The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
eIF5A Promotes Translation of Polyproline Motifs
Open accessAbstract
SUMMARY 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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Cites
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EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues
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Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches
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Self-citationCrystal Structure of the Eukaryotic Ribosome
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Cited by
The bacterial translation stress response.
Starosta, A. L., Lassak, J., Jung, K., & Wilson, D. N. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12083 · Cited by 210
Biosynthesis of polyamines and polyamine-containing molecules
Michael, A. J. (2016) · Biochemical Journal · doi:10.1042/bcj20160185 · Cited by 180
Sequence selectivity of macrolide-induced translational attenuation
Davis, A. R., Gohara, D. W., & Yap, M.-N. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410356111 · Cited by 123
Alsaleh, G., Panse, I., Swadling, L., Zhang, H., Richter, F. C., Meyer, A., Lord, J., Barnes, E., Klenerman, P., Green, C., et al. (2020) · eLife · doi:10.7554/elife.57950 · Cited by 120
“Spermidine provides a moiety to the translation factor eIF5A, which in addition to its role in initiation and termination also promotes the translation of polyproline-rich domains, which are difficult to translate (Gutierrez et al., 2013).”
Tan, T. C. J., Kelly, V., Zou, X., Wright, D., Ly, T., & Zamoyska, R. (2022) · Nature Communications · doi:10.1038/s41467-022-35252-y · Cited by 30
Metadata
- Authors
- Gutierrez, E., Shin, B.-S., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., & Dever, T. E.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 51
- Issue
- 1
- Pages
- 35-45
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1968202347
- Cited by
- 522
- References
- 41
- FWCI
- 16.81
- Type
- journal article
- Language
- en
- Open access
- bronze
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