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Title:
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Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters
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Author:
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Bandyopadhyay, Sibali; Gama, Filipe; Molina Navarro, Maria Micaela; Gualberto, José Manuel; Claxton, Ronald; Huynh, Boi Hanh; Herrero Perpiñán, Enrique; Jacquot, Jean Pierre; Johnson, Michael K.; Naik, Sunil G.; Rouhier, Nicolas
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Notes:
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Glutaredoxins (Grxs) are small oxidoreductases that
reduce disulphide bonds or protein-glutathione mixed
disulphides. More than 30 distinct grx genes are expressed
in higher plants, but little is currently known concerning
their functional diversity. This study presents biochemical
and spectroscopic evidence for incorporation of a
[2Fe–2S] cluster in two heterologously expressed chloroplastic
Grxs, GrxS14 and GrxS16, and in vitro cysteine
desulphurase-mediated assembly of an identical [2Fe–2S]
cluster in apo-GrxS14. These Grxs possess the same monothiol
CGFS active site as yeast Grx5 and both were able to
complement a yeast grx5 mutant defective in Fe–S cluster
assembly. In vitro kinetic studies monitored by CD spectroscopy
indicate that [2Fe–2S] clusters on GrxS14 are rapidly
and quantitatively transferred to apo chloroplast ferredoxin.
These data demonstrate that chloroplast CGFS Grxs
have the potential to function as scaffold proteins for
the assembly of [2Fe–2S] clusters that can be transferred
intact to physiologically relevant acceptor proteins.
Alternatively, they may function in the storage and/or
delivery of preformed Fe–S clusters or in the regulation
of the chloroplastic Fe–S cluster assembly machinery. |
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Subject(s):
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-chloroplast
-glutaredoxin
-iron-sulphur protein |
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Rights:
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(c) European Molecular Biology Organization, 2008
info:eu-repo/semantics/restrictedAccess |
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Document type:
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article
publishedVersion |
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Published by:
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EMBO Press
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