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Updated: Jan 28, 2026

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
Published on: October 19, 2012
Anaerobic Fungal Carbohydrate-Binding Modules Exhibit Preference for Fusion to Hemicellulases and Enhance Their
Qicheng Shi1, Dongyang Wang1, Chen Duan1
1Laboratory of Gastrointestinal Microbiology, National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China.
Abstract:
As auxiliary components of the carbohydrate active enzymes (CAZymes), carbohydrate-binding modules (CBMs) influence the enzymatic hydrolysis of substrates. To investigate the role of anaerobic fungal CBMs in lignocellulose degradation, an architectural analysis of bacterial and fungal CBM-containing protein sequences was completed. Results indicated that 67.9% of the fungal CBMs were incorporated into the plant-biomass-degrading enzymes and 51.1% of the anaerobic fungal CBMs were biased to be fused with the hemicellulose-degrading enzymes. Based on the transcriptomic data of anaerobic fungus Pecoramyces ruminantium F1, three upregulated CBM-fused hemicellulose-degrading enzyme gene clusters were identified. Results suggested that the fused CBMs retained the enzymatic function of the associated CAZymes. Importantly, the CBM1 domains of acetyl xylan esterase (AxeA16138) and α-L-arabinofuranosidase (AraA02173) possessed a crucial role to promote the xylanase-mediated hydrolysis of hemicellulose. These results demonstrated that anaerobic fungal CBMs harbor substantial potential to enhance hemicellulose degradation.
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