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Disruption of Brachypodium lichenase alters metabolism of mixed‐linkage glucan and starch
SUMMARY Mixed‐linkage glucan, which is widely distributed in grasses, is a polysaccharide highly abundant in cell walls of grass endosperm and young vegetative tissues. Lichenases are enzymes that hydrolyze mixed‐linkage glucan first identified in mixed‐linkage glucan‐rich lichens. In this study, we...
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Published in: | The Plant journal : for cell and molecular biology 2021-11, Vol.109 (4) |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | SUMMARY
Mixed‐linkage glucan, which is widely distributed in grasses, is a polysaccharide highly abundant in cell walls of grass endosperm and young vegetative tissues. Lichenases are enzymes that hydrolyze mixed‐linkage glucan first identified in mixed‐linkage glucan‐rich lichens. In this study, we identify a gene encoding a lichenase we name
Brachypodium distachyon LICHENASE 1
(
BdLCH1
), which is highly expressed in the endosperm of germinating seeds and coleoptiles and at lower amounts in mature shoots. RNA
in situ
hybridization showed that
BdLCH1
is primarily expressed in chlorenchyma cells of mature leaves and internodes. Disruption of BdLCH1 resulted in an eight‐fold increase in mixed‐linkage glucan content in senesced leaves. Consistent with the
in situ
hybridization data, immunolocalization results showed that mixed‐linkage glucan was not removed in chlorenchyma cells of
lch1
mutants as it was in wild type and implicate the BdLCH1 enzyme in removing mixed‐linkage glucan in chlorenchyma cells in mature vegetative tissues. We also show that mixed‐linkage glucan accumulation in
lch1
mutants was resistant to dark‐induced degradation, and 8‐week‐old
lch1
plants showed a faster rate of starch breakdown than wild type in darkness. Our results suggest a role for BdLCH1 in modifying the cell wall to support highly metabolically active cells. |
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ISSN: | 0960-7412 1365-313X |