{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":56,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["20(15)"],"submitter":["Boni IV"],"pubmed_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."],"journal":["The EMBO journal"],"pagination":["4222-32"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC149162"],"repository":["biostudies-literature"],"pubmed_title":["Non-canonical mechanism for translational control in bacteria: synthesis of ribosomal protein S1."],"pmcid":["PMC149162"],"pubmed_authors":["Boni IV","Dreyfus M","Artamonova VS","Tzareva NV"],"view_count":["56"],"additional_accession":[]},"is_claimable":false,"name":"Non-canonical mechanism for translational control in bacteria: synthesis of ribosomal protein S1.","description":"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.","dates":{"release":"2001-01-01T00:00:00Z","publication":"2001 Aug","modification":"2024-12-03T21:52:24.749Z","creation":"2019-03-27T00:17:37Z"},"accession":"S-EPMC149162","cross_references":{"pubmed":["11483525"],"doi":["10.1093/emboj/20.15.4222"]}}