Open Access

Erratum to: The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway

BMC MicrobiologyBMC series – open, inclusive and trusted201717:186

https://doi.org/10.1186/s12866-017-1071-x

Published: 23 August 2017

The original article was published in BMC Microbiology 2010 10:281

Erratum

After publication of our article [1] we became aware that two errors had been introduced during the revision process. These errors affect two figures (Fig. 2 and Fig. 4):
  • In Fig. 2B the control panels with the non-transformed cells were wrong.

  • In Fig. 4A the right panel (+CheW) was wrong.

Fig. 2

Chemotaxis of E. coli is inhibited by the expression of Ppr or Pph. a The chemotactic wild type strain E. coli MM500 was transformed with the plasmids pBAD-Ppr (lanes 1 and 2), pBAD-Pph (lanes 3 and 4) and pBAD-Pph H670A (lanes 5 and 6). Cells were grown in TB medium to an OD600 = 0.5, 0.2% fructose (lanes 1, 3 and 5) or 0.2% arabinose (lanes 2, 4 and 6) was added, and growth was continued for 3 h. Protein expression was analyzed by SDS-PAGE and Coomassie blue staining. The positions of molecular weight markers are indicated. b TB swarm agar plates containing either 0.2% arabinose (upper panels) or 0.2% fructose (lower panels) were inoculated with E. coli MM500 cells bearing the plasmids pBAD-Ppr, pBAD-Pph and pBAD-Pph H670A, pBAD (vector without insert) or pBAD-KdpE. To develop chemotactic rings the plates were incubated for 6 h at 37 °C

Fig. 4

Interaction between Pph and the chemotactic protein Rc-CheW. a The binding of the histidine kinase domain Pph and CheW was analyzed in pull-down assays. R. centenaria 6his-Rc-CheW was expressed in E. coli C41 cells and purified. The Pph protein was translated in vitro in the presence of [35S]-methionine (lane 1 and 4). Rc-CheW was added (50 μg) to the reaction and incubated at 37 °C. The sample was applied to a Cu-Sepharose column and after washing the bound complexes were eluted (lanes 3 and 6). The fractions were analysed by phosphorimaging. The in vitro translating protein extracts are shown in lanes 1 and 4, the final wash steps in lanes 2 and 5 and the elution fractions in lanes 3 and 6, respectively. The co-elution rate was calculated and is indicated. The positions of molecular weight markers are indicated. b The binding of the Pph protein and Rc-CheW was analysed in the presence of ATP. The Pph protein was translated and Rc-CheW was added as described in (A). ATP or apyrase was added to each reaction as indicated and the samples were analysed as described in (A). The co-elution rate was calculated and is indicated in % as bound Pph protein

Neither error changes the outcome of the experiments or the conclusions of the article. The corrected figures are shown as follows:

Notes

Declarations

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

Authors’ Affiliations

(1)
Institute of Microbiology and Molecular Biology

Reference

  1. Kreutel S, Kuhn A, Kiefer D. The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway. BMC Microbiol. 2010;10(1):281.Google Scholar

Copyright

© The Author(s). 2017

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