Abstract：
:In eukaryotes, a crucial step of translation initiation is the binding of the multifactor complex eIF4F to the 5' end of the mRNA, a prerequisite to recruitment of the activated small ribosomal 43S particle. Histone H4 mRNAs have short 5'UTRs, which do not conform to the conventional scanning-initiation model. Here we show that the ORF of histone mRNA contains two structural elements critical for translation initiation. One of the two structures binds eIF4E without the need of the cap. Ribosomal 43S particles become tethered to this site and directly loaded in the vicinity of the AUG. The other structure, 19 nucleotides downstream of the initiation codon, forms a three-way helix junction, which sequesters the m(7)G cap. This element facilitates direct positioning of the ribosome on the cognate start codon. This unusual translation initiation mode might be considered as a hybrid mechanism between the canonical and the IRES-driven translation initiation process.
journal_name
Mol Celljournal_title
Molecular cellauthors
Martin F,Barends S,Jaeger S,Schaeffer L,Prongidi-Fix L,Eriani Gdoi
10.1016/j.molcel.2010.12.019subject
Has Abstractpub_date
2011-01-21 00:00:00pages
197-209issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(10)01004-Xjournal_volume
41pub_type
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