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Reference: Lee JH, et al. (1999) Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2. Proc Natl Acad Sci U S A 96(8):4342-7

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Abstract

Binding of initiator methionyl-tRNA to ribosomes is catalyzed in prokaryotes by initiation factor (IF) IF2 and in eukaryotes by eIF2. The discovery of both IF2 and eIF2 homologs in yeast and archaea suggested that these microbes possess an evolutionarily intermediate protein synthesis apparatus. We describe the identification of a human IF2 homolog, and we demonstrate by using in vivo and in vitro assays that human IF2 functions as a translation factor. In addition, we show that archaea IF2 can substitute for its yeast homolog both in vivo and in vitro. We propose a universally conserved function for IF2 in facilitating the proper binding of initiator methionyl-tRNA to the ribosomal P site.

Reference Type
Journal Article | Research Support, U.S. Gov't, Non-P.H.S.
Authors
Lee JH, Choi SK, Roll-Mecak A, Burley SK, Dever TE
Primary Lit For
FUN12 | Eukaryotic translation initiation factor 2 complex

Functional Complementation Annotations 1 entry for 1 complement

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GeneSpeciesGene IDStrain backgroundDirectionDetailsSource
FUN12Homo sapiensHGNC:30793S288Cother complements yeastHuman eukaryotic translation initiation factor 5B (eIF-5B) (ENSP00000289371) is also known as Translation initiation factor IF-2.P-POD
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