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Interactions of Hsp70 chaperones with Fe‐S cluster scaffold proteins
Author(s) -
Luo WenI,
Cowan James A.
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.713.1
To probe the mechanism and the regulation of Hsp70 chaperones in iron‐sulfur (Fe‐S) cluster biogenesis, interactions in between chaperones and Fe‐S cluster assembling scaffold proteins, ISU (eukaryotic)/IscU (prokaryotic), are examined. The interactions are investigated by biophysical approaches including fluorescence anisotropy and isothermal titration calorimetry (ITC) under various conditions. In addition to distinguishing similarities and differences in eukaryotic and prokaryotic systems, a cross‐system comparison is conducted. Chaperone pairs: human mortalin and Thermotoga maritima DnaK ( Tm DnaK), as well as scaffold protein pairs: human ISU and Tm IscU, are used as models for the cross‐system comparison. The results show the direct participation of Hsp70 chaperones in Fe‐S cluster biogenesis and demonstrate the diversity regarding the mechanism and the regulation of chaperones in Fe‐S cluster biogenesis among species. These findings provide mechanistic insights concerning the role of Hsp70 chaperones in Fe‐S cluster biogenesis. This work is supported by National Institutes of Health Grant AI072443 (to J.A.C.) and Alumni Grants for Graduate Research and Scholarship (to W.‐I. L.).