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http://purl.uniprot.org/citations/12966069http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12966069http://www.w3.org/2000/01/rdf-schema#comment"IscA homologues are involved in iron-sulfur cluster biosynthesis. In the non-nitrogen-fixing cyanobacterium Synechocystis PCC 6803, there are two IscA homologues, SLR1417 and SLR1565 (designated IscA1 and IscA2), of which only IscA2 exists as a protein complex with the HEAT-repeat-containing protein, SLR1098 (IaiH). We observed that the absorption spectrum of the recombinant IscA2/IaiH complex resembles that of IscA2 alone, although it is sharper. In the presence of dithiothreitol, the [2Fe-2S] cluster of IscA2 alone, but not of the IscA2/IaiH complex, became reductively labile upon the addition of sodium dithionite. This implies that the IscA2 moiety of the [2Fe-2S] cluster is stabilized by the presence of IaiH. The [2Fe-2S] cluster of the IscA2/IaiH complex was destabilized by sodium dithionite in the absence of dithiothreitol, suggesting that the in vivo stability of the iron-sulfur cluster in the IscA2/IaiH complex is influenced by the redox state of cellular thiols. When any one of three conserved cysteine residues in IscA2, potential ligands for the [2Fe-2S] cluster, was replaced with serine, the amount of assembled [2Fe-2S] cluster and protein complex was significantly reduced in E. coli cells. The cysteine mutated IscA2/IaiH complexes that were present all contained a [2Fe-2S]-like cluster suggesting that the assembly of a stable iron-sulfur cluster bound to IscA2 is required for efficient and stable complex formation. Truncated IaiH proteins were analyzed using the yeast two-hybrid assay to identify the essential domain of IaiH that interacts physically with IscA2. At least 2 of the 5 N-terminal HEAT repeats of IaiH were found to be required for interaction with IscA2."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvg131"xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/author"Sato S."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/author"Tabata S."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/author"Nakai M."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/author"Morimoto K."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/name"J Biochem"xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/pages"211-217"xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/title"A HEAT-repeats containing protein, IaiH, stabilizes the iron-sulfur cluster bound to the cyanobacterial IscA homologue, IscA2."xsd:string
http://purl.uniprot.org/citations/12966069http://purl.uniprot.org/core/volume"134"xsd:string
http://purl.uniprot.org/citations/12966069http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12966069
http://purl.uniprot.org/citations/12966069http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12966069
http://purl.uniprot.org/uniprot/P27320#attribution-98B3C86582479A50A2C84203AD48312Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/P74596#attribution-98B3C86582479A50A2C84203AD48312Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/P72742#attribution-98B3C86582479A50A2C84203AD48312Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/#_P72742-mappedCitation-12966069http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/#_P74596-mappedCitation-12966069http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/P72742http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12966069
http://purl.uniprot.org/uniprot/P74596http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12966069