Direct ribosomal binding by a cellular inhibitor of translation.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Colón-Ramos, DA; Shenvi, CL; Weitzel, DH; Gan, EC; Matts, R; Cate, J; Kornbluth, S

Published Date

  • February 2006

Published In

Volume / Issue

  • 13 / 2

Start / End Page

  • 103 - 111

PubMed ID

  • 16429152

Pubmed Central ID

  • 16429152

Electronic International Standard Serial Number (EISSN)

  • 1545-9985

International Standard Serial Number (ISSN)

  • 1545-9993

Digital Object Identifier (DOI)

  • 10.1038/nsmb1052

Language

  • eng