Structural analysis and engineering of aldo-keto reductase from glyphosate-resistant Echinochloa colona

Li, Hao; Yang, Yu; Hu, Yumei; Chen, Chun‐Chi; Huang, Jian‐Wen; Min, Jian; Dai, Longhai; Guo, Rey‐Ting

doi:10.1016/j.jhazmat.2022.129191

Cited by 5 publications

(15 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As LrAKR4C10 shares 73% identity with the known glyphosate‐metabolizing EcAKR4C16/17, it is expected that LrAKR4C10 follows similar structural mechanisms to bind and detoxify glyphosate. Indeed, recently resolved EcAKR4C17 crystal structure revealed some important catalytic residues and glyphosate binding sites 24 . Sequence alignment between LrAKR4C10 and EcAKR4C16/17 showed identical catalytic tetrad residues (D44, Y49, K78, and H111) (Fig.…”

Section: Discussionmentioning

confidence: 88%

“…Amino acid sequence alignment of EcAKR4C16/17 and LrAKR4C10. Glyphosate binding and catalytic residues according to Li et al 24 . are in boxes.…”

Section: Discussionmentioning

confidence: 99%

“…7). As replacement of W111 by other residues reduces AKR activity, 24 the variation in this residue may account for the difference in glyphosate resistance observed at the whole transgenic rice seedling level for LrAKR4C10 versus EcAKRC16.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, we established that plant AKRs (EcAKR4‐1 and EcAKR4‐2, later designated as AKR4C16 and AKR4C17 in AKR superfamily website) can endow glyphosate resistance in Echinochloa colona by metabolizing glyphosate to a less phytotoxic compound AMPA 23 . More recently, the three‐dimensional structure of the EcAKR4‐1 in complex with cofactors has been resolved by performing X‐ray crystallography and the glyphosate binding‐mode elucidated 24 …”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Aldo‐keto reductase may contribute to glyphosate resistance in Lolium rigidum

Zhou

Han

et al. 2022

Pest Management Science

View full text Add to dashboard Cite

Background We have previously demonstrated that an aldo‐keto reductase (AKR) from Echinochloa colona (EcAKR4‐1) can metabolize glyphosate and confers glyphosate resistance. This study aims to investigate if the EcAKR4‐1 orthologs from Lolium rigidum also play a role in glyphosate resistance in non‐target‐site based, glyphosate‐resistant (R) L. rigidum populations from Western Australia. Results The full‐length L. rigidum AKR gene (LrAKR4C10) orthologous to EcAKR4‐1, together with a distinct LrAKR1, were cloned from plants of a glyphosate‐susceptible (S) (VLR1) and three glyphosate R L. rigidum populations (WALR50, WALR60 and WALR70). Reverse transcription quantitative polymerase chain reaction (RT‐qPCR) results showed that basal expression levels of the two LrAKR genes did not differ between the R and S populations, but their expression was significantly induced by glyphosate (up to 4.3‐fold) or 2,4‐D treatment (up to 3.4‐fold) in R populations. Escherichia coli cells transformed respectively with LrAKR4C10 and LrAKR1 were more tolerant to glyphosate. Rice (Oryza sativa) seedlings overexpressing each of the two LrAKR gene survived glyphosate rates that were lethal to the green fluorescence protein (GFP) control plants. Structural modeling predicts a similar way of glyphosate binding and detoxification by LrAKR4C10 and EcAKR4‐1, but an alternative way of glyphosate binding by LrAKR1. Relatively lower capacity of the two LrAKRs in conferring glyphosate resistance than the known EcAKR4‐1 was discussed in relation to structural interaction. Conclusion Glyphosate‐induced higher expression of the two LrAKR genes in L. rigidum populations contributes to a moderate level of glyphosate resistance likely through enhanced glyphosate metabolism. The herbicide 2,4‐D can also induce the LrAKR expression, indicating the potential antagonistic effect of 2,4‐D to glyphosate. © 2022 The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

show abstract

Section: Discussionmentioning

confidence: 88%

“…Amino acid sequence alignment of EcAKR4C16/17 and LrAKR4C10. Glyphosate binding and catalytic residues according to Li et al 24 . are in boxes.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Aldo‐keto reductase may contribute to glyphosate resistance in Lolium rigidum

Zhou

Han

et al. 2022

Pest Management Science

View full text Add to dashboard Cite

show abstract

“…[ 33 , 34 ]. In addition, the positive roles of PsAKR1, OsAKR4-1 and EcAKR4 in glyphosate degradation have been observed [ 21 , 22 , 35 ]. However, systematic studies in AKRs of plants that are regularly exposed to glyphosate are limited.…”

Section: Introductionmentioning

confidence: 99%

Comparison of Glyphosate-Degradation Ability of Aldo-Keto Reductase (AKR4) Proteins in Maize, Soybean and Rice

Chen

Wang

et al. 2023

IJMS

View full text Add to dashboard Cite

Genes that participate in the degradation or isolation of glyphosate in plants are promising, for they endow crops with herbicide tolerance with a low glyphosate residue. Recently, the aldo-keto reductase (AKR4) gene in Echinochloa colona (EcAKR4) was identified as a naturally evolved glyphosate-metabolism enzyme. Here, we compared the glyphosate-degradation ability of theAKR4 proteins from maize, soybean and rice, which belong to a clade containing EcAKR4 in the phylogenetic tree, by incubation of glyphosate with AKR proteins both in vivo and in vitro. The results indicated that, except for OsALR1, the other proteins were characterized as glyphosate-metabolism enzymes, with ZmAKR4 ranked the highest activity, and OsAKR4-1 and OsAKR4-2 exhibiting the highest activity among the AKR4 family in rice. Moreover, OsAKR4-1 was confirmed to endow glyphosate-tolerance at the plant level. Our study provides information on the mechanism underlying the glyphosate-degradation ability of AKR proteins in crops, which enables the development of glyphosate-resistant crops with a low glyphosate residue, mediated by AKRs.

show abstract

Functional characterization and structural basis of an efficient ochratoxin A-degrading amidohydrolase

Hu,

Dai,

et al. 2024

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Structural analysis and engineering of aldo-keto reductase from glyphosate-resistant Echinochloa colona

Cited by 5 publications

References 42 publications

Aldo‐keto reductase may contribute to glyphosate resistance in Lolium rigidum

Aldo‐keto reductase may contribute to glyphosate resistance in Lolium rigidum

Comparison of Glyphosate-Degradation Ability of Aldo-Keto Reductase (AKR4) Proteins in Maize, Soybean and Rice

Functional characterization and structural basis of an efficient ochratoxin A-degrading amidohydrolase

Contact Info

Product

Resources

About