Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability

Author:

Tomazini Atilio1,Lal Sadhana2,Munir Riffat2,Stott Matthew3,Henrissat Bernard4,Polikarpov Igor1,Sparling Richard5,Levin David B.2

Affiliation:

1. São Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590, São Paulo, Brazil.

2. Department of Biosystems Engineering, University of Manitoba, Winnipeg, MB R3T 5V6, Canada.

3. School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.

4. Architecture et fonction des macromolécules biologiques (AFMB), CNRS–INRA, Aix-Marseille Université, Marseille, France USC1408.

5. Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada.

Abstract

The phylum Chloroflexi is phylogenetically diverse and is a deeply branching lineage of bacteria that express a broad spectrum of physiological and metabolic capabilities. Members of the order Ktedonobacteriales, including the families Ktedonobacteriaceae, Thermosporotrichaceae, and Thermogemmatisporaceae, all have flexible aerobic metabolisms capable of utilizing a wide range of carbohydrates. A number of species within these families are considered cellulolytic and are capable of using cellulose as a sole carbon and energy source. In contrast, Ktedonobacter racemifer, the type strain of the order, does not appear to possess this cellulolytic phenotype. In this study, we confirmed the ability of Thermogemmatispora sp. strain T81 to hydrolyze cellulose, determined the whole-genome sequence of Thermogemmatispora sp. T81, and using comparative bioinformatics analyses, identified genes encoding putative carbohydrate-active enzymes (CAZymes) in the Thermogemmatispora sp. T81, Thermogemmatispora onikobensis, and Ktedonobacter racemifer genomes. Analyses of the Thermogemmatispora sp. T81 genome identified 64 CAZyme gene sequences belonging to 57 glycoside hydrolase families. The genome of Thermogemmatispora sp. T81 encodes 19 genes for putative extracellular CAZymes, similar to the number of putative extracellular CAZymes identified in T. onikobensis (17) and K. racemifer (17), despite K. racemifer not possessing a cellulolytic phenotype. These results suggest that these members of the order Ktedonobacteriales may use a broader range of carbohydrate polymers than currently described.

Publisher

Canadian Science Publishing

Subject

Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology

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