期刊
FEBS LETTERS
卷 587, 期 8, 页码 1172-1179出版社
WILEY
DOI: 10.1016/j.febslet.2013.01.003
关键词
Conformational equilibrium; Protein-protein interaction; Protein evolution; Iron-sulfur cluster; Peptidyl-prolyl peptide bond isomerization; Metamorphic protein
资金
- US National Institutes of Health (NIH) [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 [8P41 GM103399-27]
IscU from Escherichia coli, the scaffold protein for iron-sulfur cluster biosynthesis and delivery, populates a complex energy landscape. IscU exists as two slowly interconverting species: one (S) is largely structured with all four peptidyl-prolyl bonds trans; the other (D) is partly disordered but contains an ordered domain that stabilizes two cis peptidyl-prolyl peptide bonds. At pH 8.0, the S-state is maximally populated at 25 degrees C, but its population decreases at higher or lower temperatures or at lower pH. The D-state binds preferentially to the cysteine desulfurase (IscS), which generates and transfers sulfur to IscU cysteine residues to form persulfides. The S-state is stabilized by Fe-S cluster binding and interacts preferentially with the DnaJ-type co-chaperone (HscB), which targets the holo-IscU: HscB complex to the DnaK-type chaperone (HscA) in its ATP-bound from. HscA is involved in delivery of Fe-S clusters to acceptor proteins by a mechanism dependent on ATP hydrolysis. Upon conversion of ATP to ADP, HscA binds the D-state of IscU ensuring release of the cluster and HscB. These findings have led to a more complete model for cluster biosynthesis and delivery. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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