Direct ribosomal binding by a cellular inhibitor of translation.

Imagen de Daniel Alfonso Colón-Ramos
PDF versionPDF version
TítuloDirect ribosomal binding by a cellular inhibitor of translation.
Publication TypeJournal Article
Year of Publication2006
AutoresColón-Ramos, DA, Shenvi, CL, Weitzel, DH, Gan, EC, Matts, R, Cate, J, Kornbluth, S
JournalNat Struct Mol Biol
Volume13
Issue2
Pagination103-11
Date Published2006 Feb
ISSN1545-9993
Palabras claveAnimals, Biological Transport, Codon, Initiator, DNA Repair, Drosophila melanogaster, Drosophila Proteins, Phosphorylation, Protein Binding, Protein Biosynthesis, Rabbits, Ribosomes, RNA, Messenger
Abstract

During apoptosis and under conditions of cellular stress, several signaling pathways promote inhibition of cap-dependent translation while allowing continued translation of specific messenger RNAs encoding regulatory and stress-response proteins. We report here that the apoptotic regulator Reaper inhibits protein synthesis by binding directly to the 40S ribosomal subunit. This interaction does not affect either ribosomal association of initiation factors or formation of 43S or 48S complexes. Rather, it interferes with late initiation events upstream of 60S subunit joining, apparently modulating start-codon recognition during scanning. CrPV IRES-driven translation, involving direct ribosomal recruitment to the start site, is relatively insensitive to Reaper. Thus, Reaper is the first known cellular ribosomal binding factor with the potential to allow selective translation of mRNAs initiating at alternative start codons or from certain IRES elements. This function of Reaper may modulate gene expression programs to affect cell fate.

DOI10.1038/nsmb1052
Alternate JournalNat. Struct. Mol. Biol.
PubMed ID16429152