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A C4-cytidine riboswitch confers mRNA-level expression of genes that catalyze the biosynthesis of cytidine, which is a major component of RNA. This riboswitch consists of an aptamer that binds C4-cytidine and an antiterminator that attenuates termination during translation. It has been found that the C4-cytidine riboswitch forms a translational ribosome-separating complex (TRSC) that separates ribosomes at the C-terminus of the 16S rRNA using an ATP-dependent channel-forming function of the ribosome. Here, we show that in this ribosome-separating event, the ribosome-binding protein S1C, which is an integral component of the TRSC, moves to a position near the C4-cytidine riboswitch by virtue of the ribosome chaperone Hfq and a suppressor protein S1T. Despite the AT-rich sequence of the ribosome-separating channel, the ribosome-segregating activity of S1C depends on the cognate mRNA, not on the aptamer sequence of the riboswitch. Our findings provide new insights into the mechanism of

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