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dc.contributor.authorNwokoye, Ebelechukwu C.; orcid: 0000-0003-2571-9209
dc.contributor.authorAlNaseem, Eiman; orcid: 0000-0002-7070-8245
dc.contributor.authorCrawford, Robert A.; orcid: 0000-0002-9788-5137
dc.contributor.authorCastelli, Lydia M.; orcid: 0000-0003-3620-4219
dc.contributor.authorJennings, Martin D.; orcid: 0000-0001-6173-0988
dc.contributor.authorKershaw, Christopher J.; orcid: 0000-0001-6625-7894
dc.contributor.authorPavitt, Graham D.; orcid: 0000-0002-8593-2418; email: graham.pavitt@manchester.ac.uk
dc.date.accessioned2021-06-29T15:40:01Z
dc.date.available2021-06-29T15:40:01Z
dc.date.issued2021-06-29
dc.date.submitted2021-04-08
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625081/41598_2021_Article_92931.pdf?sequence=2
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625081/41598_2021_Article_92931_nlm.xml?sequence=3
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625081/41598_2021_92931_MOESM1_ESM.pdf?sequence=4
dc.identifier.citationScientific Reports, volume 11, issue 1, page 13467
dc.identifier.urihttp://hdl.handle.net/10034/625081
dc.descriptionFrom Springer Nature via Jisc Publications Router
dc.descriptionHistory: received 2021-04-08, accepted 2021-06-03, registration 2021-06-18, pub-electronic 2021-06-29, online 2021-06-29, collection 2021-12
dc.descriptionPublication status: Published
dc.descriptionFunder: Tertiary Education Trust Fund; doi: http://dx.doi.org/10.13039/501100008895
dc.descriptionFunder: Office of the Civil Service Commission; doi: http://dx.doi.org/10.13039/501100004283
dc.descriptionFunder: Biotechnology and Biological Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000268; Grant(s): BB/G012571/1, BB/S014667/1, BB/M006565/1
dc.descriptionFunder: Weizmann UK; doi: http://dx.doi.org/10.13039/100014383; Grant(s): 2020 / 129488
dc.description.abstractAbstract: By interacting with the mRNA 5′ cap, the translation initiation factor eIF4E plays a critical role in selecting mRNAs for protein synthesis in eukaryotic cells. Caf20 is a member of the family of proteins found across eukaryotes termed 4E-BPs, which compete with eIF4G for interaction with eIF4E. Caf20 independently interacts with ribosomes. Thus, Caf20 modulates the mRNA selection process via poorly understood mechanisms. Here we performed unbiased mutagenesis across Caf20 to characterise which regions of Caf20 are important for interaction with eIF4E and with ribosomes. Caf20 binding to eIF4E is entirely dependent on a canonical motif shared with other 4E-BPs. However, binding to ribosomes is weakened by mutations throughout the protein, suggesting an extended binding interface that partially overlaps with the eIF4E-interaction region. By using chemical crosslinking, we identify a potential ribosome interaction region on the ribosome surface that spans both small and large subunits and is close to a known interaction site of eIF3. The function of ribosome binding by Caf20 remains unclear.
dc.languageen
dc.publisherNature Publishing Group UK
dc.rightsLicence for this article: http://creativecommons.org/licenses/by/4.0/
dc.sourceeissn: 2045-2322
dc.subjectArticle
dc.subject/631/45
dc.subject/631/337
dc.subject/631/337/574
dc.subject/631/337/574/1789
dc.subjectarticle
dc.titleOverlapping regions of Caf20 mediate its interactions with the mRNA-5′cap-binding protein eIF4E and with ribosomes
dc.typearticle
dc.date.updated2021-06-29T15:40:00Z
dc.date.accepted2021-06-03


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