title: Continually emerging mechanistic complexity of the multi-enzyme cellulosome complex.
abstract: The robust plant cell wall polysaccharide-degrading properties of anaerobic bacteria are harnessed within elegant, marcomolecular assemblages called cellulosomes, in which proteins of complementary activities amass on scaffold protein networks. Research efforts have focused and continue to focus on providing detailed mechanistic insights into cellulosomal complex assembly, topology, and function. The accumulated information is expanding our fundamental understanding of the lignocellulosic biomass decomposition process and enhancing the potential of engineered cellulosomal systems for biotechnological purposes. Ongoing biochemical studies continue to reveal unexpected functional diversity within traditional cellulase families. Genomic, proteomic, and functional analyses have uncovered unanticipated cellulosomal proteins that augment the function of the native and designer cellulosomes. In addition, complementary structural and computational methods are continuing to provide much needed insights on the influence of cellulosomal interdomain linker regions on cellulosomal assembly and activity.
authors.affiliation: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
authors.forename: Steven P
authors.initials: SP
authors.lastname: Smith
authors.affiliation: Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: ed.bayer@weizmann.ac.il.
authors.forename: Edward A
authors.initials: EA
authors.lastname: Bayer
authors.affiliation: Sorbonne Universités, UPMC, Université Paris 06, France; Centre National de la Recherche Scientifique, UMR 8227, Integrative Biology of Marine Models, Station Biologique Roscoff, CS 90074, F-29688 Roscoff cedex, Bretagne, France. Electronic address: czjzek@sb-roscoff.fr.
authors.forename: Mirjam
authors.initials: M
authors.lastname: Czjzek
mesh_terms: D044603:Cellulosomes / Q000201:enzymology* / Q000378:metabolism; D019295:Computational Biology; D006801:Humans; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D000072417:Protein Domains
chemical_list: D009097:Multienzyme Complexes