Role of the C-terminal tail of SmpB in the early stage of trans-translation

• DOI: 10.1261/rna.1916610
• Publication Date: 2010-03-27T02:41:42Z
• Authors: Daisuke Kurita; Akira Muto; Hyouta Himeno
• Keywords: A-site

Trans -translation relieves a stalled translation on the bacterial ribosome by transfer-messenger RNA (tmRNA) with help of SmpB, an essential cofactor tmRNA. Here, we examined role unstructured C-terminal tail SmpB using in vitro trans system. It was found that truncation or substitution tryptophan residue at 147 middle affected activity early stage -translation. Our investigations also revealed is not required for events until GTP hydrolyzed EF-Tu complex tmRNA-SmpB. A synthetic peptide corresponding to inhibited peptidyl-transfer alanyl-tmRNA and A-site binding but hydrolysis. These results suggest has step accommodation alanyl-tmRNA-SmpB into A-site. Directed hydroxyl radical probing indicated located just downstream decoding center mRNA path when