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• W2100099285 abstract "Trans -translation relieves a stalled translation on the bacterial ribosome by transfer-messenger RNA (tmRNA) with the help of SmpB, an essential cofactor of tmRNA. Here, we examined the role of the unstructured C-terminal tail of SmpB using an in vitro trans -translation system. It was found that truncation of the C-terminal tail or substitution of tryptophan residue at 147 in the middle of the C-terminal tail affected the activity in the early stage of trans -translation. Our investigations also revealed that the C-terminal tail is not required for the events until GTP is hydrolyzed by EF-Tu in complex with tmRNA-SmpB. A synthetic peptide corresponding to the C-terminal tail of SmpB inhibited peptidyl-transfer of alanyl-tmRNA and A-site binding of SmpB, but not GTP hydrolysis. These results suggest that the C-terminal tail has a role in the step of accommodation of alanyl-tmRNA-SmpB into the A-site. Directed hydroxyl radical probing indicated that tryptophan residue at 147 is located just downstream of the decoding center in the mRNA path when SmpB is in the A-site." @default.
• W2100099285 created "2016-06-24" @default.
• W2100099285 creator A5028074922 @default.
• W2100099285 creator A5090643088 @default.
• W2100099285 creator A5091207829 @default.
• W2100099285 date "2010-03-26" @default.
• W2100099285 modified "2023-09-26" @default.
• W2100099285 title "Role of the C-terminal tail of SmpB in the early stage of <i>trans</i>-translation" @default.
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• W2100099285 doi "https://doi.org/10.1261/rna.1916610" @default.
• W2100099285 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2856891" @default.
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