Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 26601199.
- Also identified by DOI 10.1126/sciadv.1500069 and PMC identifier 4640613.
- Licence recorded as CC BY-NC.
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Abstract
The cereal cell wall polysaccharide (1-3,1-4)-β-glucan is a linear polymer of glucose containing both β1-3 and β1-4 bonds. The structure of (1-3,1-4)-β-glucan varies between different cereals and during plant growth and development, but little is known about how this is controlled. The cellulose synthase-like CslF6 protein is an integral membrane protein and a major component of the (1-3,1-4)-β-glucan synthase. I show that a single amino acid within the predicted transmembrane pore domain of CslF6 controls (1-3,1-4)-β-glucan structure. A new mechanism for the control of the polysaccharide structure is proposed where membrane pore architecture and the translocation of the growing polysaccharide across the membrane control how the acceptor glucan is coordinated at the active site and thus the proportion of β1-3 and β1-4 bonds within the polysaccharide.