ArticleApplied and environmental microbiology2001
EndB, a multidomain family 44 cellulase from Ruminococcus flavefaciens 17, binds to cellulose via a novel cellulose-binding module and to another R. flavefaciens protein via a dockerin domain.
Article in Applied and environmental microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 48 citations in OpenAlex.
- Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024Article
- Change of Endoglucanase Activity and Rumen Microbial Community During Biodegradation of Cellulose Using Rumen Microbiota.Frontiers in microbiology · 2020Article
- Functional diversification of horizontally acquired glycoside hydrolase family 45 (GH45) proteins in Phytophaga beetles.BMC evolutionary biology · 2019Article
- A Comparative Study on the Faecal Bacterial Community and Potential Zoonotic Bacteria of Muskoxen (Microorganisms · 2018Article
- Article
- First insight into the faecal microbiota of the high Arctic muskoxen (Microbial genomics · 2016Article
- Expression of cellulosome components and type IV pili within the extracellular proteome of Ruminococcus flavefaciens 007.PloS one · 2013Article
- Cellulases: ambiguous nonhomologous enzymes in a genomic perspective.Trends in biotechnology · 2011Article
- High-yield and phylogenetically robust methods of DNA recovery for analysis of microbial biofilms adherent to plant biomass in the herbivore gut.Microbial ecology · 2011Article
- Abundance and diversity of dockerin-containing proteins in the fiber-degrading rumen bacterium, Ruminococcus flavefaciens FD-1.PloS one · 2010Article
- Diversity and strain specificity of plant cell wall degrading enzymes revealed by the draft genome of Ruminococcus flavefaciens FD-1.PloS one · 2009Article
- A novel cell surface-anchored cellulose-binding protein encoded by the sca gene cluster of Ruminococcus flavefaciens.Journal of bacteriology · 2007Article
- Conservation and divergence in cellulosome architecture between two strains of Ruminococcus flavefaciens.Journal of bacteriology · 2006Article
- Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface.Journal of bacteriology · 2005Article
- ScaC, an adaptor protein carrying a novel cohesin that expands the dockerin-binding repertoire of the Ruminococcus flavefaciens 17 cellulosome.Journal of bacteriology · 2004Article
- Ruminococcus albus 8 mutants defective in cellulose degradation are deficient in two processive endocellulases, Cel48A and Cel9B, both of which possess a novel modular architecture.Journal of bacteriology · 2004Article
- Novel organization and divergent dockerin specificities in the cellulosome system of Ruminococcus flavefaciens.Journal of bacteriology · 2003Article
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5 authors.
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Abstract
The mechanisms by which cellulolytic enzymes and enzyme complexes in Ruminococcus spp. bind to cellulose are not fully understood. The product of the newly isolated cellulase gene endB from Ruminococcus flavefaciens 17 was purified as a His-tagged product after expression in Escherichia coli and found to be able to bind directly to crystalline cellulose. The ability to bind cellulose is shown to be associated with a novel cellulose-binding module (CBM) located within a region of 200 amino acids that is unrelated to known protein sequences. EndB (808 amino acids) also contains a catalytic domain belonging to glycoside hydrolase family 44 and a C-terminal dockerin-like domain. Purified EndB is also shown to bind specifically via its dockerin domain to a polypeptide of ca. 130 kDa present among supernatant proteins from Avicel-grown R. flavefaciens that attach to cellulose. The protein to which EndB attaches is a strong candidate for the scaffolding component of a cellulosome-like multienzyme complex recently identified in this species (S.-Y. Ding et al., J. Bacteriol. 183:1945-1953, 2001). It is concluded that binding of EndB to cellulose may occur both through its own CBM and potentially also through its involvement in a cellulosome complex.
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