molecular Chaperones - metabolism Molecular Chaperones - physiology Protein Binding Recombinant Proteins - metabolism Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - physiology Surface Plasmon Resonance Time Factors
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