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Ancestral gene duplication enabled the evolution of multifunctional cellulases in stick insects (Phasmatodea)
Matan Shelomi1, David G Heckel1, Yannick Pauchet1
1Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knöll-Str. 8, 07745 Jena, Germany.
Insect Biochemistry and Molecular Biology
|February 9, 2016
Summary
Stick insects (Phasmatodea) possess multiple glycoside hydrolase family 9 (GH9) genes. These enzymes enable them to digest plant cell walls, likely aiding their specialized folivorous diet.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Phasmatodea (stick insects) exhibit numerous highly expressed glycoside hydrolase family 9 (GH9) genes.
- The evolutionary purpose behind this gene duplication was previously unknown.
Purpose of the Study:
- To investigate the enzymatic activities and substrate specificities of GH9 enzymes from Phasmatodea.
- To understand the evolutionary implications of these genes in the diet and adaptation of stick insects.
Main Methods:
- Cloning and expression of GH9 genes in insect cell lines.
- Enzymatic assays using various plant cell wall polysaccharides (e.g., carboxymethylcellulose, glucomannan, xylan, xyloglucan).
- Analysis of Phasmatodea gut extracts for plant cell wall degradation capabilities.
Main Results:
- Most isolated GH9 enzymes degraded carboxymethylcellulose.
- Many GH9 enzymes also degraded glucomannan, with some showing activity against xylan or xyloglucan.
- Phasmatodea gut extracts demonstrated complete degradation of multiple plant cell wall components into monomers.
Conclusions:
- The evolution of novel GH9 substrate specificities in an early Phasmatodea ancestor likely facilitated specialization as folivores.
- The ability to break down plant cell walls may significantly contribute to the nutritional intake of stick insects.
- Further research is needed to elucidate the structural basis for these unique enzymatic activities.
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