Proteomics

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Oxygen-Sensitive Remodeling of Central Carbon Metabolism by Archaic eIF5B


ABSTRACT: The eukaryotic translation initiation factor 5B (eIF5B) is a homolog of the ancient IF2, a translation factor that facilitates initiator methionine-tRNAiMet (met-tRNAiMet) delivery to ribosomes in prokaryotes. IF2 evolved during early anaerobic cellular life and can be traced back to the last universal common ancestor. Here, we show that eIF5B is essential for eukaryotic hypoxia tolerance, reminiscent of how IF2 supports prokaryotic anaerobiosis. Global protein synthesis analyses identified eIF5B as a hypoxia-specific translation factor involved in translocating met-tRNAiMet to initiating ribosomes. Systemic translatome studies revealed that eIF5B-dependent mRNAs encode proteins of central carbon metabolism, fructolysis, and other pathways enhanced in organisms inhabiting hypoxic niches. These pathways rely preferentially on eIF5B rather than eIF2, the canonical initiation factor that delivers met-tRNAiMet during aerobic eukaryotic protein synthesis. We suggest that eIF5B/IF2 was retained during evolution of the aerobic eukaryotic lineage to cope with episodes of oxygen deprivation.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Jonathan Krieger  

LAB HEAD: Stephen Lee

PROVIDER: PXD006799 | Pride | 2018-01-03

REPOSITORIES: Pride

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Publications

Oxygen-Sensitive Remodeling of Central Carbon Metabolism by Archaic eIF5B.

Ho J J David JJD   Balukoff Nathan C NC   Cervantes Grissel G   Malcolm Petrice D PD   Krieger Jonathan R JR   Lee Stephen S  

Cell reports 20180101 1


The eukaryotic translation initiation factor 5B (eIF5B) is a homolog of IF2, an ancient translation factor that enables initiator methionine-tRNAi<sup>Met</sup> (met-tRNAi<sup>Met</sup>) loading on prokaryotic ribosomes. While it can be traced back to the last universal common ancestor, eIF5B is curiously dispensable in modern aerobic yeast and mammalian cells. Here, we show that eIF5B is an essential element of the cellular hypoxic cap-dependent protein synthesis machinery. System-wide interrog  ...[more]

Publication: 1/2

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