The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes

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dc.contributor.author Luna, Rafael E.
dc.contributor.author Arthanari, Haribabu
dc.contributor.author Hiraishi, Hiroyuki
dc.contributor.author Akabayov, Barak
dc.contributor.author Tang, Leiming
dc.contributor.author Cox, Christian
dc.contributor.author Markus, Michelle A.
dc.contributor.author Luna, Lunet E.
dc.contributor.author Ikeda, Yuka
dc.contributor.author Watanabe, Ryosuke
dc.contributor.author Bedoya, Edward
dc.contributor.author Yu, Cathy
dc.contributor.author Alikhan, Shums
dc.contributor.author Wagner, Gerhard
dc.contributor.author Asano, Katsura
dc.date.accessioned 2014-05-06T19:41:43Z
dc.date.available 2014-05-06T19:41:43Z
dc.date.issued 2014-05-06
dc.identifier.uri http://hdl.handle.net/2097/17685
dc.description.abstract Scanning of the mRNA transcript by the preinitiation complex (PIC) requires a panel of eukaryotic initiation factors including eIF1 and eIF1A, the main transducers of stringent AUG selection. eIF1A plays an important role in start codon recognition; however, its molecular contacts with eIF5 are unknown. Using NMR, we unveil eIF1A’s binding surface on the carboxyl-terminal domain of eIF5 (eIF5-CTD). We validated this interaction by observing that eIF1A does not bind to an eIF5-CTD mutant, altering the revealed eIF1A-interaction site. We also found that the interaction between eIF1A:eIF5-CTD is conserved between human and yeast. Using GST pull down assays of purified proteins, we showed that the N-terminal tail (NTT) of eIF1A mediates the interaction with eIF5-CTD and eIF1. Genetic evidence indicates that overexpressing eIF1 or eIF5 suppresses the slow growth phenotype of eIF1A-NTT mutants. These results suggest that the eIF1A:eIF5-CTD interaction during scanning PICs contributes to the maintenance of eIF1 within the open PIC. en_US
dc.language.iso en_US en_US
dc.relation.uri http://pubs.acs.org/doi/full/10.1021/bi4009775 en_US
dc.rights Permission to archive granted by American Chemical Society, March 20, 2014. This document is the unedited Author's version of a Submitted Work that was subsequently accepted for publication in Biochemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see http://pubs.acs.org/doi/full/10.1021/bi4009775 en_US
dc.subject Preinitiation complex en_US
dc.subject Eukaryotic initiation factors en_US
dc.subject eIF1 en_US
dc.subject eIF1A en_US
dc.subject eIF5 en_US
dc.title The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes en_US
dc.type Article (author version) en_US
dc.date.published 2013 en_US
dc.citation.doi doi:10.1021/bi4009775 en_US
dc.citation.epage 9518 en_US
dc.citation.issue 52 en_US
dc.citation.jtitle Biochemistry en_US
dc.citation.spage 9510 en_US
dc.citation.volume 52 en_US
dc.contributor.authoreid hiraishi en_US
dc.contributor.authoreid kasano en_US


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