File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1111/nph.16498
- Scopus: eid_2-s2.0-85082405154
- Find via
Supplementary
-
Citations:
- Scopus: 0
- Appears in Collections:
Article: Convergent recruitment of 5´-hydroxylase activities by CYP75B flavonoid B-ring hydroxylases for tricin biosynthesis in Medicago legumes
Title | Convergent recruitment of 5´-hydroxylase activities by CYP75B flavonoid B-ring hydroxylases for tricin biosynthesis in Medicago legumes |
---|---|
Authors | |
Keywords | Alfalfa (Medicago sativa) dicot legume Medicago truncatula pathway evolution |
Issue Date | 2020 |
Publisher | Wiley-Blackwell Publishing Ltd. The Journal's web site is located at https://nph-onlinelibrary-wiley-com.eproxy.lib.hku.hk/journal/14698137 |
Citation | New Phytologist, 2020, Epub 2020-02-21 How to Cite? |
Abstract | Tricin (3´,5´‐dimethoxylated flavone) is a predominant flavonoid amongst monocots but occurs only in isolated and unrelated dicot lineages. Although tricin biosynthesis has been intensively studied in monocots, it remained largely elusive in tricin‐accumulating dicots.
We investigated a subgroup of cytochrome P450 (CYP) 75B subfamily flavonoid B‐ring hydroxylases (FBHs) from two tricin‐accumulating legumes, Medicago truncatula and alfalfa (M. sativa), by phylogenetic, molecular, biochemical and mutant analyses.
Five Medicago cytochrome P450 CYP75B FBHs are phylogenetically distant from other legume CYP75B members. Among them, MtFBH‐4, MsFBH‐4 and MsFBH‐10 were expressed in tricin‐accumulating vegetative tissues. In vitro and in planta analyses demonstrated that these proteins catalyze 3´‐ and 5´‐hydroxylations critical to tricin biosynthesis. A key amino acid polymorphism, T492G, at their Substrate Recognition Site 6 domain is required for the novel 5´‐hydroxylation activities. M. truncatula mtfbh‐4 mutants were tricin‐deficient, indicating that MtFBH‐4 is indispensable for tricin biosynthesis.
Our results revealed that these Medicago legumes had acquired the tricin pathway through molecular evolution of CYP75B FBHs subsequent to speciation from other non‐tricin‐accumulating legumes. Moreover, their evolution is independent from that of grass‐specific CYP75B apigenin 3´‐hydroxylases/chrysoeriol 5´‐hydroxylases dedicated to tricin production and Asteraceae CYP75B flavonoid 3´,5´‐hydroxylases catalyzing the production of delphinidin‐based pigments. |
Description | Link to Free access |
Persistent Identifier | http://hdl.handle.net/10722/280932 |
ISSN | 2019 Impact Factor: 8.512 2015 SCImago Journal Rankings: 3.603 |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | LUI, ACW | - |
dc.contributor.author | LAM, PY | - |
dc.contributor.author | Chan, KH | - |
dc.contributor.author | WANG, L | - |
dc.contributor.author | Tobimatsu, Y | - |
dc.contributor.author | Lo, C | - |
dc.date.accessioned | 2020-02-25T07:42:55Z | - |
dc.date.available | 2020-02-25T07:42:55Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | New Phytologist, 2020, Epub 2020-02-21 | - |
dc.identifier.issn | 0028-646X | - |
dc.identifier.uri | http://hdl.handle.net/10722/280932 | - |
dc.description | Link to Free access | - |
dc.description.abstract | Tricin (3´,5´‐dimethoxylated flavone) is a predominant flavonoid amongst monocots but occurs only in isolated and unrelated dicot lineages. Although tricin biosynthesis has been intensively studied in monocots, it remained largely elusive in tricin‐accumulating dicots. We investigated a subgroup of cytochrome P450 (CYP) 75B subfamily flavonoid B‐ring hydroxylases (FBHs) from two tricin‐accumulating legumes, Medicago truncatula and alfalfa (M. sativa), by phylogenetic, molecular, biochemical and mutant analyses. Five Medicago cytochrome P450 CYP75B FBHs are phylogenetically distant from other legume CYP75B members. Among them, MtFBH‐4, MsFBH‐4 and MsFBH‐10 were expressed in tricin‐accumulating vegetative tissues. In vitro and in planta analyses demonstrated that these proteins catalyze 3´‐ and 5´‐hydroxylations critical to tricin biosynthesis. A key amino acid polymorphism, T492G, at their Substrate Recognition Site 6 domain is required for the novel 5´‐hydroxylation activities. M. truncatula mtfbh‐4 mutants were tricin‐deficient, indicating that MtFBH‐4 is indispensable for tricin biosynthesis. Our results revealed that these Medicago legumes had acquired the tricin pathway through molecular evolution of CYP75B FBHs subsequent to speciation from other non‐tricin‐accumulating legumes. Moreover, their evolution is independent from that of grass‐specific CYP75B apigenin 3´‐hydroxylases/chrysoeriol 5´‐hydroxylases dedicated to tricin production and Asteraceae CYP75B flavonoid 3´,5´‐hydroxylases catalyzing the production of delphinidin‐based pigments. | - |
dc.language | eng | - |
dc.publisher | Wiley-Blackwell Publishing Ltd. The Journal's web site is located at https://nph-onlinelibrary-wiley-com.eproxy.lib.hku.hk/journal/14698137 | - |
dc.relation.ispartof | New Phytologist | - |
dc.rights | Preprint This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. Postprint This is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. | - |
dc.subject | Alfalfa (Medicago sativa) | - |
dc.subject | dicot legume | - |
dc.subject | Medicago truncatula | - |
dc.subject | pathway evolution | - |
dc.title | Convergent recruitment of 5´-hydroxylase activities by CYP75B flavonoid B-ring hydroxylases for tricin biosynthesis in Medicago legumes | - |
dc.type | Article | - |
dc.identifier.email | Lo, C: clivelo@hku.hk | - |
dc.identifier.authority | Lo, C=rp00751 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1111/nph.16498 | - |
dc.identifier.scopus | eid_2-s2.0-85082405154 | - |
dc.identifier.hkuros | 309223 | - |
dc.identifier.volume | Epub 2020-02-21 | - |
dc.publisher.place | United Kingdom | - |