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https://hdl.handle.net/1822/51384
Título: | Functional characterization of a 28-Kilobase Catabolic Island from Pseudomonas sp. Strain M1 involved in biotransformation of β-Myrcene and related plant-derived volatiles |
Autor(es): | Castro, Pedro Miguel Soares Silva, Pedro Montenegro Heipieper, Hermann J. Santos, Pedro M. |
Palavras-chave: | Biotransformation Computational Biology DNA Mutational Analysis Gene Expression Profiling Gene Order Genotype Metabolic Networks and Pathways Monoterpenes Phytochemicals Pseudomonas Transcription, Genetic Volatile Organic Compounds Genes, Bacterial Genomic Islands genomic island promoter probes beta-myrcene hydroxylase β-myrcene hydroxylase |
Data: | 2017 |
Editora: | American Society for Microbiology |
Revista: | Applied and Environmental Microbiology |
Citação: | Soares-Castro, P., Montenegro-Silva, P., Heipieper, H. J., & Santos, P. M. (2017, May). Functional Characterization of a 28-Kilobase Catabolic Island from Pseudomonas sp. Strain M1 Involved in Biotransformation of β-Myrcene and Related Plant-Derived Volatiles. (M. Kivisaar, Ed.), Applied and Environmental Microbiology. American Society for Microbiology. http://doi.org/10.1128/aem.03112-16 |
Resumo(s): | Pseudomonas sp. strain M1 is able to mineralize highly hydrophobic and recalcitrant compounds, such as benzene, phenol, and their methylated/halogenated derivatives, as well as the backbone of several monoterpenes. The ability to use such a spectrum of compounds as the sole carbon source is, most probably, associated with a genetic background evolved under different environmental constraints. The outstanding performance of strain M1 regarding β-myrcene catabolism was elucidated in this work, with a focus on the biocatalytical potential of the β-myrcene-associated core code, comprised in a 28-kb genomic island (GI), predicted to be organized in 8 transcriptional units. Functional characterization of this locus with promoter probes and analytical approaches validated the genetic organization predictedin silicoand associated the β-myrcene-induced promoter activity to the production of β-myrcene derivatives. Notably, by using a whole-genome mutagenesis strategy, different genotypes of the 28-kb GI were generated, resulting in the identification of a novel putative β-myrcene hydroxylase, responsible for the initial oxidation of β-myrcene into myrcen-8-ol, and a sensor-like regulatory protein, whose inactivation abolished themyr + trait of M1 cells. Moreover, it was demonstrated that the range of monoterpene substrates of the M1 enzymatic repertoire, besides β-myrcene, also includes other acyclic (e.g., β-linalool) and cyclic [e.g.,R-(+)-limonene and (-)-β-pinene] molecules. Our findings are the cornerstone for following metabolic engineering approaches and hint at a major role of the 28-kb GI in the biotransformation of a broad monoterpene backbone spectrum for its future biotechnological applications.IMPORTANCEInformation regarding microbial systems able to biotransform monoterpenes, especially β-myrcene, is limited and focused mainly on nonsystematic metabolite identification. Complete and detailed knowledge at the genetic, protein, metabolite, and regulatory levels is essential in order to set a model organism or a catabolic system as a biotechnology tool. Moreover, molecular characterization of reported systems is scarce, almost nonexistent, limiting advances in the development of optimized cell factories with strategies based on the new generation of metabolic engineering platforms. This study provides new insights into the intricate molecular functionalities associated with β-myrcene catabolism inPseudomonas, envisaging the production of a molecular knowledge base about the underlying catalytic and regulatory mechanisms of plant-derived volatile catabolic pathways. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/51384 |
DOI: | 10.1128/AEM.03112-16 |
ISSN: | 0099-2240 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | DBio - Artigos/Papers |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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e03112-16.pdf | 2,58 MB | Adobe PDF | Ver/Abrir |
Este trabalho está licenciado sob uma Licença Creative Commons