Email updates

Keep up to date with the latest news and content from BMC Evolutionary Biology and BioMed Central.

Open Access Correction

Correction: Early evolution of the biotin-dependent carboxylase family

Jonathan Lombard and David Moreira*

Author Affiliations

Unité d’Ecologie, Systématique et Evolution, UMR CNRS 8079, Univ. Paris-Sud, Paris-Sud, Orsay Cedex 91405, France

For all author emails, please log on.

BMC Evolutionary Biology 2012, 12:117  doi:10.1186/1471-2148-12-117


The electronic version of this article is the complete one and can be found online at: http://www.biomedcentral.com/1471-2148/12/117


Received:2 May 2012
Accepted:11 May 2012
Published:20 July 2012

© 2012 Lombard and Moreira; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Correction

After publication of our work [1], we noticed several major mistakes in the figure images provided for final publication: although the main text and the legends are correct, Figure three (Figure 1) has been replaced by an image present in the Addition file 1 and Figure four (Figure 2), Figure five (Figure 3) and Figure six (Figure 4) are displaced with regard to their correct numbers and legends. Please, accept our apologies and refer to the correct corresponding Figure three (Figure 1), Figure four (Figure 2), Figure five (Figure 3) and Figure six (Figure 4) that we provide in this erratum. Legends are the same as in the original article.

thumbnailFigure 1. Maximum likelihood tree of the biotin carboxylase (BC) domain. This tree is based on 284 representative sequences and 384 conserved sites and was arbitrarily roosted on the bacterial ACC-related sequences. Numbers at nodes indicate bootstrap values higher than 50. Triangles correspond to collapsed groups of eukaryotes and Proteobacteria. Colors on leaves represent the affiliation of the sequences to their respective domain of life: archaea (red), bacteria (blue) and eukaryotes (green). Bars on the right report the functional assignment of the sequences; sequences that are not in front of any bar are assumed to bear an acyl-CoA carboxylase activity.

thumbnailFigure 2. Maximum likelihood tree of archaeal and bacterial biotin carboxylase (BC) domain sequences. This tree is based on 196 representative sequences and 322 conserved sites and was arbitrarily rooted on the PYC-related sequences. Numbers at nodes indicate bootstrap robustness values higher than 50. Colors on leaves represent the affiliation of the sequences to their respective domain of life: archaea (red), bacteria (blue) and eukaryotes (green). Bars on the right report the functional assignment of the sequences; sequences that are not in front of any bar are assumed to bear an acyl-CoA carboxylase activity.

thumbnailFigure 3. Maximum likelihood tree of CoA-substrate related carboxyl tranferase (CCT) domain sequences. This tree is based on 179 representative sequences and 438 conserved sites and was midpoint rooted. Numbers at nodes indicate bootstrap robustness values higher than 50. Triangles correspond to collapsed groups of eukaryotes. Colors on leaves represent the affiliation of the sequences to their respective domain of life: archaea (red), bacteria (blue) and eukaryotes (green). Bars on the right report the functional assignment of the sequences; sequences that are not in front of any bar are assumed to bear an acyl-CoA carboxylase activity.

thumbnailFigure 4. Maximum likelihood tree of pyruvate carboxylase carboxyl tranferase (PCT) domain sequences. This tree is based on 126 representative sequences and 432 conserved sites and was midpoint rooted. Numbers at nodes indicate bootstrap robustness values higher than 50. Colors on leaves represent the affiliation of the sequences to their respective domain of life: archaea (red), bacteria (blue) and eukaryotes (green). Bars on the right report the functional assignment of the sequences; sequences that are not in front of any bar have unknown function.

Competing interests

The authors declare no competing interests.

Authors' contributions

JL and DM designed research; JL carried out phylogenetic analyses, and JL and DM wrote the manuscript. Both authors read and approved the final version.

References

  1. Lombard J, Moreira D: Early evolution of the biotin-dependent carboxylase family.

    BMC Evol Biol 2011, 11:232. PubMed Abstract | BioMed Central Full Text | PubMed Central Full Text OpenURL