Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation
| dc.contributor.author | MartÃnez-Ruiz, Erika Berenice | |
| dc.contributor.author | Cooper, Myriel | |
| dc.contributor.author | Barrero-Canosa, Jimena | |
| dc.contributor.author | Haryono, Mindia A. S. | |
| dc.contributor.author | Bessarab, Irina | |
| dc.contributor.author | Williams, Rohan B. H. | |
| dc.contributor.author | Szewzyk, Ulrich | |
| dc.date.accessioned | 2021-07-06T07:32:51Z | |
| dc.date.available | 2021-07-06T07:32:51Z | |
| dc.date.issued | 2021-06-22 | |
| dc.description.abstract | Background Cylindrospermopsin is a highly persistent cyanobacterial secondary metabolite toxic to humans and other living organisms. Strain OF001 and A210 are manganese-oxidizing bacteria (MOB) able to transform cylindrospermopsin during the oxidation of Mn2+. So far, the enzymes involved in manganese oxidation in strain OF001 and A210 are unknown. Therefore, we analyze the genomes of two cylindrospermopsin-transforming MOB, Pseudomonas sp. OF001 and Rubrivivax sp. A210, to identify enzymes that could catalyze the oxidation of Mn2+. We also investigated specific metabolic features related to pollutant degradation and explored the metabolic potential of these two MOB with respect to the role they may play in biotechnological applications and/or in the environment. Results Strain OF001 encodes two multicopper oxidases and one haem peroxidase potentially involved in Mn2+ oxidation, with a high similarity to manganese-oxidizing enzymes described for Pseudomonas putida GB-1 (80, 83 and 42% respectively). Strain A210 encodes one multicopper oxidase potentially involved in Mn2+ oxidation, with a high similarity (59%) to the manganese-oxidizing multicopper oxidase in Leptothrix discophora SS-1. Strain OF001 and A210 have genes that might confer them the ability to remove aromatic compounds via the catechol meta- and ortho-cleavage pathway, respectively. Based on the genomic content, both strains may grow over a wide range of O2 concentrations, including microaerophilic conditions, fix nitrogen, and reduce nitrate and sulfate in an assimilatory fashion. Moreover, the strain A210 encodes genes which may convey the ability to reduce nitrate in a dissimilatory manner, and fix carbon via the Calvin cycle. Both MOB encode CRISPR-Cas systems, several predicted genomic islands, and phage proteins, which likely contribute to their genome plasticity. Conclusions The genomes of Pseudomonas sp. OF001 and Rubrivivax sp. A210 encode sequences with high similarity to already described MCOs which may catalyze manganese oxidation required for cylindrospermopsin transformation. Furthermore, the analysis of the general metabolism of two MOB strains may contribute to a better understanding of the niches of cylindrospermopsin-removing MOB in natural habitats and their implementation in biotechnological applications to treat water. | en |
| dc.description.sponsorship | TU Berlin, Open-Access-Mittel – 2021 | en |
| dc.identifier.eissn | 1471-2164 | |
| dc.identifier.uri | https://depositonce.tu-berlin.de/handle/11303/13359 | |
| dc.identifier.uri | http://dx.doi.org/10.14279/depositonce-12148 | |
| dc.language.iso | en | en |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en |
| dc.subject.ddc | 570 Biowissenschaften; Biologie | de |
| dc.subject.other | metabolic potential | en |
| dc.subject.other | manganese-oxidizing bacteria | en |
| dc.subject.other | biotransformation | en |
| dc.subject.other | cyanotoxins | en |
| dc.title | Genome analysis of Pseudomonas sp. OF001 and Rubrivivax sp. A210 suggests multicopper oxidases catalyze manganese oxidation required for cylindrospermopsin transformation | en |
| dc.type | Article | en |
| dc.type.version | publishedVersion | en |
| dcterms.bibliographicCitation.articlenumber | 464 | en |
| dcterms.bibliographicCitation.doi | 10.1186/s12864-021-07766-0 | en |
| dcterms.bibliographicCitation.journaltitle | BMC Genomics | en |
| dcterms.bibliographicCitation.originalpublishername | Springer Nature | en |
| dcterms.bibliographicCitation.originalpublisherplace | Heidelberg | en |
| dcterms.bibliographicCitation.volume | 22 | en |
| tub.accessrights.dnb | free | en |
| tub.affiliation | Fak. 3 Prozesswissenschaften::Inst. Technischen Umweltschutz::FG Umweltmikrobiologie | de |
| tub.affiliation.faculty | Fak. 3 Prozesswissenschaften | de |
| tub.affiliation.group | FG Umweltmikrobiologie | de |
| tub.affiliation.institute | Inst. Technischen Umweltschutz | de |
| tub.publisher.universityorinstitution | Technische Universität Berlin | en |