AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth

Twenty-two amino acid substitutions at seven conserved amino acid residues in the acetohydroxyacid synthase [AHAS] gene have been identified to date that confer target-site resistance to AHAS-inhibiting herbicides in biotypes of field-evolved resistant weed species. However, the effect of resistance mutations on AHAS functionality and plant growth has been investigated for only a very few mutations. This research investigates the effect of various AHAS resistance mutations in Lolium rigidum on AHAS functionality and plant growth. The enzyme kinetics of AHAS from five purified L. rigidum populations, each homozygous for the resistance mutations Pro-197-Ala, Pro-197-Arg, Pro-197-Gln, Pro-197-Ser or Trp-574-Leu, were characterized and the pleiotropic effect of three mutations on plant growth was assessed via relative growth rate analysis. All these resistance mutations endowed a herbicide-resistant AHAS and most resulted in higher extractable AHAS activity, with no-to-minor changes in AHAS kinetics. The Pro-197-Arg mutation slightly [but significantly] increased the K m for pyruvate and remarkably increased sensitivity to feedback inhibition by branched chain amino acids. Whereas the Pro-197-Ser and Trp-574-Leu mutations exhibited no significant effects on plant growth, the Pro-197-Arg mutation resulted in lower growth rates. It is clear that, at least in L. rigidum, these five AHAS resistance mutations have no major impact on AHAS functionality and hence probably no plant resistance costs. These results, in part, explain why so many Pro-197 AHAS resistance mutations in AHAS have evolved and why the Pro-197-Ser and the Trp-574-Leu AHAS resistance mutations are frequently found in many weed species.

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Bibliographic Details
Main Authors: Yu, Qin, Han, Heping, Vila Aiub, Martín Miguel, Powles, Stephen B.
Format: Texto biblioteca
Language:eng
Subjects:AHAS RESISTANCE MUTATION, ENZYME KINETICS, HERBICIDE RESISTANCE, RELATIVE GROWTH RATE, ACETOLACTATE SYNTHASE, BRANCHED CHAIN AMINO ACID, HERBICIDE, DRUG ANTAGONISM, DRUG EFFECT, ENZYMOLOGY, GENETICS, GROWTH, DEVELOPMENT AND AGING, HOMOZYGOTE, LOLIUM, METABOLISM, MUTATION, AMINO ACID SUBSTITUTION, AMINO ACIDS, BRANCHED-CHAIN, HERBICIDES, LOLIUM RIGIDUM,
Online Access:http://ceiba.agro.uba.ar/cgi-bin/koha/opac-detail.pl?biblionumber=46445
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id KOHA-OAI-AGRO:46445
record_format koha
institution UBA FA
collection Koha
country Argentina
countrycode AR
component Bibliográfico
access En linea
En linea
databasecode cat-ceiba
tag biblioteca
region America del Sur
libraryname Biblioteca Central FAUBA
language eng
topic AHAS RESISTANCE MUTATION
ENZYME KINETICS
HERBICIDE RESISTANCE
RELATIVE GROWTH RATE
ACETOLACTATE SYNTHASE
BRANCHED CHAIN AMINO ACID
HERBICIDE
DRUG ANTAGONISM
DRUG EFFECT
ENZYMOLOGY
GENETICS
GROWTH, DEVELOPMENT AND AGING
HERBICIDE RESISTANCE
HOMOZYGOTE
LOLIUM
METABOLISM
MUTATION
ACETOLACTATE SYNTHASE
AMINO ACID SUBSTITUTION
AMINO ACIDS, BRANCHED-CHAIN
HERBICIDES
HOMOZYGOTE
LOLIUM RIGIDUM
AHAS RESISTANCE MUTATION
ENZYME KINETICS
HERBICIDE RESISTANCE
RELATIVE GROWTH RATE
ACETOLACTATE SYNTHASE
BRANCHED CHAIN AMINO ACID
HERBICIDE
DRUG ANTAGONISM
DRUG EFFECT
ENZYMOLOGY
GENETICS
GROWTH, DEVELOPMENT AND AGING
HERBICIDE RESISTANCE
HOMOZYGOTE
LOLIUM
METABOLISM
MUTATION
ACETOLACTATE SYNTHASE
AMINO ACID SUBSTITUTION
AMINO ACIDS, BRANCHED-CHAIN
HERBICIDES
HOMOZYGOTE
LOLIUM RIGIDUM
spellingShingle AHAS RESISTANCE MUTATION
ENZYME KINETICS
HERBICIDE RESISTANCE
RELATIVE GROWTH RATE
ACETOLACTATE SYNTHASE
BRANCHED CHAIN AMINO ACID
HERBICIDE
DRUG ANTAGONISM
DRUG EFFECT
ENZYMOLOGY
GENETICS
GROWTH, DEVELOPMENT AND AGING
HERBICIDE RESISTANCE
HOMOZYGOTE
LOLIUM
METABOLISM
MUTATION
ACETOLACTATE SYNTHASE
AMINO ACID SUBSTITUTION
AMINO ACIDS, BRANCHED-CHAIN
HERBICIDES
HOMOZYGOTE
LOLIUM RIGIDUM
AHAS RESISTANCE MUTATION
ENZYME KINETICS
HERBICIDE RESISTANCE
RELATIVE GROWTH RATE
ACETOLACTATE SYNTHASE
BRANCHED CHAIN AMINO ACID
HERBICIDE
DRUG ANTAGONISM
DRUG EFFECT
ENZYMOLOGY
GENETICS
GROWTH, DEVELOPMENT AND AGING
HERBICIDE RESISTANCE
HOMOZYGOTE
LOLIUM
METABOLISM
MUTATION
ACETOLACTATE SYNTHASE
AMINO ACID SUBSTITUTION
AMINO ACIDS, BRANCHED-CHAIN
HERBICIDES
HOMOZYGOTE
LOLIUM RIGIDUM
Yu, Qin
Han, Heping
Vila Aiub, Martín Miguel
Powles, Stephen B.
AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
description Twenty-two amino acid substitutions at seven conserved amino acid residues in the acetohydroxyacid synthase [AHAS] gene have been identified to date that confer target-site resistance to AHAS-inhibiting herbicides in biotypes of field-evolved resistant weed species. However, the effect of resistance mutations on AHAS functionality and plant growth has been investigated for only a very few mutations. This research investigates the effect of various AHAS resistance mutations in Lolium rigidum on AHAS functionality and plant growth. The enzyme kinetics of AHAS from five purified L. rigidum populations, each homozygous for the resistance mutations Pro-197-Ala, Pro-197-Arg, Pro-197-Gln, Pro-197-Ser or Trp-574-Leu, were characterized and the pleiotropic effect of three mutations on plant growth was assessed via relative growth rate analysis. All these resistance mutations endowed a herbicide-resistant AHAS and most resulted in higher extractable AHAS activity, with no-to-minor changes in AHAS kinetics. The Pro-197-Arg mutation slightly [but significantly] increased the K m for pyruvate and remarkably increased sensitivity to feedback inhibition by branched chain amino acids. Whereas the Pro-197-Ser and Trp-574-Leu mutations exhibited no significant effects on plant growth, the Pro-197-Arg mutation resulted in lower growth rates. It is clear that, at least in L. rigidum, these five AHAS resistance mutations have no major impact on AHAS functionality and hence probably no plant resistance costs. These results, in part, explain why so many Pro-197 AHAS resistance mutations in AHAS have evolved and why the Pro-197-Ser and the Trp-574-Leu AHAS resistance mutations are frequently found in many weed species.
format Texto
topic_facet AHAS RESISTANCE MUTATION
ENZYME KINETICS
HERBICIDE RESISTANCE
RELATIVE GROWTH RATE
ACETOLACTATE SYNTHASE
BRANCHED CHAIN AMINO ACID
HERBICIDE
DRUG ANTAGONISM
DRUG EFFECT
ENZYMOLOGY
GENETICS
GROWTH, DEVELOPMENT AND AGING
HERBICIDE RESISTANCE
HOMOZYGOTE
LOLIUM
METABOLISM
MUTATION
ACETOLACTATE SYNTHASE
AMINO ACID SUBSTITUTION
AMINO ACIDS, BRANCHED-CHAIN
HERBICIDES
HOMOZYGOTE
LOLIUM RIGIDUM
author Yu, Qin
Han, Heping
Vila Aiub, Martín Miguel
Powles, Stephen B.
author_facet Yu, Qin
Han, Heping
Vila Aiub, Martín Miguel
Powles, Stephen B.
author_sort Yu, Qin
title AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
title_short AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
title_full AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
title_fullStr AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
title_full_unstemmed AHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growth
title_sort ahas herbicide resistance endowing mutations effect on ahas functionality and plant growth
url http://ceiba.agro.uba.ar/cgi-bin/koha/opac-detail.pl?biblionumber=46445
work_keys_str_mv AT yuqin ahasherbicideresistanceendowingmutationseffectonahasfunctionalityandplantgrowth
AT hanheping ahasherbicideresistanceendowingmutationseffectonahasfunctionalityandplantgrowth
AT vilaaiubmartinmiguel ahasherbicideresistanceendowingmutationseffectonahasfunctionalityandplantgrowth
AT powlesstephenb ahasherbicideresistanceendowingmutationseffectonahasfunctionalityandplantgrowth
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spelling KOHA-OAI-AGRO:464452023-08-11T15:21:55Zhttp://ceiba.agro.uba.ar/cgi-bin/koha/opac-detail.pl?biblionumber=46445AAGAHAS herbicide resistance endowing mutations effect on AHAS functionality and plant growthYu, QinHan, HepingVila Aiub, Martín MiguelPowles, Stephen B.textengapplication/pdfTwenty-two amino acid substitutions at seven conserved amino acid residues in the acetohydroxyacid synthase [AHAS] gene have been identified to date that confer target-site resistance to AHAS-inhibiting herbicides in biotypes of field-evolved resistant weed species. However, the effect of resistance mutations on AHAS functionality and plant growth has been investigated for only a very few mutations. This research investigates the effect of various AHAS resistance mutations in Lolium rigidum on AHAS functionality and plant growth. The enzyme kinetics of AHAS from five purified L. rigidum populations, each homozygous for the resistance mutations Pro-197-Ala, Pro-197-Arg, Pro-197-Gln, Pro-197-Ser or Trp-574-Leu, were characterized and the pleiotropic effect of three mutations on plant growth was assessed via relative growth rate analysis. All these resistance mutations endowed a herbicide-resistant AHAS and most resulted in higher extractable AHAS activity, with no-to-minor changes in AHAS kinetics. The Pro-197-Arg mutation slightly [but significantly] increased the K m for pyruvate and remarkably increased sensitivity to feedback inhibition by branched chain amino acids. Whereas the Pro-197-Ser and Trp-574-Leu mutations exhibited no significant effects on plant growth, the Pro-197-Arg mutation resulted in lower growth rates. It is clear that, at least in L. rigidum, these five AHAS resistance mutations have no major impact on AHAS functionality and hence probably no plant resistance costs. These results, in part, explain why so many Pro-197 AHAS resistance mutations in AHAS have evolved and why the Pro-197-Ser and the Trp-574-Leu AHAS resistance mutations are frequently found in many weed species.Twenty-two amino acid substitutions at seven conserved amino acid residues in the acetohydroxyacid synthase [AHAS] gene have been identified to date that confer target-site resistance to AHAS-inhibiting herbicides in biotypes of field-evolved resistant weed species. However, the effect of resistance mutations on AHAS functionality and plant growth has been investigated for only a very few mutations. This research investigates the effect of various AHAS resistance mutations in Lolium rigidum on AHAS functionality and plant growth. The enzyme kinetics of AHAS from five purified L. rigidum populations, each homozygous for the resistance mutations Pro-197-Ala, Pro-197-Arg, Pro-197-Gln, Pro-197-Ser or Trp-574-Leu, were characterized and the pleiotropic effect of three mutations on plant growth was assessed via relative growth rate analysis. All these resistance mutations endowed a herbicide-resistant AHAS and most resulted in higher extractable AHAS activity, with no-to-minor changes in AHAS kinetics. The Pro-197-Arg mutation slightly [but significantly] increased the K m for pyruvate and remarkably increased sensitivity to feedback inhibition by branched chain amino acids. Whereas the Pro-197-Ser and Trp-574-Leu mutations exhibited no significant effects on plant growth, the Pro-197-Arg mutation resulted in lower growth rates. It is clear that, at least in L. rigidum, these five AHAS resistance mutations have no major impact on AHAS functionality and hence probably no plant resistance costs. These results, in part, explain why so many Pro-197 AHAS resistance mutations in AHAS have evolved and why the Pro-197-Ser and the Trp-574-Leu AHAS resistance mutations are frequently found in many weed species.AHAS RESISTANCE MUTATIONENZYME KINETICSHERBICIDE RESISTANCERELATIVE GROWTH RATEACETOLACTATE SYNTHASEBRANCHED CHAIN AMINO ACIDHERBICIDEDRUG ANTAGONISMDRUG EFFECTENZYMOLOGYGENETICSGROWTH, DEVELOPMENT AND AGINGHERBICIDE RESISTANCEHOMOZYGOTELOLIUMMETABOLISMMUTATIONACETOLACTATE SYNTHASEAMINO ACID SUBSTITUTIONAMINO ACIDS, BRANCHED-CHAINHERBICIDESHOMOZYGOTELOLIUM RIGIDUMJournal of Experimental Botany