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Field | Value |
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Namespace | Biological process |
Short description | Protein maturation by iron-sulfur cluster transfer |
Full defintion | The transfer of an assembled iron-sulfur cluster from a scaffold protein to an acceptor protein that contributes to the attainment of the full functional capacity of a protein. |
Subterm of |
The relationship of GO:0097428 with other GO terms.
Relationship type | GO terms |
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Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0097428, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
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GOC | mah |
PMID | Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange. Biochemistry. 2011 Nov 8; 50 (44): 9641–50.PMID: 21977977 The scaffold protein IscU and molecular chaperones HscA and HscB play central roles in biological assembly of iron-sulfur clusters and maturation of iron-sulfur proteins. However, the structure of IscU-FeS complexes and the molecular mechanism whereby the chaperones facilitate cluster transfer to acceptor proteins are not well understood. We have prepared amino acid substitution mutants of Escherichia coli IscU in which potential ligands to the FeS cluster (Cys-37, Cys-63, His-105, and Cys-106) were individually replaced with alanine. The properties of the IscU-FeS complexes formed were investigated by measuring both their ability to transfer preformed FeS clusters to apo-ferredoxin and the activity of the IscU proteins in catalyzing cluster assembly on apo-ferredoxin using inorganic iron with inorganic sulfide or with IscS and cysteine as a sulfur source. The ability of the HscA/HscB chaperone system to accelerate ATP-dependent cluster transfer from each IscU substitution mutant to apo-ferredoxin was also determined. All of the mutants formed FeS complexes with a stoichiometry similar to the wild-type holo-protein, i.e., IscU(2)[2Fe2S], raising the possibility that different cluster ligation states may occur during iron-sulfur protein maturation. Spectroscopic properties of the mutants and the kinetics of transfer of performed IscU-FeS clusters to apo-ferredoxin indicate that the most stable form of holo-IscU involves iron coordination by Cys-63 and Cys-106. Results of studies on the ability of mutants to catalyze formation of holo-ferredoxin using iron and different sulfur sources were consistent with proposed roles for Cys-63 and Cys-106 in FeS cluster binding and also indicated an essential role for Cys-106 in sulfide transfer to IscU from IscS. Measurements of the ability of the chaperones HscA and HscB to facilitate cluster transfer from holo-IscU to apo-ferredoxin showed that only IscU(H105A) behaved similarly to wild-type IscU in exhibiting ATP-dependent stimulation of cluster transfer. IscU(C63A) and IscU(C106A) displayed elevated rates of cluster transfer in the ±ATP whereas IscU(C37A) exhibited low rates of cluster transfer ±ATP. In interpreting these findings, we propose that IscU(2)[2Fe2S] is able undergo structural isomerization to yield conformers having different cysteine residues bound to the cluster. On the basis of the crystal structure of HscA complexed with an IscU-derived peptide, we propose that the chaperone binds and stabilizes an isomer of IscU(2)[2Fe2S] in which the cluster is bound by cysteine residues 37 and 63 and that the [2Fe2S] cluster, being held less tightly than that coordinated by Cys-63 and Cys-106 in free IscU(2)[2Fe2S], is more readily transferred to acceptor proteins such as apo-ferredoxin. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | Iron-sulfur assembly protein IscA-like protein [Medicago truncatula] gi|357511065|ref|XP_003625821.1| | 3 | ||
– | PREDICTED: iron-sulfur assembly protein IscA-like 2, mitochondrial-like isoform X1 [Cicer arietinum] gi|502111834|ref|XP_004494179.1| | 3 | ||
– | PREDICTED: iron-sulfur assembly protein IscA, chloroplastic-like [Cicer arietinum] gi|502140001|ref|XP_004504011.1| | 3 | ||
– | PREDICTED: iron-sulfur assembly protein IscA, chloroplastic-like [Cicer arietinum] gi|502140001|ref|XP_004504011.1| | 3 | ||
– | MMS19 nucleotide excision repair protein like; TAIR: AT5G48120.1 ARM repeat superfamily protein; Swiss-Prot: sp|Q0WVF8|MMS19_ARATH MMS19 nucleotide excision repair protein homolog; TrEMBL-Plants: tr|K7M923|K7M923_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0202000 | 1 | ||
– | MMS19 nucleotide excision repair protein like; TAIR: AT5G48120.1 ARM repeat superfamily protein; Swiss-Prot: sp|Q0WVF8|MMS19_ARATH MMS19 nucleotide excision repair protein homolog; TrEMBL-Plants: tr|K7M923|K7M923_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0202000 | 1 | ||
– | Iron-sulfur cluster insertion protein ErpA; TAIR: AT5G03905.1 Iron-sulfur cluster biosynthesis family protein; Swiss-Prot: sp|Q8LCY2|ISAM2_ARATH Iron-sulfur assembly protein IscA-like 2, mitochondrial; TrEMBL-Plants: tr|I3SBC4|I3SBC4_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0675900 | 3 | ||
– | Iron-sulfur cluster insertion protein erpA; TAIR: AT2G16710.1 Iron-sulfur cluster biosynthesis family protein; Swiss-Prot: sp|Q8LBM4|ISAM1_ARATH Iron-sulfur assembly protein IscA-like 1, mitochondrial; TrEMBL-Plants: tr|I1JQ14|I1JQ14_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0676300 | 3 | ||
– | Iron-sulfur cluster insertion protein ErpA; TAIR: AT5G03905.1 Iron-sulfur cluster biosynthesis family protein; Swiss-Prot: sp|Q8LCY2|ISAM2_ARATH Iron-sulfur assembly protein IscA-like 2, mitochondrial; TrEMBL-Plants: tr|I3SWV2|I3SWV2_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0741100 | 3 | ||
– | Co-chaperone, HscB-like protein; TAIR: AT5G06410.1 DNAJ heat shock N-terminal domain-containing protein; Swiss-Prot: sp|Q8IWL3|HSC20_HUMAN Iron-sulfur cluster co-chaperone protein HscB, mitochondrial; TrEMBL-Plants: tr|I1L9M4|I1L9M4_SOYBN Uncharacterized protein; Found in the gene: LotjaGi5g1v0107400 | 3 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Biological process | Protein maturation by iron-sulfur cluster transfer | 1 | 10.00 |