A monthly journal publishing high-quality, peer-reviewed research on all topics related to RNA and its metabolism in all organisms

The ATPase ABCE1, a member of the ubiquitous ATP-Binding Cassette protein superfamily, is essential in eukaryotic and archaeal ribosome recycling. It comprises a pair of homologous nucleotide-binding ...

Read the full paper: Profound alterations of cancer transcriptomes by the RNase L inhibitor ABCE1 through the modulation of UU/UA-dinucleotide rich transcript abundance

The ATPase ABCE1, a member of the ubiquitous ATP-Binding Cassette protein superfamily, is essential in eukaryotic and archaeal ribosome recycling. It comprises a pair of homologous nucleotide-binding ...

Ribosome-associated quality control (RQC) monitors ribosomes for aberrant translation. While the role of RQC in neurodegenerative disease is beginning to be appreciated, its involvement in cancer is understudied. Here, we show a positive correlation between RQC proteins ABCE1 and ZNF598 and hi...

Background Myalgic Encephalomyelitis/Chronic Fatigue Syndrome (ME/CFS) is a debilitating condition that can lead to severe impairment of physical, psychological, cognitive, social, and occupational fu...

Zhu et al. find a critical role of the ribosome recycling factor ABCE1 in nonsense-mediated decay and other forms of 3ʹ UTR-mediated regulation. The iron-sulfur cluster of ABCE1 is highly sensitive to lysosomal dysfunction and reactive oxygen species, linking these pathologic stresses to defective post-transcriptional control.

In eukaryotic translation, the termination and recycling phases are linked to subsequent initiation by persistence of several factors. These comprise the large eIF3 complex, eIF3j (Hcr1 in yeast) and the ATP-binding cassette protein ABCE1 (Rli1 in yeast). The ATPase is mainly active as a recycling factor, but it can remain bound to the dissociated 40S subunit until formation of 43S pre-initiation complexes. However, its functional role and native architectural context remains largely enigmatic. Here, we present an architectural inventory of native yeast and human ABCE1-containing pre-initiation complexes by cryo-EM. We found that ABCE1 was mostly associated with early 43S but also later 48S phases of initiation. It directly interacted with eIF3j via its unique iron-sulfur cluster domain and adopted a novel hybrid conformation, which was ATPase-inhibited and stabilized by an unknown factor bound between the nucleotide binding sites. Moreover, the native human samples provided a near-complete molecular picture of the architecture and sophisticated interaction network of the 43S-bound eIF3 complex and also the eIF2 ternary complex containing the initiator tRNA. ### Competing Interest Statement The authors have declared no competing interest.