PMID:11483525
| Citation |
Boni, IV, Artamonova, VS, Tzareva, NV and Dreyfus, M (2001) Non-canonical mechanism for translational control in bacteria: synthesis of ribosomal protein S1. EMBO J. 20:4222-32 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC149162 Online version:10.1093/emboj/20.15.4222 |
| Keywords |
5' Untranslated Regions; Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Base Sequence; Binding Sites; Escherichia coli/genetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Peptide Chain Initiation, Translational; Phylogeny; Protein Biosynthesis; Proteobacteria/genetics; RNA, Bacterial/chemistry; Ribosomal Proteins/biosynthesis; Ribosomal Proteins/genetics |
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