Corrigendum

Errata

This article corrects:

  1. Consortia modulation of the stress response: proteomic analysis of single strain versus mixed culture Volume 12, Issue 9, 2436–2449, Article first published online: 19 April 2010

E-mail rbobadi@utem.cl; Tel. (+56) 2787 7300; Fax (+56) 2787 7321; **E-mail vitor.mds@wur.nl; Tel. (+31) 317 482865; Fax (+31) 317 483829.

In the article ‘Consortia modulation of the stress response: proteomic analysis of single strain versus mixed culture’ (Bobadilla Fazzini et al., 2010), the following errors were published:

The list of authors and affiliations were:

Roberto A. Bobadilla Fazzini,1,2* Maria J. Preto,1 Ana C. Poucas Quintas,1 Agata Bielecka,1 Kenneth N. Timmis1 and Vitor A. P. Martins dos Santos1

1Division of Microbiology, HZI-Helmholtz-Zentrum für Infektionsforschung, Braunschweig, Germany.

2Departamento de Prevencion de Riesgos y Medio Ambiente, Facultad de Ciencias de la Construccion y Ordenamiento Territorial, Universidad Tecnologica Metropolitana, Santiago de Chile, Chile.

The correct list of authors and respective affiliations are:

Roberto A. Bobadilla Fazzini,1,2* Maria J. Preto,1 Ana C. Poucas Quintas,1 Agata Bielecka1 and Vitor A. P. Martins dos Santos1,3**

1Division of Microbiology, HZI-Helmholtz-Zentrum für Infektionsforschung, Braunschweig, Germany.

2Departamento de Prevencion de Riesgos y Medio Ambiente, Facultad de Ciencias de la Construccion y Ordenamiento Territorial, Universidad Tecnologica Metropolitana, Santiago de Chile, Chile.

3Laboratory of Systems and Synthetic Biology, Wageningen University, Dreijenplein 10, 6703 HB Wageningen, The Netherlands.

Figures 3 and 5 were:

  • image(3)

[ 4-chlorosalicylate load and oxidative stress response scheme including degradation, transport and proposed detoxification pathways (OprF, outer membrane porin F; AhpC, Alkyl hydroperoxide reductase, C subunit) in Pseudomonas reinekei MT1. Main induced pathway highlighted (SalA, salicylate 1-hydroxylase; CatA, catechol 1,2-dioxygenase; SalC, muconate cycloisomerase; trans-DLH, trans-dienelactone hydrolase; MAR, maleylacetate reductase; CatJ, 3-oxoadipate : succinyl-CoA transferase) and parallel pathways via protocatechuate (3,4-PCD, protocatechuate 3,4-dioxygenase) and via gentisate (Sal5, salicylate 5-hydroxylase). ]

  • image(5)

[ 4-chlorosalicylate metabolic response scheme including degradation and proposed transport (porin D) in the consortia (P. reinekei MT1: A. xylosoxidans MT3). The main induced pathway in strain MT1 is highlighted (SalA, salicylate 1-hydroxylase; CatA, catechol 1,2-dioxygenase; SalC, muconate cycloisomerase; trans-DLH, trans-dienelactone hydrolase; MAR, maleylacetate reductase; CatJ, 3-oxoadipate : succinyl-CoA transferase) and parallel pathways via protocatechuate (3,4-PCD, protocatechuate 3,4-dioxygenase; CatD, 3-oxoadipate enol-lactonase) and via gentisate (Sal5, salicylate 5-hydroxylase). ]

They should be:

  • image(3)

[ 4-chlorosalicylate load and oxidative stress response scheme including degradation, transport and proposed detoxification pathways (OprF: Outer membrane porin F; AhpC: Alkyl hydroperoxide reductase, C subunit) in Pseudomonas reinekei MT1. Main induced pathway highlighted (SalA: salicylate 1-hydroxylase; CatA, SalD, CcaA: catechol 1,2-dioxygenases; CatB, SalC, CcaB: muconate cycloisomerases; CcaC: trans-dienelactone hydrolase; CcaD: maleylacetate reductase; CatJ: 3-oxoadipate:succinyl-CoA transferase) and parallel pathway via 4-chlorogentisate (Sal5: salicylate 5-hydroxylase). ]

  • image(5)

[ 4-chlorosalicylate metabolic response scheme including degradation and proposed transport (porin D) in the consortia (P. reinekei MT1: A. xylosoxidans MT3). The main induced pathway in strain MT1 is highlighted (SalA: salicylate 1-hydroxylase; CatA, SalD, CcaA: catechol 1,2-dioxygenases; CatB, SalC, CcaB: muconate cycloisomerases; CcaC: trans-dienelactone hydrolase; CcaD: maleylacetate reductase; CatJ: 3-oxoadipate:succinyl-CoA transferase) and parallel pathway via 4-chlorogentisate (Sal5: salicylate 5-hydroxylase). ]

Additionally, the authors would like to include the following acknowledgements:

We gratefully acknowledge the financial support by the Deutsche Forschungsgemeinschaft (DFG, Project No. 444CHL-113/24/0-1) and the Bundesministerium für Bildung und Forschung (BMBF, Project No. 0313980A). We thank Dr Dietmar Pieper at the HZI for valuable comments and discussions.

We apologise for these errors.

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