Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/101033
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dc.contributor.authorDimitroff, G.en
dc.contributor.authorLittle, A.en
dc.contributor.authorLahnstein, J.en
dc.contributor.authorSchwerdt, J.en
dc.contributor.authorSrivastava, V.en
dc.contributor.authorBulone, V.en
dc.contributor.authorBurton, R.en
dc.contributor.authorFincher, G.en
dc.date.issued2016en
dc.identifier.citationBiochemistry, 2016; 55(13):2054-2061en
dc.identifier.issn0006-2960en
dc.identifier.issn1520-4995en
dc.identifier.urihttp://hdl.handle.net/2440/101033-
dc.description.abstractCellulose synthase-like F6 (CslF6) genes encode polysaccharide synthases responsible for (1,3;1,4)-β-glucan biosynthesis in cereal grains. However, it is not clear how both (1,3)- and (1,4)-linkages are incorporated into a single polysaccharide chain and how the frequency and arrangement of the two linkage types that define the fine structure of the polysaccharide are controlled. Through transient expression in Nicotiana benthamiana leaves, two CSLF6 orthologs from different cereal species were shown to mediate the synthesis of (1,3;1,4)-β-glucans with very different fine structures. Chimeric cDNA constructs with interchanged sections of the barley and sorghum CslF6 genes were developed to identify regions of the synthase enzyme responsible for these differences. A single amino acid residue upstream of the TED motif in the catalytic region was shown to dramatically change the fine structure of the polysaccharide produced. The structural basis of this effect can be rationalized by reference to a homology model of the enzyme and appears to be related to the position and flexibility of the TED motif in the active site of the enzyme. The region and amino acid residue identified provide opportunities to manipulate the solubility of (1,3;1,4)-β-glucan in grains and vegetative tissues of the grasses and, in particular, to enhance the solubility of dietary fibers that are beneficial to human health.en
dc.description.statementofresponsibilityGeorge Dimitroff, Alan Little, Jelle Lahnstein, Julian G. Schwerdt, Vaibhav Srivastava, Vincent Bulone, Rachel A. Burton, and Geoffrey B. Fincheren
dc.language.isoenen
dc.publisherAmerican Chemical Societyen
dc.rights© 2016 American Chemical Societyen
dc.subject(1,3;1,4)- β -glucanen
dc.title(1,3;1,4)-β-glucan biosynthesis by the CSLF6 enzyme: position and flexibility of catalytic residues influence product fine structureen
dc.title.alternative(1,3;1,4)-beta-glucan biosynthesis by the CSLF6 enzyme: position and flexibility of catalytic residues influence product fine structureen
dc.typeJournal articleen
dc.identifier.rmid0030045196en
dc.identifier.doi10.1021/acs.biochem.5b01384en
dc.identifier.pubid239484-
pubs.library.collectionAgriculture, Food and Wine publicationsen
pubs.library.teamDS14en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Agriculture, Food and Wine publications

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