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Content archived on 2024-05-07

Properties of the s-layer-like domains present in cell surface proteins of clostridium thermocellum


Research objectives and content
Several exocellular proteins of Clostridium thermocellum, a thermophilic Gram-positive cellulolytic bacterium possess a carboxy-terminal triplicated sequence which shows similarity to bacterial surface layer proteins. This sequence was named SLH domain (for S-layer homology) and is involved in the attachment of proteins to the cell surface. An objective of this project is to identify the sites of interaction between SLH domains and the cell envelope. Therefore, comparitive in vitro binding studies of SLH domains with purified and biochemically characterized compartments of the cell envelope of Clostridium thermocellum will be undertaken. Proteins interacting with SLH domains will be purified and characterized. To study the binding specificity of SLH domains in vivo, fusion proteins of SLH domains with a reporter protein will be produced and localized in an appropriate Bacillus strain.
Training content (objective, benefit and expected impact)
The objective is to learn new techniques in protein chemistry, e.g. analysis of protein-protein interactions, in addition to some special techniques in molecular biology. Those methods are very important for my future work in research and education in France or Germany. Links with industry / industrial relevance (22)
The commercialization of the results of this project, e.g. new techniques for immobilization of proteins will be consulted with WISSTRANS GmbH, Goettingen in collaboration with Prof. Dr. Gerhard Gottschalk.

Call for proposal

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Centre National de la Recherche Scientifique
EU contribution
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25,Rue du Docteur Roux
75724 Paris

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Participants (1)