eIF5A promotes translation of polyproline motifs.
eIF5A promotes translation of polyproline motifs.
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DOI:
10.1016/j.molcel.2013.04.021
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发表时间:
2013-07-11
期刊:
影响因子:
16
通讯作者:
Dever, Thomas E.
中科院分区:
文献类型:
--
作者:
Gutierrez, Erik;Shin, Byung-Sik;Woolstenhulme, Christopher J.;Kim, Joo-Ran;Saini, Preeti;Buskirk, Allen R.;Dever, Thomas E.
Translation factor eIF5A, containing the unique amino acid hypusine, was originally shown to stimulate methionyl-puromycin synthesis, a model assay for peptide bond formation. More recently, eIF5A was shown to promote translation elongation; however, its precise requirement in protein synthesis has remained elusive. Here we use in vivo assays in yeast and in vitro reconstituted translation assays to reveal a specific requirement for eIF5A to promote peptide-bond formation between consecutive proline residues. Addition of eIF5A relieves ribosomal stalling during translation of three consecutive proline residues in vitro, and loss of eIF5A function impairs translation of polyproline-containing proteins in vivo. Hydroxyl radical probing experiments localized eIF5A near the E site of the ribosome with its hypusine residue adjacent to the acceptor stem of the P-site tRNA. Thus, eIF5A, like its bacterial ortholog EFP, is proposed to stimulate the peptidyl-transferase activity of the ribosome and facilitate the reactivity of poor substrates like proline.
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影响因子:
16
作者:
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通讯作者:
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DOI:
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发表时间:
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DOI:
10.1073/pnas.72.11.4257
发表时间:
1975-01-01
影响因子:
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作者:
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通讯作者:
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