Journal
JOURNAL OF BIOCHEMISTRY
Volume 167, Issue 5, Pages 451-462Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvaa022
Keywords
eIF5A; hypusine; intrinsic ribosome destabilization; in vitro translation; polyproline
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Funding
- MEXT/JSPS Grant-inAid for Scientific Research [26116002]
- Takeda Science Foundation
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [26116002] Funding Source: KAKEN
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We have recently developed an in vitro yeast reconstituted translation system, which is capable of synthesizing long polypeptides. Utilizing the system, we examined the role of eIF5A and its hypusine modification in translating polyproline sequence within long open reading frames. We found that polyproline motif inserted at the internal position of the protein arrests translation exclusively at low Mg2+ concentrations, and peptidylpolyproline-tRNA intrinsically destabilizes 80S ribosomes. We demonstrate that unmodified eIF5A essentially resolves such ribosome stalling; however, the hypusine modification drastically stimulates ability of eIF5A to rescue polyproline-mediated ribosome stalling and is particularly important for the efficient translation of the N-terminal or long internal polyproline motifs.
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