BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis

• DOI: 10.1073/pnas.1314063110
• Publication Date: 2013-10-15T00:21:48Z
• Authors: Okako Omadjela; Adishesh Narahari; Joanna Strumillo; Hugo Mélida; Olga Mazur; Vincent Bulone; Jochen Zimmer
• Keywords: Electrophoresis; 0301 basic medicine; 570; Biopolymer; Blotting, Western; Glycobiology; Rhodobacter sphaeroides; Gas Chromatography-Mass Spectrometry; 03 medical and health sciences; Ingeniería agrícola; Escherichia coli; Cellulose; Membrane transport; Polyacrylamide Gel; Blotting; 2417.19 Fisiología Vegetal; Biological Transport; 540; In vitro reconstitution; Protein Subunits; Glucosyltransferases; Biofilms; Electrophoresis, Polyacrylamide Gel; Western

Significance

Cellulose is the most abundant biopolymer on Earth, primarily formed by vascular plants, but also by some bacteria. Bacterial extracellular polysaccharides, such as cellulose and alginate, are an important component of biofilms, which are multicellular, usually sessile, aggregates of bacteria. Biofilms exhibit a greater resistance to antimicrobial treatments compared with isolated bacteria and thus are a particular concern to human health. Cellulose synthases synthesize cellulose by polymerizing UDP-activated glucose and transport the growing polymer across the cell membrane during its synthesis. Despite numerous attempts, reconstituting cellulose synthesis in vitro from purified components has been unsuccessful. Here we present the complete reconstitution of bacterial cellulose synthesis from components from Rhodobacter sphaeroides, thereby establishing an experimental basis for cellulose and biofilm research.