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. 2013 Jul 23;14(9):811–816. doi: 10.1038/embor.2013.106

Figure 1.

Figure 1

Biochemical characterization. (A) The normal elongation cycle of translation: a cognate, aminoacylated tRNA (purple) in complex with EF-Tu (orange) and GTP is delivered to the A-site of the ribosome (left). Following peptidyl transfer and the formation of hybrid tRNA states (middle), EF-G catalyses the translocation of tRNA and mRNA in the 30S subunit (right). (B) During starvation, an uncharged tRNA (purple) binds to the A-site of the ribosome in the absence of EF-Tu, leading to stalling. This stalled state is recognized by RelA (red). (C) Diagram representing the domain organization of the relA gene. The two constructs (NT-454-RelA and full length) used for this work are represented. (D) 4–12% SDS–PAGE loaded with the pull-downs of the full-length RelA (left) or with the truncated NT-454-RelA construct (right) with different programmed states of the 70 S. mRNA, messenger RNA; tRNA, transfer RNAs.