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Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure

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 syn...

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Autor principal: Jobling, Stephen A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4640613/
https://www.ncbi.nlm.nih.gov/pubmed/26601199
http://dx.doi.org/10.1126/sciadv.1500069
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author Jobling, Stephen A.
author_facet Jobling, Stephen A.
author_sort Jobling, Stephen A.
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description 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.
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spelling pubmed-46406132015-11-23 Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure Jobling, Stephen A. Sci Adv Research Articles 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. American Association for the Advancement of Science 2015-06-12 /pmc/articles/PMC4640613/ /pubmed/26601199 http://dx.doi.org/10.1126/sciadv.1500069 Text en Copyright © 2015, The Authors http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Research Articles
Jobling, Stephen A.
Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title_full Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title_fullStr Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title_full_unstemmed Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title_short Membrane pore architecture of the CslF6 protein controls (1-3,1-4)-β-glucan structure
title_sort membrane pore architecture of the cslf6 protein controls (1-3,1-4)-β-glucan structure
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4640613/
https://www.ncbi.nlm.nih.gov/pubmed/26601199
http://dx.doi.org/10.1126/sciadv.1500069
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