FIGURE 7.

RNase V₁ cleavage of the DsrA–Hfq complex. DsrA in the presence or absence of Hfq was cleaved by RNase V₁. Samples were fractionated on a denaturing polyacrylamide gel. (A) RNase V₁ cleavage of the DsrA–Hfq complex. (Lanes 1,2) Markers: the limited alkaline hydrolysis ladder of DsrA (OH) and 38-nt DsrA_DII (see Materials and Methods). (Lane 3) 5′-end-labeled DsrA (16 nM) that was not treated with RNase V₁. DsrA (16 nM) was treated with RNase V₁ with (+) or without (−) purified Hfq protein (3.1 μM). (B) Structure of DsrA proposed by Lease and Belfort (2000), with upward arrows showing the nucleotides that have increased cleavage in the presence of Hfq. The data shown are representative of several independent experiments.