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In silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4T

2022-09-15Journal article Open access
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dc.contributor.authorLopes, A. R.
dc.contributor.authorBunin, E.
dc.contributor.authorViana, A. T.
dc.contributor.authorFroufe, H.
dc.contributor.authorMuñoz-Merida, A.
dc.contributor.authorPinho, D.
dc.contributor.authorFigueiredo, J
dc.contributor.authorBarroso, C.
dc.contributor.authorVaz-Moreira, I.
dc.contributor.authorBellanger, X.
dc.contributor.authorEgas, C.
dc.contributor.authorNunes, O. C.
dc.date.accessioned2022-09-21T17:04:17Z
dc.date.available2022-09-21T17:04:17Z
dc.date.issued2022-09-15
dc.description.abstractGulosibacter molinativorax ON4 T is the only known organism to produce molinate hydrolase (MolA), which catalyses the breakdown of the thiocarbamate herbicide into azepane-1-carboxylic acid (ACA) and ethanethiol. A combined genomic and transcriptomic strategy was used to fully characterize the strain ON4 T genome, particularly the molA genetic environment, to identify the potential genes encoding ACA degradation enzymes. Genomic data revealed that molA is the only catabolic gene of a novel composite transposon (Tn6311), located in a novel low copy number plasmid (pARLON1) harbouring a putative T4SS of the class FATA. pARLON1 had an ANI value of 88.2% with contig 18 from Agrococcus casei LMG 22410 T draft genome. Such results suggest that pARLON1 is related to genomic elements of other Actinobacteria, although Tn6311 was observed only in strain ON4 T. Furthermore, genomic and transcriptomic data demonstrated that the genes involved in ACA degradation are chromosomal. Based on their overexpression when growing in the presence of molinate, the enzymes potentially involved in the heterocyclic ring breakdown were predicted. Among these, the activity of a protein related to caprolactone hydrolase was demonstrated using heterologous expression. However, further studies are needed to confirm the role of the other putative enzymes.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1038/s41598-022-18732-5pt_PT
dc.identifier.eid85137886980
dc.identifier.issn2045-2322
dc.identifier.pmcPMC9477822
dc.identifier.pmid36109598
dc.identifier.urihttp://hdl.handle.net/10400.14/38967
dc.identifier.wos000854795200063
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleIn silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4Tpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue1pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume12pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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