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Das, M.* ; Reichman, J.R.* ; Haberer, G. ; Welzl, G. ; Aceituno, F.F.* ; Mader, M.T. ; Watrud, L.S.* ; Pfleeger, T.G.* ; Gutiérrez, R.A.* ; Schäffner, A. ; Olszyk, D.M.*

A composite transcriptional signature differentiates responses towards closely related herbicides in Arabidopsis thaliana and Brassica napus.

Plant Mol. Biol. 72, 545-556 (2010)
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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
In this study, genome-wide expression profiling based on Affymetrix ATH1 arrays was used to identify discriminating responses of Arabidopsis thaliana to five herbicides, which contain active ingredients targeting two different branches of amino acid biosynthesis. One herbicide contained glyphosate, which targets 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), while the other four herbicides contain different acetolactate synthase (ALS) inhibiting compounds. In contrast to the herbicide containing glyphosate, which affected only a few transcripts, many effects of the ALS inhibiting herbicides were revealed based on transcriptional changes related to ribosome biogenesis and translation, secondary metabolism, cell wall modification and growth. The expression pattern of a set of 101 genes provided a specific, composite signature that was distinct from other major stress responses and differentiated among herbicides targeting the same enzyme (ALS) or containing the same chemical class of active ingredient (sulfonylurea). A set of homologous genes could be identified in Brassica napus that exhibited a similar expression pattern and correctly distinguished exposure to the five herbicides. Our results show the ability of a limited number of genes to classify and differentiate responses to closely related herbicides in A. thaliana and B. napus and the transferability of a complex transcriptional signature across species.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Differentiation of herbicides; Gene expression signature; Transfer from model to crop plant; Acetolactate synthase; 5-enolpyruvylshikimate-3-phosphate synthase
ISSN (print) / ISBN 0167-4412
e-ISSN 0167-4412
Quellenangaben Band: 72, Heft: 4-5, Seiten: 545-556 Artikelnummer: , Supplement: ,
Verlag Springer
Begutachtungsstatus Peer reviewed