Novel α-tubulin mutations conferring resistance to dinitroaniline herbicides in Lolium rigidum

Zhizhan Chu, Jinyi Chen, Alex Nyporko, Heping Han, Qin Yu, Stephen Powles

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The dinitroaniline herbicides (particularly trifluralin) have been globally used in many crops for selective grass weed control. Consequently, trifluralin resistance has been documented in several important crop weed species and has recently reached a level of concern in Australian Lolium rigidum populations. Here, we report novel mutations in the L. rigidum α-tubulin gene which confer resistance to trifluralin and other dinitroaniline herbicides. Nucleotide mutations at the highly conserved codon Arg-243 resulted in amino acid substitutions of Met or Lys. Rice calli transformed with the mutant 243-Met or 243-Lys α-tubulin genes were 4- to 8-fold more resistant to trifluralin and other dinitroaniline herbicides (e.g., ethalfluralin and pendimethalin) compared to calli transformed with the wild type α-tubulin gene from L. rigidum. Comprehensive modeling of molecular docking predicts that Arg-243 is close to the trifluralin binding site on the α-tubulin surface and that replacement of Arg-243 by Met/Lys-243 results in a spatial shift of the trifluralin binding domain, reduction of trifluralin-tubulin contacts, and unfavorable interactions. The major effect of these substitutions is a significant rise of free interaction energy between α-tubulin and trifluralin, as well as between trifluralin and its whole molecular environment. These results demonstrate that the Arg-243 residue in α-tubulin is a determinant for trifluralin sensitivity, and the novel Arg-243-Met/Lys mutations may confer trifluralin resistance in L. rigidum.

Original languageEnglish
Article number97
JournalFrontiers in Plant Science
Volume9
DOIs
Publication statusPublished - 6 Feb 2018

Fingerprint

dinitroaniline herbicides
Lolium rigidum
trifluralin
tubulin
mutation
callus
ethalfluralin
pendimethalin
grass weeds
genes
amino acid substitution
crops
codons
weed control

Cite this

@article{902354141e464e739da8fa3e5e98948b,
title = "Novel α-tubulin mutations conferring resistance to dinitroaniline herbicides in Lolium rigidum",
abstract = "The dinitroaniline herbicides (particularly trifluralin) have been globally used in many crops for selective grass weed control. Consequently, trifluralin resistance has been documented in several important crop weed species and has recently reached a level of concern in Australian Lolium rigidum populations. Here, we report novel mutations in the L. rigidum α-tubulin gene which confer resistance to trifluralin and other dinitroaniline herbicides. Nucleotide mutations at the highly conserved codon Arg-243 resulted in amino acid substitutions of Met or Lys. Rice calli transformed with the mutant 243-Met or 243-Lys α-tubulin genes were 4- to 8-fold more resistant to trifluralin and other dinitroaniline herbicides (e.g., ethalfluralin and pendimethalin) compared to calli transformed with the wild type α-tubulin gene from L. rigidum. Comprehensive modeling of molecular docking predicts that Arg-243 is close to the trifluralin binding site on the α-tubulin surface and that replacement of Arg-243 by Met/Lys-243 results in a spatial shift of the trifluralin binding domain, reduction of trifluralin-tubulin contacts, and unfavorable interactions. The major effect of these substitutions is a significant rise of free interaction energy between α-tubulin and trifluralin, as well as between trifluralin and its whole molecular environment. These results demonstrate that the Arg-243 residue in α-tubulin is a determinant for trifluralin sensitivity, and the novel Arg-243-Met/Lys mutations may confer trifluralin resistance in L. rigidum.",
keywords = "Dinitroanilines, Lolium rigidum, Mutation, Trifluralin resistance, α-tubulin",
author = "Zhizhan Chu and Jinyi Chen and Alex Nyporko and Heping Han and Qin Yu and Stephen Powles",
year = "2018",
month = "2",
day = "6",
doi = "10.3389/fpls.2018.00097",
language = "English",
volume = "9",
journal = "Frontiers in Plant Science",
issn = "1664-462X",
publisher = "Frontiers Media SA",

}

Novel α-tubulin mutations conferring resistance to dinitroaniline herbicides in Lolium rigidum. / Chu, Zhizhan; Chen, Jinyi; Nyporko, Alex; Han, Heping; Yu, Qin; Powles, Stephen.

In: Frontiers in Plant Science, Vol. 9, 97, 06.02.2018.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Novel α-tubulin mutations conferring resistance to dinitroaniline herbicides in Lolium rigidum

AU - Chu, Zhizhan

AU - Chen, Jinyi

AU - Nyporko, Alex

AU - Han, Heping

AU - Yu, Qin

AU - Powles, Stephen

PY - 2018/2/6

Y1 - 2018/2/6

N2 - The dinitroaniline herbicides (particularly trifluralin) have been globally used in many crops for selective grass weed control. Consequently, trifluralin resistance has been documented in several important crop weed species and has recently reached a level of concern in Australian Lolium rigidum populations. Here, we report novel mutations in the L. rigidum α-tubulin gene which confer resistance to trifluralin and other dinitroaniline herbicides. Nucleotide mutations at the highly conserved codon Arg-243 resulted in amino acid substitutions of Met or Lys. Rice calli transformed with the mutant 243-Met or 243-Lys α-tubulin genes were 4- to 8-fold more resistant to trifluralin and other dinitroaniline herbicides (e.g., ethalfluralin and pendimethalin) compared to calli transformed with the wild type α-tubulin gene from L. rigidum. Comprehensive modeling of molecular docking predicts that Arg-243 is close to the trifluralin binding site on the α-tubulin surface and that replacement of Arg-243 by Met/Lys-243 results in a spatial shift of the trifluralin binding domain, reduction of trifluralin-tubulin contacts, and unfavorable interactions. The major effect of these substitutions is a significant rise of free interaction energy between α-tubulin and trifluralin, as well as between trifluralin and its whole molecular environment. These results demonstrate that the Arg-243 residue in α-tubulin is a determinant for trifluralin sensitivity, and the novel Arg-243-Met/Lys mutations may confer trifluralin resistance in L. rigidum.

AB - The dinitroaniline herbicides (particularly trifluralin) have been globally used in many crops for selective grass weed control. Consequently, trifluralin resistance has been documented in several important crop weed species and has recently reached a level of concern in Australian Lolium rigidum populations. Here, we report novel mutations in the L. rigidum α-tubulin gene which confer resistance to trifluralin and other dinitroaniline herbicides. Nucleotide mutations at the highly conserved codon Arg-243 resulted in amino acid substitutions of Met or Lys. Rice calli transformed with the mutant 243-Met or 243-Lys α-tubulin genes were 4- to 8-fold more resistant to trifluralin and other dinitroaniline herbicides (e.g., ethalfluralin and pendimethalin) compared to calli transformed with the wild type α-tubulin gene from L. rigidum. Comprehensive modeling of molecular docking predicts that Arg-243 is close to the trifluralin binding site on the α-tubulin surface and that replacement of Arg-243 by Met/Lys-243 results in a spatial shift of the trifluralin binding domain, reduction of trifluralin-tubulin contacts, and unfavorable interactions. The major effect of these substitutions is a significant rise of free interaction energy between α-tubulin and trifluralin, as well as between trifluralin and its whole molecular environment. These results demonstrate that the Arg-243 residue in α-tubulin is a determinant for trifluralin sensitivity, and the novel Arg-243-Met/Lys mutations may confer trifluralin resistance in L. rigidum.

KW - Dinitroanilines

KW - Lolium rigidum

KW - Mutation

KW - Trifluralin resistance

KW - α-tubulin

UR - http://www.scopus.com/inward/record.url?scp=85043333990&partnerID=8YFLogxK

U2 - 10.3389/fpls.2018.00097

DO - 10.3389/fpls.2018.00097

M3 - Article

VL - 9

JO - Frontiers in Plant Science

JF - Frontiers in Plant Science

SN - 1664-462X

M1 - 97

ER -