Abstract:
: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.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Abe T,Nagai R,Shimazaki S,Kondo S,Nishimura S,Sakaguchi Y,Suzuki T,Imataka H,Tomita K,Takeuchi-Tomita Ndoi
10.1093/jb/mvaa022subject
Has Abstractpub_date
2020-05-01 00:00:00pages
451-462issue
5eissn
0021-924Xissn
1756-2651pii
5735469journal_volume
167pub_type
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