Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 37, Pages 31406-31413Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.352617
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Funding
- National Institutes of Health [R01 GM58667, U01 GM94622]
- National Magnetic Resonance Facility at Madison
- NIH grants from the National Center for Research Resources [5P41RR002301-27, RR02301-26S1]
- National Institute for General Medical Sciences [8 P41 GM103399-27]
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The Escherichia coli protein IscU serves as the scaffold for Fe-S cluster assembly and the vehicle for Fe-S cluster transfer to acceptor proteins, such as apoferredoxin. IscU populates two conformational states in solution, a structured conformation (S) that resembles the conformation of the holoproteinIsc U-[2Fe-2S] and a dynamically disordered conformation (D) that does not bind metal ions. NMR spectroscopic results presented here show that the specialized Hsp70 chaperone (HscA), alone or as the HscA-ADP complex, preferentially binds to and stabilizes the D-state of IscU. IscU is released when HscA binds ATP. By contrast, the J-protein HscB binds preferentially to the S-state of IscU. Consistent with these findings, we propose a mechanism in which cluster transfer is coupled to hydrolysis of ATP bound to HscA, conversion of IscU to the D-state, and release of HscB.
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