Research article2020Peer reviewedOpen access
The Peptidoglycan Biosynthesis Gene murC in Frankia: Actinorhizal vs. Plant Type
Berckx, Fede; Wibberg, Daniel; Kalinowski, Joern; Pawlowski, Katharina
Abstract
Nitrogen-fixing Actinobacteria of the genus Frankia can be subdivided into four phylogenetically distinct clades; members of clusters one to three engage in nitrogen-fixing root nodule symbioses with actinorhizal plants. Mur enzymes are responsible for the biosynthesis of the peptidoglycan layer of bacteria. The four Mur ligases, MurC, MurD, MurE, and MurF, catalyse the addition of a short polypeptide to UDP-N-acetylmuramic acid. Frankia strains of cluster-2 and cluster-3 contain two copies of murC, while the strains of cluster-1 and cluster-4 contain only one. Phylogenetically, the protein encoded by the murC gene shared only by cluster-2 and cluster-3, termed MurC1, groups with MurC proteins of other Actinobacteria. The protein encoded by the murC gene found in all Frankia strains, MurC2, shows a higher similarity to the MurC proteins of plants than of Actinobacteria. MurC2 could have been either acquired via horizontal gene transfer or via gene duplication and convergent evolution, while murC1 was subsequently lost in the cluster-1 and cluster-4 strains. In the nodules induced by the cluster-2 strains, the expression levels of murC2 were significantly higher than those of murC1. Thus, there is clear sequence divergence between both types of Frankia MurC, and Frankia murC1 is in the process of being replaced by murC2, indicating selection in favour of murC2. Nevertheless, protein modelling showed no major structural differences between the MurCs from any phylogenetic group examined.
Keywords
Peptidoglycan; MurC; Frankia; nitrogen fixation; actinorhizal symbiosis; root nodules
Published in
Genes
2020, Volume: 11, number: 4, article number: 432Publisher: MDPI
UKÄ Subject classification
Genetics
Publication identifier
DOI: https://doi.org/10.3390/genes11040432
Permanent link to this page (URI)
https://res.slu.se/id/publ/127250