Erratum

Genes & Development 19: 2176–2186 (2005)

RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs

Teppei Morita, Kimika Maki, and Hiroji Aiba

In the above-mentioned paper, there were two errors in the reproduction of Figures 1B and 3B, in which the Enolase and RNase E-Flag panels were mistakenly used, respectively. The correct figures appear below, with their legends.

Figure 1.

(B) Effect of enolase depletion on the expression of SgrS RNA and ptsG mRNA. TM461(Δpgi Pbla-ptsG) and TM509 (Δpgi Pbla-ptsG PBAD-eno) cells were grown in M9 medium containing 0.2% succinate and 0.02% glycerol. At A600 = 0.6, crude extracts and total RNAs were prepared. The crude extracts corresponding to 0.01 A600 unit were subjected to Western blot analysis using anti-enolase antibody. Each RNA sample (15 or 5 μg) was subjected to Northern blot analysis using ptsG or sgrS probe, respectively.


Figure 3.

(B) Effect of nuclease treatment on the Hfq–RNase E interaction. TM338 (rne-Flag-cat) cells were grown in LB medium. At A600 = 0.6, 1% αMG was added to each culture and incubation was continued for 20 min. (Lanes 4–6) A crude extract was prepared and treated with micrococcal nuclease and subjected to the pull-down assay using anti-Flag agarose. (Lanes 1–3) As a control, the extract without micrococcal nuclease was also subjected to the pull-down assay. The crude extracts, unbound fractions, and bound fractions were analyzed by Western blotting using anti-Flag, anti-enolase, and anti-Hfq antibodies. For analysis of RNAs associated with RNase E analysis, 5 μL of deprotenized crude extracts, unbound fractions, and bound fractions were subjected to Northern blotting using the sgrS probe.


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