Coupled tRNA(Sec)-dependent assembly of the selenocysteine decoding apparatus |
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Authors: | Zavacki Ann Marie Mansell John B Chung Mirra Klimovitsky Boris Harney John W Berry Marla J |
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Institution: | Thyroid Division, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA. |
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Abstract: | SECIS elements recode UGA codons from "stop" to "sense." These RNA secondary structures, present in eukaryotic selenoprotein mRNA 3' untranslated regions, recruit a SECIS binding protein, which recruits a selenocysteine-specific elongation factor-tRNA complex. Elucidation of the assembly of this multicomponent complex is crucial to understanding the mechanism of selenocysteine incorporation. Coprecipitation studies identified the C-terminal 64 amino acids of the elongation factor as sufficient for interaction with the SECIS binding protein. Selenocysteyl-tRNA is required for this interaction; the two factors do not coprecipitate in its absence. Finally, through promoting this interaction, selenocysteyl-tRNA stabilizes the C-terminal domain of the elongation factor. We suggest that the coupling effect is critical to preventing nonproductive decoding attempts and hence forms a basis for effective selenoprotein synthesis. |
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