Recombinant Human NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (NFU1)

1. data support a hypothesis in which Nfu can serve as an alternative carrier protein for chaperone-mediated cluster release and delivery in Fe-S cluster biogenesis and trafficking PMID: 29211945
2. NFU1 gene mutations may cause severe mitochondrial respiratory chain defects, mitochondrial encephalomyopathies and death, early in life (Review) PMID: 27381105
3. Novel NFU1 variants were identified in Chinese patients with multiple mitochondrial dysfunctions syndrome. PMID: 28470589
4. report the results of an investigation on the effect of these substitutions on both cluster coordination and NFU1 structure and function PMID: 28906593
5. Gly189Arg substitution on NFU1 is associated with multiple mitochondrial dysfunctions syndrome 1. PMID: 28906594
6. a direct role for human Nfu in the process of [2Fe-2S] cluster trafficking and delivery PMID: 27538573
7. Analysis of protein stability and oligomeric state demonstrates that the Gly208Cys mutant increases the propensity to dimerize and perturbs the secondary structure composition. These changes appear to underlie the severely decreased ability of mutant NFU1 to accept an Fe/S cluster from physiologically relevant sources. PMID: 28161430
8. Study used NMR spectroscopy and small-angle X-ray scattering data to determine the 3D structure of human mitochondrial NFU1 in its apo- and iron-sulfur cluster-containing holo-form. Apo- NFU1 is monomeric, whereas holo-NFU1 consists of a trimer of three [4Fe-4S] cluster-linked dimers. PMID: 27818104
9. a leaky splicing regulation due to a splice site mutation (c.545+5G>A) that produces small amounts of wild type NFU1 mRNA that might result in enough protein to partially lipoylate and restore the activity of lipoic acid-dependent enzymes and the assembly and activity of complex I. PMID: 26688339
10. A new NFU1 mutation is reported in a patient presenting with a milder phenotype characterized by a later onset, a slowly progressive spastic paraparesis with relapsing-remitting episodes, mild cognitive impairment and a long survival. PMID: 25758857
11. This study provides new insights into the molecular bases of NFU1 disease. PMID: 23179554
12. A fatal mitochondrial disease is associated with defective NFU1 function in the maturation of a subset of mitochondrial Fe-S proteins PMID: 22077971
13. Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes [case report] PMID: 21944046
14. Analyses of genomic DNA, transcripts, and translation products indicate that alternative splicing of a common pre-mRNA results in synthesis of two Nfu isoforms with distinct subcellular localizations. PMID: 12886008
15. Laforin interacts with HIRIP5. PMID: 12915448
16. NFU binds to NifS and reduces the persulfide bond on activated NifS (following formation of the persulfide bond by abstraction of S from the Cys amino acid), yielding inorganic sulfide on a time frame that is compatible with Fe-S cluster assembly. PMID: 19146390
17. NFU is a functionally competent reducing agent for cysteinyl persulfide bond cleavage, releasing inorganic sulfide for incorporation into the iron-sulfur-bound [2Fe-2S] cluster, a reactivity that may be facilitated by flexibility of the C-terminal domain. PMID: 19722697

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HGNC: 16287

OMIM: 605711

KEGG: hsa:27247

STRING: 9606.ENSP00000387219

UniGene: Hs.430439