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.
(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.
(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.
Footnotes
- Copyright © 2006, Cold Spring Harbor Laboratory Press


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