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Interaction of different tRNAs with translation elongation factors 1A from lower and higher eukaryotes

Interaction of different tRNAs with translation elongation factors 1A from lower and higher eukaryotes

The work is aimed at confirmation of earlier assumed mechanism of tRNA channeling. Methods. The methods of band shift assay and Forsters resonance energy transfer were used. Results. The affinities of mammalian tRNAs for two tissue specific isoforms of elongator factor eEF1A1 and eEF1A2 were compare...

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Bibliographic Details
Main Authors: Futernyk, P.V., Negrutskii, B.S., El'skaya, A.V.
Format: Article
Language:English
Published: Інститут молекулярної біології і генетики НАН України 2009
Series:Вiopolymers and Cell
Subjects:
Структура та функції біополімерів
Online Access:http://dspace.nbuv.gov.ua/handle/123456789/153843
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Summary:The work is aimed at confirmation of earlier assumed mechanism of tRNA channeling. Methods. The methods of band shift assay and Forsters resonance energy transfer were used. Results. The affinities of mammalian tRNAs for two tissue specific isoforms of elongator factor eEF1A1 and eEF1A2 were compared. For the first time we have shown the ability of yeast eEF1A*GDP to form non-canonical ternary complex with deacylated tRNAs. The complexation of eukaryotic eEF1A with initiator tRNA, of both bacterial and mammalian origin, was also demonstrated. Conclusions. The formation of the non-canonical complexes of eEF1A*GDP with deacylated tRNAs is common for higher and lower eukaryotes, which is in favor of universality of eukaryotic tRNA-channeling.

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