Two Chalcone Synthase Isozymes Participate Redundantly in UV-Induced Sakuranetin Synthesis in Rice
Chalcone synthase (CHS) is a key enzyme in the flavonoid pathway, participating in the production of phenolic phytoalexins. The rice genome contains 31 family genes ( s). The molecular characterization of s suggests that and belong in the bona fide CHSs, while the other members are categorized in th...
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Published in | International journal of molecular sciences Vol. 21; no. 11; p. 3777 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
MDPI
27.05.2020
MDPI AG |
Subjects | |
Online Access | Get full text |
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Summary: | Chalcone synthase (CHS) is a key enzyme in the flavonoid pathway, participating in the production of phenolic phytoalexins. The rice genome contains 31
family genes (
s). The molecular characterization of
s suggests that
and
belong in the bona fide CHSs, while the other members are categorized in the non-CHS group of type III polyketide synthases (PKSs). Biochemical analyses of recombinant OsCHSs also showed that OsCHS24 and OsCHS8 catalyze the formation of naringenin chalcone from
-coumaroyl-CoA and malonyl-CoA, while the other OsCHSs had no detectable CHS activity. OsCHS24 is kinetically more efficient than OsCHS8. Of the
s,
also showed the highest expression levels in different tissues and developmental stages, suggesting that it is the major CHS isoform in rice. In
mutant leaves, sakuranetin content decreased to 64.6% and 80.2% of those in wild-type leaves at 2 and 4 days after UV irradiation, respectively, even though
expression was mostly suppressed. Instead, the
expression was markedly increased in the
mutant under UV stress conditions compared to that in the wild-type, which likely supports the UV-induced production of sakuranetin in
. These results suggest that OsCHS24 acts as the main CHS isozyme and OsCHS8 redundantly contributes to the UV-induced production of sakuranetin in rice leaves. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address; Department of Botany and Plant Pathology, and Center for Plant Biology, Purdue University, West Lafayette, IN 47907, USA |
ISSN: | 1422-0067 1661-6596 1422-0067 |
DOI: | 10.3390/ijms21113777 |