Structural highlights
Function
A0A0J9X202_LACKL Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.[ARBA:ARBA00025502][RuleBase:RU004365]
Publication Abstract from PubMed
Eukaryotic translation initiation requires cooperative assembly of a large protein complex at the 40S ribosomal subunit. We have resolved a budding yeast initiation complex by cryo-EM, allowing placement of prior structures of eIF1, eIF1A, eIF3a, eIF3b and eIF3c. Our structure highlights differences in initiation-complex binding to the ribosome compared to that of mammalian eIF3, demonstrates a direct contact between eIF3j and eIF1A and reveals the network of interactions between eIF3 subunits.
Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex.,Aylett CH, Boehringer D, Erzberger JP, Schaefer T, Ban N Nat Struct Mol Biol. 2015 Mar;22(3):269-71. doi: 10.1038/nsmb.2963. Epub 2015 Feb, 9. PMID:25664723[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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 Mar;22(3):269-71. doi: 10.1038/nsmb.2963. Epub 2015 Feb, 9. PMID:25664723 doi:http://dx.doi.org/10.1038/nsmb.2963
