ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation
- PMID: 28498001
- PMCID: PMC5711452
- DOI: 10.1080/15476286.2016.1269993
ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation
Abstract
For many years initiation and termination of mRNA translation have been studied separately. However, a direct link between these 2 isolated stages has been suggested by the fact that some initiation factors also control termination and can even promote ribosome recycling; i.e. the last stage where post-terminating 80S ribosomes are split to start a new round of initiation. Notably, it is now firmly established that, among other factors, ribosomal recycling critically requires the NTPase ABCE1. However, several earlier reports have proposed that ABCE1 also somehow participates in the initiation complex assembly. Based on an extended analysis of our recently published late-stage 48S initiation complex from rabbit, here we provide new mechanistic insights into this putative role of ABCE1 in initiation. This point of view represents the first structural evidence in which the regulatory role of the recycling factor ABCE1 in initiation is discussed and establishes a corner stone for elucidating the interplay between ABCE1 and several initiation factors during the transit from ribosomal recycling to formation of the elongation competent 80S initiation complex.
Keywords: ABCE1; cryo-EM; recycling; ribosome; translation.
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References
-
- Wagner S, Herrmannová A, Malík R, Peclinovská L, Valášek LS. Functional and biochemical characterization of human eukaryotic translation initiation factor 3 in living cells. Mol Cell Biol 2014; 34:3041-52; PMID:24912683; https://doi.org/10.1128/MCB.00663-14 - DOI - PMC - PubMed
-
- Majumdar R, Bandyopadhyay A, Maitra U. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex. J Biol Chem 2003; 278:6580-7; PMID:12493757; https://doi.org/10.1074/jbc.M210357200 - DOI - PubMed
-
- Hashem Y, des Georges A, Dhote V, Langlois R, Liao HY, Grassucci RA, Hellen CU, Pestova TV, Frank J. Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29. Cell 2013; 153:1108-19; PMID:23706745; https://doi.org/10.1016/j.cell.2013.04.036 - DOI - PMC - PubMed
-
- Aylett CH, Boehringer D, Erzberger JP, Schaefer T, Ban N. Structure of a Yeast 40S–eIF1–eIF1A–eIF3–eIF3j initiation complex. Nat Struct Mol Biol 2015; 22:269-71; PMID:25664723; https://doi.org/10.1038/nsmb.2963 - DOI - PubMed
-
- Hinnebusch AG. The scanning mechanism of eukaryotic translation initiation. Annu Rev Biochem 2014; 83:779-812; PMID:24499181; https://doi.org/10.1146/annurev-biochem-060713-035802 - DOI - PubMed
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