Cysteine proteases are activated in sensitive Amaranthus palmeri populations upon treatment with herbicides inhibiting amino acid biosynthesis

Author:

Barco‐Antoñanzas Maria1ORCID,Font‐Farre Maria2ORCID,Eceiza Mikel V.1ORCID,Gil‐Monreal Miriam1ORCID,van der Hoorn Renier A. L.2ORCID,Royuela Mercedes1ORCID,Zabalza Ana1ORCID

Affiliation:

1. Institute for Multidisciplinary Research in Applied Biology (IMAB), Universidad Pública de Navarra (UPNA), Campus de Arrosadía Pamplona Spain

2. The Plant Chemetics Laboratory, Department of Biology Sciences University of Oxford Oxford UK

Abstract

AbstractThe herbicides glyphosate and pyrithiobac inhibit the enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) in the aromatic amino acid biosynthetic pathway and acetolactate synthase (ALS) in the branched‐chain amino acid biosynthetic pathway, respectively. Here we characterise the protease activity profiles of a sensitive (S), a glyphosate‐resistant (GR) and a multiple‐resistant (MR) population of Amaranthus palmeri in response to glyphosate and pyrithiobac. Amino acid accumulation and cysteine protease activities were induced with both herbicides in the S population and with pyrithiobac in the GR population, suggesting that the increase in cysteine proteases is responsible for the increased degradation of the available proteins and the observed increase in free amino acids. Herbicides did not induce any changes in the proteolytic activities in the populations with target‐site resistance, indicating that this effect was only induced in sensitive plants.

Funder

Eusko Jaurlaritza

Ministerio de Ciencia e Innovación

Ministerio de Economía y Competitividad

Publisher

Wiley

Subject

Cell Biology,Plant Science,Genetics,General Medicine,Physiology

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