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Boni, I.V. et al.

Boni, Artamonova, Tzareva, Dreyfus,

Non-canonical mechanism for translational control in bacteria: synthesis of ribosomal protein S1.

Translation initiation region (TIR) of the rpsA mRNA encoding ribosomal protein S1 is one of the most efficient in Escherichia coli despite the absence of a canonical Shine-Dalgarno-element. Its high efficiency is under strong negative autogenous control, a puzzling phenomenon as S1 has no strict sequence specificity. To define sequence and structural elements responsible for translational efficiency and autoregulation of the rpsA mRNA, a series of rpsA'-'lacZ chromosomal fusions bearing various mutations in the rpsA TIR was created and tested for beta-galactosidase activity in the absence and presence of excess S1. These in vivo results, as well as data obtained by in vitro techniques and phylogenetic comparison, allow us to propose a model for the structural and functional organization of the rpsA TIR specific for proteobacteria related to E.coli. According to the model, the high efficiency of translation initiation is provided by a specific fold of the rpsA leader forming a non-contiguous ribosome entry site, which is destroyed upon binding of free S1 when it acts as an autogenous repressor.[1]

References

Non-canonical mechanism for translational control in bacteria: synthesis of ribosomal protein S1. Boni, I.V., Artamonova, V.S., Tzareva, N.V., Dreyfus, M. EMBO J. (2001) [Pubmed]

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