Journal
ENVIRONMENTAL MICROBIOLOGY
Volume 18, Issue 12, Pages 5112-5122Publisher
WILEY
DOI: 10.1111/1462-2920.13501
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Funding
- United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel
- Israel Science Foundation (ISF) [1349]
- European Union [604530]
- Scottish Government Rural and Environmental Sciences and Analytical Services (SG-RESAS)
- BBSRC [BB/L009951/1]
- BBSRC [BB/L009951/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L009951/1] Funding Source: researchfish
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Ruminococcus champanellensis is a keystone species in the human gut that produces an intricate cellulosome system of various architectures. A variety of cellulosomal enzymes have been identified, which exhibit a range of hydrolytic activities on lignocellulosic substrates. We describe herein a unique R. champanellensis scaffoldin, ScaK, which is expressed during growth on cellobiose and comprises a cohesin module and a family 25 glycoside hydrolase (GH25). The GH25 is non-autolytic and exhibits lysozyme-mediated lytic activity against several bacterial species. Despite the narrow acidic pH curve, the enzyme is active along a temperature range from 2 to 85 degrees C and is stable at very high temperatures for extended incubation periods. The ScaK cohesin was shown to bind selectively to the dockerin of a monovalent scaffoldin (ScaG), thus enabling formation of a cell-free cellulosome, whereby ScaG interacts with a divalent scaffodin (ScaA) that bears the enzymes either directly or through additional monovalent scaffoldins (ScaC and ScaD). The ScaK cohesin also interacts with the dockerin of a protein comprising multiple Fn3 domains that can potentially promote adhesion to carbohydrates and the bacterial cell surface. A cell-free cellulosomal GH25 lysozyme may provide a bacterial strategy to both hydrolyze lignocellulose and repel eventual food competitors and/or cheaters.
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