Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation.
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IBA57 localizes to mitochondria
"ISCA1, ISCA2, and IBA57 are localized to mitochondria"
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Depletion of IBA57 specifically affects mitochondrial 4Fe-4S proteins
"The activities of mitochondrial [4Fe-4S] proteins, including aconitase, respiratory complex I, and lipoic acid synthase, were diminished following depletion of the three proteins"
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Affected proteins include aconitase, respiratory complex I, and lipoic acid synthase
"The activities of mitochondrial [4Fe-4S] proteins, including aconitase, respiratory complex I, and lipoic acid synthase, were diminished following depletion of the three proteins"
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Ferrochelatase (a 2Fe-2S protein) is not affected by IBA57 depletion
"the mitochondrial [2Fe-2S] enzyme ferrochelatase and cellular heme content were unaffected"
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
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High-throughput screen identified many proteins not previously known to bind RNA
"nearly one-third were not previously annotated as RNA binding"
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Many hits may not represent physiological RNA-binding functions
"about 15% were not predictable by computational methods to interact with RNA"
Mutation of the iron-sulfur cluster assembly gene IBA57 causes severe myopathy and encephalopathy.
IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex.
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IBA57 forms a 2Fe-2S-bridged complex with ISCA2
"IBA57 forms a heterodimeric complex with ISCA2 by bridging a [2Fe-2S] cluster"
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Cys259 of IBA57 is required for cluster coordination
"the cysteine of the conserved motif characterizing IBA57 protein family and the three conserved cysteines of the ISCA protein family act as cluster ligands"
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Crystal structure at 1.55 A resolution
Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery.
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ISCA2-IBA57 forms a dimer of dimers structure
"a structural organization of dimer of dimers for the [2Fe-2S]2+ ISCA2-IBA57 complex with ISCA2 providing the homodimerization core interface"
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R146 of IBA57 is critical for interaction with ISCA2
"the pathogenic mutation Arg146Trp in IBA57"
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The 2Fe-2S cluster is shared between ISCA2 and IBA57
"The [2Fe-2S] cluster is out of the ISCA2 core while being shared with IBA57"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Defects in the Maturation of Mitochondrial Iron-Sulfur Proteins: Biophysical Investigation of the MMDS3 Causing Gly104Cys Variant of IBA57.
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G104C pathogenic variant destabilizes ISCA2-IBA57 complex
"the G104C-IBA57 mutant has a lower conformational stability than WT-IBA57"
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Does not completely abolish complex formation
"G104C Mutation of IBA57 Does Not Impair the Interaction with ISCA2 upon [2Fe-2S] Cluster Binding"
Multimodal cell maps as a foundation for structural and functional genomics.
Deep research report on IBA57