title: Proteolytic pathways induced by herbicides that inhibit amino acid biosynthesis.
abstract: BACKGROUND
  The herbicides glyphosate (Gly) and imazamox (Imx) inhibit the biosynthesis of aromatic and branched-chain amino acids, respectively. Although these herbicides inhibit different pathways, they have been reported to show several common physiological effects in their modes of action, such as increasing free amino acid contents and decreasing soluble protein contents. To investigate proteolytic activities upon treatment with Gly and Imx, pea plants grown in hydroponic culture were treated with Imx or Gly, and the proteolytic profile of the roots was evaluated through fluorogenic kinetic assays and activity-based protein profiling.
  
  
  RESULTS
  Several common changes in proteolytic activity were detected following Gly and Imx treatment. Both herbicides induced the ubiquitin-26 S proteasome system and papain-like cysteine proteases. In contrast, the activities of vacuolar processing enzymes, cysteine proteases and metacaspase 9 were reduced following treatment with both herbicides. Moreover, the activities of several putative serine protease were similarly increased or decreased following treatment with both herbicides. In contrast, an increase in YVADase activity was observed under Imx treatment versus a decrease under Gly treatment.
  
  
  CONCLUSIONS
  These results suggest that several proteolytic pathways are responsible for protein degradation upon herbicide treatment, although the specific role of each proteolytic activity remains to be determined.
authors.affiliation: Departamento de Ciencias del Medio Natural, Universidad Pública de Navarra, Pamplona, Spain.
authors.forename: Amaia
authors.initials: A
authors.lastname: Zulet
authors.forename: Miriam
authors.initials: M
authors.lastname: Gil-Monreal
authors.forename: Joji Grace
authors.initials: JG
authors.lastname: Villamor
authors.forename: Ana
authors.initials: A
authors.lastname: Zabalza
authors.forename: Renier A L
authors.initials: RA
authors.lastname: van der Hoorn
authors.forename: Mercedes
authors.initials: M
authors.lastname: Royuela
mesh_terms: D000596:Amino Acids / Q000096:biosynthesis*; D015153:Blotting, Western; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D005998:Glycine / Q000031:analogs & derivatives / Q000494:pharmacology; D006540:Herbicides / Q000494:pharmacology*; D018527:Hydroponics; D007093:Imidazoles / Q000494:pharmacology; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D007976:Leupeptins / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology; D018532:Pisum sativum / Q000187:drug effects* / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism; D018517:Plant Roots / Q000187:drug effects* / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D059748:Proteolysis / Q000187:drug effects*; D015398:Signal Transduction / Q000187:drug effects; D013997:Time Factors; D000097797:Glyphosate
chemical_list: D000596:Amino Acids; D015853:Cysteine Proteinase Inhibitors; D005998:Glycine; D006540:Herbicides; D007093:Imidazoles; D007930:Leucine; D007976:Leupeptins; D009842:Oligopeptides; D010940:Plant Proteins; D046988:Proteasome Endopeptidase Complex; D000097797:Glyphosate; C024974:E 64; C072553:benzyloxycarbonylleucyl-leucyl-leucine aldehyde; C494197:imazamox; C078846:epoxomicin
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