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Title

Promiscuity and extremophily: expanding the pool of substrates available to extremophiles that mineralize aromatic pollutants

AuthorsAlcaide, María ; Tornés, Jesús ; Stogios, Peter J.; Xu, Xiaohui; Gertler, Christoph; Di Leo, Rosa; Bargiela, Rafael ; Lafraya Aguado, Álvaro ; Chernikova, Tatyana; Golyshina, Olga V. ; Nechitaylo, Taras Y.; Plumeier, Iris; Pieper, Dietmar H.; Yakimov, Michail M.; Savchenko, Alexei; Golyshin, Peter N.; Ferrer, Manuel
Issue Date17-Sep-2014
Citation10th International Congress on Extremophiles (2014)
AbstractSeveral microorganisms have the ability to gain energy from hydrophobic organic solvents that are highly toxic for the majority of them. When bacteria are confronted with aromatic compounds, cells face an enticing contradiction. Briefly these chemical species can be mineralized, allowing the microorganism to colonize niches refractory to other microbes for which they are toxic. Therefore, once a site is contaminated, the microbial community greatly changed allowing “extremophiles” to develop. Microbial ability to thrive in polluted sites depends upon adaptation of their enzymatic machinery. To note is that enzymes commonly work in complex environments. External factors (substrate diversity, concentration, presence of ions, temperature, pH, protein-protein interactions, etc.), and protein features themselves (modularity, overall structure and single or multiple mutations), exemplified a complex scenario that may influence activity levels and substrate specificity in a way that cannot be derived from community genome and transcript datasets. Accordingly, this stresses the need for further biochemical and structural studies in order to quantify more accurately enzyme activity characteristics as they may have ecological implications. C-C meta-cleavage product (MCP) hydrolases are key enzymes for the complete mineralization of aromatic pollutants. The catalytic mechanism of MCP hydrolases is well-known; still the mechanisms by which promiscuity can be gained in this protein family, in particular the unusual ability to hydrolyze both esters and MCP, is not clearly understood. Herein, we describe six distinct α/β hydrolases obtained by genomic approaches, four of which have the un-precedent characteristic of activity towards multiple substrates. Using crystallography and site-directed mutagenesis we have identified three residues of the binding site (S32, V130 and W144) of one of these proteins that provides a cogent explanation for the unusual selectivity profile (Alcaide et al., 2013). The data suggest that hydrolases with such broad substrate range may persist in microbial communities to much greater extent than previously anticipated, expanding the pool of substrates available to microorganisms that mineralize organic carbon. Hence this type of enzyme may contribute to the global carbon cycling processes and for channeling complex substrates into the common catabolic pathways, including recalcitrant organic pollutants. The results may open up new research avenues into comparative catalysis models, structural and mechanistic studies, as well as expand the ecological implications and biotechnological applications of MCP hydrolases.
DescriptionTrabajo presentado en el 10th International Congress on Extremophiles, celebrado en San Petesburgo (Rusia) del 07 al 11 de septiembre de 2014.
URIhttp://hdl.handle.net/10261/189130
Appears in Collections:(ICP) Comunicaciones congresos
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