Gene Ontology annotation through association of InterPro records with GO terms
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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization.
-
Alternative AUG usage generates mitochondrial and cytosolic/nuclear NFS1 isoforms
"different forms of NifS that localize either to mitochondria or to the cytosol and nucleus are synthesized from a single transcript"
Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells.
Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly.
-
Cytosolic NFS1 is an active cysteine desulfurase
"the cytosolic form of ISCS is an active cysteine desulfurase that covalently binds 35S acquired from desulfuration of radiolabeled cysteine"
-
NFS1 homodimerizes and forms complex with ISCU
"Human cytosolic ISCS dimerized as efficiently as bacterial ISCS"
-
Can support [4Fe-4S] cluster formation on IRP1
"the cytosolic forms of ISCS and ISCU facilitated efficient formation of a [4Fe-4S] cluster on IRP1"
Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation.
-
NFS1 is essential for both mitochondrial and cytosolic Fe-S protein biogenesis
"huNfs1 performs an essential function in Fe/S protein biogenesis in human cells"
-
Mitochondrial localization is required for function
"huNfs1 is required inside mitochondria for efficient maturation of cellular Fe/S proteins"
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.
-
NFS1 interacts with LYRM4/ISD11 for activity
"A variant of Nfs1 was purified in conjunction with Isd11"
-
NFS1 transfers sulfur to MOCS3 for Moco biosynthesis
"sulfur is transferred from L-cysteine to MOCS3-RLD via an Nfs1-bound persulfide intermediate"
Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex.
Mammalian frataxin - an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
-
NFS1 detected in cytosol, mitochondria, and nucleus
"we were also able to detect NFS1 in the cytosolic fraction"
-
NFS1 interacts with MOCS3 in cytosol by FRET
"Here, we present direct data to show the interaction of NFS1 and MOCS3 in the cytosol of human cells using Förster resonance energy transfer and a split-EGFP system"
Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU).
Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.
Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly.
Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery.
Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.
Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.
-
Crystal structures of NFS1-ISD11-ACP with and without ISCU
"crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU"
-
NFS1 functions as homodimer
"The three structures with a central NFS1 dimer"
-
ISD11 stabilizes NFS1 but does not directly participate in catalysis
"ISD11 binds to NFS1 distal from the desulfurase active site and does not directly participate in catalysis"
-
PLP bound to Lys258
"The large domain of NFS1 (residues 71-315) harbors the PLP cofactor, which is covalently bound to Lys258 as an internal aldimine"
Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the CIAO1-mediated transfer to recipients.
Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent Localization of NFS1 at the Tips of the Centrosome.
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism.
-
3.2 A cryo-EM structure of FXN-bound ISC complex
"Here the 3.2 Å resolution cryo-electron microscopy structure of the FXN-bound active human complex, containing two copies of the NFS1-ISD11-ACP-ISCU-FXN hetero-pentamer, delineates the interactions of FXN with other component proteins of the complex"
-
FXN binds at interface of two NFS1 and one ISCU
"FXN binds at the interface of two NFS1 and one ISCU subunits"
Structure of the Human ACP-ISD11 Heterodimer.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization.
Mechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2.
-
Cryo-EM snapshots of persulfide transfer from NFS1 Cys381 to ISCU2 Cys138
"High-resolution cryo-EM structures obtained from anaerobically prepared samples provide snapshots that both visualize different stages of persulfide transfer from Cys381NFS1 to Cys138ISCU2"
-
Clarifies molecular role of frataxin
"clarify the molecular role of frataxin in optimally positioning assembly site residues for fast sulfur transfer"
FXN:NFS1:ISD11:ISCU assembles 2Fe-2S iron-sulfur cluster
Mitochondrial iron-sulfur cluster biogenesis
PXLP-K198-NFS1 transfers sulfur from cysteine onto MOCS3
Transfer of Fe-S clusters to SDHB
2Fe-2S is inserted in UQCRFS1
Deep research on NFS1 function and mechanism