| 2004 |
Yeast RLI1 (ABCE1) co-purifies with eIF3, eIF5, and eIF2 but not with elongation or termination factors; depletion reduces polysome content and 40S-bound eIF2/eIF1, indicating a direct role in 43S preinitiation complex assembly. Mutations in conserved ATP-hydrolysis residues are lethal; a dominant-negative NBD2 mutation inhibits translation initiation in vivo and in cell extracts. RLI1-GFP localizes to both nucleus and cytoplasm. |
Affinity co-purification, polysome profiling, dominant-negative mutagenesis, luciferase reporter translation assay, GFP live imaging |
The Journal of biological chemistry |
High |
15277527
|
| 2006 |
Human ABCE1 is essential for in vitro and in vivo mRNA translation and binds eIF2α and eIF5. Inhibition of Xenopus ABCE1 arrests development at the gastrula stage, consistent with a translation block. |
In vitro translation assay, co-immunoprecipitation (eIF2α/eIF5 binding), Xenopus morpholino knockdown with developmental phenotype readout |
The Journal of biological chemistry |
High |
16421098
|
| 2007 |
Crystal structure of Pyrococcus abyssi ABCE1 at 2.8 Å reveals four domains: two NBDs arranged head-to-tail via a hinge domain (suggesting tweezers-like ATP-driven powerstroke), and an N-terminal FeS domain structurally related to bacterial ferredoxins containing two [4Fe-4S] clusters. The FeS domain makes intimate contacts with the Y-loop of NBD1, suggesting a linkage between FeS function and ATP-induced conformational changes. |
X-ray crystallography (2.8 Å resolution) |
The Journal of biological chemistry |
High |
18160405
|
| 2005 |
Crystal structure of P. furiosus RLI twin-cassette ATPase at 1.9 Å reveals two NBDs forming two composite active sites in a head-to-tail interface with a unique hinge domain, consistent with ATP-driven clamp-like motion; establishes the structural basis for ABC domain heterodimers in RLI/ABCE1. |
X-ray crystallography (1.9 Å), yeast in vivo functional analysis of motif mutants |
Structure |
High |
15837203
|
| 2007 |
ABCE1 harbors two essential diamagnetic [4Fe-4S]²⁺ clusters: a ferredoxin-like cluster (Cys 4–7) and a unique ABCE1-type cluster (Cys 1,2,3,8). Seven of the eight conserved coordinating cysteines are essential for cell viability; mutation of Cys6 yields a [3Fe-4S]⁺ state but remains functional; a lethal Cys4 mutation is rescued by ligand swapping with an adjacent eukaryote-conserved cysteine. |
EPR/Mössbauer spectroscopy, biophysical characterization, yeast genetic complementation, site-directed mutagenesis |
The Journal of biological chemistry |
High |
17355973
|
| 2011 |
ABCE1 in archaea drives ribosome recycling via an ATP-dependent conformational switch from open to closed (ATP-occluded) state, which dissociates ribosomes and disengages aRF1. ATP hydrolysis is not required for a single round of ribosome splitting but is required for ABCE1 release from the 30S subunit. The FeS cluster domain is essential for both ribosome binding and recycling. aRF1 directly interacts with ABCE1 and synergistically promotes recycling. |
Biochemical ribosome recycling assay, ATPase mutant analysis, direct interaction assay, conformational state analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
21292982
|
| 2017 |
Cryo-EM structure of yeast 40S-ABCE1 post-splitting complex at 3.9 Å shows the FeS cluster domain rotates ~150° into a binding pocket on the 40S subunit compared to the pre-splitting state. This repositioning (i) confers anti-association activity preventing 60S rejoining, and (ii) its collision trajectory with A-site factors explains the splitting mechanism. ABCE1 is also detected in native 43S initiation complexes. |
Cryo-electron microscopy (3.9 Å), mutational analysis of key interactions, polysome/sedimentation analysis |
Nature structural & molecular biology |
High |
28368393
|
| 2018 |
ABCE1 undergoes an allosterically coupled ATPase cycle for ribosome recycling: ATP occlusion in the low-turnover control site II (NBS2) promotes pre-splitting complex formation and facilitates ATP engagement at the high-turnover site I (NBS1), which drives structural reorganization for ribosome splitting. ATP hydrolysis and ensuing ABCE1 release from the small subunit terminate the post-splitting complex. |
ATPase kinetics with site-specific Walker-B mutants, ribosome splitting assays, functional mutagenesis |
Life science alliance |
High |
30198020
|
| 2020 |
Cryo-EM structure of archaeal 30S-ABCE1 post-splitting complex at 2.8 Å reveals how conformational rearrangements of the FeS cluster domain and hinge regions are coupled to nucleotide-binding site closure, and defines an allosteric network between the ribosome, ABCE1 regulatory domains, and the two structurally and functionally asymmetric ATP-binding sites. |
Cryo-electron microscopy (2.8 Å), mutational analysis, biochemical functional assays |
The EMBO journal |
High |
32064661
|
| 2020 |
Native cryo-EM inventory of yeast and human ABCE1-containing pre-initiation complexes shows ABCE1 predominantly associates with early 43S (and also 48S) initiation complexes, adopts a novel hybrid NBD conformation, and interacts with the N-terminus of eIF3j; eIF3j occupies the mRNA entry channel via its C-terminus, providing a structural explanation for its antagonism of mRNA binding. |
Cryo-electron microscopy of native complexes, biochemical fractionation |
The EMBO journal |
High |
33289941
|
| 2015 |
The yeast proteins Yae1 and Lto1 function as a target-specific CIA adaptor complex that recruits apo-Rli1 (ABCE1) to the CIA Fe-S assembly machinery for Fe-S cluster insertion. Depletion of Yae1 or Lto1 causes defective Fe-S maturation of Rli1 but not other CIA targets. Lto1 uses its conserved C-terminal tryptophan to contact the CIA targeting complex; deca-GX3 motifs in both proteins mediate their complex formation; Yae1 directly recruits Rli1. Human YAE1D1 and ORAOV1 functionally replace their yeast counterparts. |
Systematic protein interaction screens, co-IP, genetic depletion with Fe-S maturation assays, cross-species complementation |
eLife |
High |
26182403
|
| 2018 |
Mitochondrial damage causes stalled translation of C-I30 mRNA on the mitochondrial outer membrane, recruiting Pelo, ABCE1, and the E3 ligase NOT4 to the ribosome/mRNA complex. NOT4 ubiquitinates ABCE1, generating poly-ubiquitin signals that recruit autophagy receptors to the MOM to initiate PINK1-dependent mitophagy. In Drosophila PINK1 mutants, these factors synergistically restore mitophagy and neuromuscular tissue integrity. |
Co-immunoprecipitation, ubiquitination assay, in vivo Drosophila genetics, mitophagy imaging |
Cell metabolism |
High |
29861391
|
| 2020 |
A genome-wide screen reveals that ABCE1 activity (maintained by lysosomal acidification → transferrin-mediated iron uptake → Fe-S cluster biogenesis) is required for proper ribosome recycling; impaired ABCE1 function causes ribosomes to move into 3' UTRs, displacing exon junction complexes and abrogating nonsense-mediated decay (NMD) and other 3' UTR-directed regulatory mechanisms including miRNA- and RNA-binding-protein-mediated repression. |
Genome-wide CRISPR/siRNA screen, ribosome profiling, NMD reporter assays, iron/lysosome perturbation experiments |
Cell reports |
High |
32668236
|
| 2005 |
The NC domain of HIV-1 Gag is required for interaction with endogenous primate ABCE1; specifically, basic residues in NC (not the zinc finger cysteine/histidine residues) are necessary for the Gag-ABCE1 interaction. Constructs failing to interact with ABCE1 also fail to form capsids, implicating ABCE1 in immature HIV-1 capsid assembly intermediates. |
Co-immunoprecipitation with deletion and point mutants, capsid assembly assays |
The Journal of biological chemistry |
High |
16275648
|
| 2011 |
Assembly-competent HIV-1 GagZip chimeras (NC replaced by leucine zipper) form ABCE1-containing capsid assembly intermediates, whereas assembly-incompetent GagZip mutants (disrupted dimerization) do not. This demonstrates that ABCE1 does not bind NC directly or through an RNA bridge; instead, Gag dimerization (mediated by NC or zipper) exposes an ABCE1-binding domain elsewhere in Gag. |
Co-immunoprecipitation with GagZip chimeras, capsid assembly assays, RNase A resistance assay |
Journal of virology |
High |
21543480
|
| 2012 |
ROS toxicity in yeast is primarily mediated through impairment of Rli1 (ABCE1) function: mild oxidative stress impairs Rli1p activity in nuclear ribosomal-subunit export; prooxidant resistance is decreased by RLI1 repression and increased by RLI1 overexpression; the dependency is abolished under anaerobic conditions and accentuated by a FeS cluster-defective Rli1 construct. ROS primarily disrupts [55Fe]S-cluster supply to Rli1p rather than damaging clusters already incorporated. |
Yeast genetic manipulation (RLI1 repression/overexpression), FeS cluster-defective mutant, 55Fe-radiolabeling, anaerobic conditions |
Molecular biology of the cell |
High |
22855532
|
| 2014 |
ABCE1 plays a functional role in nonstop mRNA decay (NSD) in Drosophila cells, acting as the eukaryotic ribosome recycling factor that triggers ribosome rescue at the 3' end of nonstop mRNAs. |
RNAi knockdown in Drosophila cells with NSD reporter assays |
Biochimie |
Medium |
25128630
|
| 2018 |
The ribosomal stalk protein (archaeal aP1) binds via conserved hydrophobic C-terminal residues to NBD1 of aABCE1, and this interaction is crucial for ATPase activation of ABCE1 on the ribosome and for ribosome subunit dissociation; functional role of stalk–ABCE1 interaction is conserved in yeast. |
Biochemical ATPase assay, crystal structure of stalk–NBD1 interaction, yeast mutagenesis/complementation |
Nucleic acids research |
High |
30010948
|
| 2015 |
ABCE1 functions as an endogenous suppressor of RNA silencing in a conserved manner: human ABCE1 suppresses RNA silencing in N. benthamiana, HEK293 cells, and C. elegans. Co-IP/MS identified potential interactors including translin and TRAX, components that support RNAi. |
Cross-species RNA silencing suppression assay, co-immunoprecipitation and mass spectrometry |
PloS one |
Medium |
25659154
|
| 2001 |
A fraction of cellular RNase L and RLI (ABCE1) is localized in mitochondria. Stable transfection of RLI sense cDNA (overexpression) or RNase L antisense prevented IFNα-induced post-transcriptional down-regulation of mitochondrial mRNAs and blocked IFNα-induced cell growth inhibition, demonstrating that ABCE1 (through inhibition of RNase L) mediates IFNα antiproliferative effects via mitochondrial mRNA degradation. |
Subcellular fractionation, stable transfection with RLI sense/RNase L antisense constructs, mitochondrial mRNA stability assays |
The Journal of biological chemistry |
Medium |
11585831
|
| 1998 |
RLI (ABCE1) mRNA is induced by double-stranded RNA (poly(I):poly(C)) but not by interferon; this induction leads to inhibition of RNase L 2-5A-binding activity. RLI protein has rapid turnover, making the inhibition transient. |
Northern blot/Western blot, RNase L activity assay after dsRNA treatment |
Journal of interferon & cytokine research |
Medium |
9877446
|
| 2021 |
Not5 (CCR4-NOT complex) co-purifies with ribosomes and Rli1 (ABCE1) but not with eIF5A; Not4 and Not5 modulate translation elongation in a codon-dependent manner that inversely correlates with eIF5A depletion and positively correlates with Rli1 depletion. Overexpression of wild-type or non-complementing Rli1, and loss of Rps7A ubiquitination, enable Not4 E3 ligase-dependent translation of polyarginine stretches, indicating a moonlighting function of Rli1 in elongation. |
Ribosome profiling, co-purification, genetic epistasis with elongation factor mutants, polyarginine translation reporter |
Cell reports |
Medium |
34469733
|
| 2019 |
ABCE1 is specifically required for efficient translation of paramyxoviral and pneumoviral mRNAs (measles, mumps, RSV) but not for general cellular protein synthesis, indicating that these viral mRNAs exploit specific ABCE1-dependent translation mechanisms. |
Genome-scale siRNA screens, viral replication assays, pulse-labeling of viral vs. cellular proteins after ABCE1 knockdown |
mBio |
Medium |
31088929
|
| 2021 |
ABCE1 regulates RNase L activity and RNase L-induced autophagy during viral infections. ABCE1 knockdown enhances 2-5A-induced RNase L activity and accelerates autophagy onset; enhanced autophagy in ABCE1-depleted cells promotes EMCV replication. ABCE1 depletion sensitizes cells to apoptosis via caspase-3-mediated cleavage of Beclin-1, switching autophagy to apoptosis. |
ABCE1 siRNA knockdown, RNase L activity assay, autophagy and apoptosis assays, EMCV infection |
Viruses |
Medium |
33670646
|
| 2020 |
ABCE1 directly binds to form a complex with RNase L and accelerates RNase L dimer formation in the absence of 2-5A. Depletion of ABCE1 represses 2-5A-induced RNase L activation and stabilizes exogenous RNA, and the double depletion of both ABCE1 and RNase L does not further stabilize RNA beyond single depletion, indicating they act together in RNA decay. This positions ABCE1 as a positive regulator of RNase L-mediated exogenous RNA decay. |
Co-immunoprecipitation, RNase L dimerization assay, RNA stability assays, single/double siRNA depletion |
Viruses |
Medium |
32033097
|
| 2017 |
Abce1 localizes as small dots in the nucleus at the germinal vesicle (GV) stage in mouse oocytes, disperses around the spindle after GVBD, and caps the spindle poles during anaphase/telophase. Knockdown of Abce1 by siRNA injection delays GVBD, impairs first polar body extrusion, disrupts spindle assembly and chromosome alignment, dissociates γ-tubulin and p-MAPK from spindle poles, and causes aneuploidy. |
Immunostaining/confocal microscopy for localization, siRNA injection with meiotic phenotype analysis, γ-tubulin and p-MAPK localization |
Oncotarget |
Medium |
28380459
|
| 2019 |
Tip60 acetyltransferase directly acetylates ABCE1 in lung cancer cells; knockdown of Tip60 decreases ABCE1 acetylation and inhibits lung cancer cell proliferation, invasion, and migration in vitro and tumor growth in vivo. |
Co-immunoprecipitation, Western blot for acetylation, Tip60 siRNA knockdown, xenograft model |
Experimental and therapeutic medicine |
Medium |
30936993
|
| 2016 |
ABCE1 interacts with β-actin (demonstrated by GST pull-down and reciprocal Co-IP). ABCE1 overexpression increases F-actin rearrangement and lung cancer cell migration; the FeS cluster domain of ABCE1 is the key domain mediating β-actin binding, and deletion of FeS clusters reverses the pro-migratory and pro-proliferative effects of ABCE1 overexpression. |
GST pull-down, co-immunoprecipitation, FeS deletion mutagenesis, migration assays, F-actin immunofluorescence |
Oncology reports / Cellular physiology and biochemistry |
Medium |
27109616 29145194
|
| 2007 |
TULA proteins associate with ABCE1 (identified by mass spectrometry) and substantially inhibit production of both sub-genomic and full-length HIV-1 viral particles; this inhibitory effect depends on the UBA domain of TULA, suggesting TULA is recruited to HIV assembly sites via ABCE1 where it disrupts ubiquitylation-dependent late steps of the HIV life cycle. |
Mass spectrometry-based protein interaction, HIV-1 particle production assay, UBA domain mutant analysis |
Virology |
Low |
18006034
|
| 2016 |
ABCE1 depletion by siRNA in human cells causes accumulation in S phase with inefficient DNA synthesis and reduced histone mRNA and protein levels, indicating ABCE1 is essential for histone biosynthesis and normal S phase progression beyond its general translation role. |
siRNA knockdown, BrdU incorporation, flow cytometry cell cycle analysis, histone mRNA/protein quantification |
Cell cycle |
Medium |
26985706
|
| 2021 |
Human ABCE1 mRNA translation is tightly regulated by AUG upstream open reading frames (uORFs) in the 5'-leader sequence in colorectal cells: uORF1 acts as a barrier to downstream uORF translation; ribosomes bypassing uORF1/2 initiate at inhibitory uORF3 or uORF5 that repress main ORF translation. This inhibitory regulation is slightly overcome during ER stress. |
Luciferase reporter assays with uORF mutagenesis, ribosome profiling analysis, ER stress induction |
Biomedicines |
Medium |
34440115
|
| 2025 |
Cryo-EM structure of the AMD1 C-tail-stalled ribosome complex captures eRF1 and ABCE1 trapped together on the ribosome; the AMD1 nascent chain C-tail forms a molecular clamp positioning an arginine finger in the peptidyl-transferase center that blocks eRF1 GGQ motif accommodation, thereby arresting translation termination at the pre-ABCE1-recycling step. |
Cryo-electron microscopy of ribosome-nascent chain complex, structural analysis |
bioRxiv (preprint)preprint |
Medium |
bio_10.1101_2025.11.16.688537
|
| 2025 |
Genetic epistasis in yeast using heterologous eRF3 and ABCE1 factors demonstrates that eRF3 remains bound to the ribosomal GTPase center after eRF1-mediated peptide release, awaiting ABCE1 arrival; eRF3 interacts sequentially with eRF1 and then ABCE1 during final translation termination/recycling steps. |
Yeast conditional double-knockout epistasis using heterologous eRF1/eRF3/ABCE1 variants, genetic complementation |
bioRxiv (preprint)preprint |
Medium |
bio_10.1101_2025.02.05.636767
|