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Target‐site resistance to ALS‐inhibiting herbicides in Apera spica‐venti populations is conferred by documented and previously unknown mutations
Author(s) -
MASSA D,
KRENZ B,
GERHARDS R
Publication year - 2011
Publication title -
weed research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 74
eISSN - 1365-3180
pISSN - 0043-1737
DOI - 10.1111/j.1365-3180.2011.00843.x
Subject(s) - acetolactate synthase , genetics , biology , population , mutation , weed , cleaved amplified polymorphic sequence , gene , wild type , herbicide resistance , polymerase chain reaction , botany , mutant , medicine , environmental health , restriction fragment length polymorphism
Massa D, Krenz B & Gerhards R (2011). Target‐site resistance to ALS‐inhibiting herbicides in Apera spica‐venti populations is conferred by documented and previously unknown mutations. Weed Research 51 , 294–303. Summary In this study, whole‐plant bioassays were performed on 72 Apera spica‐venti populations that have survived application of acetolactate synthase (ALS)‐inhibiting herbicides in recent years. Molecular genetic analysis of the ALS gene revealed a Thr mutation at Pro 197 within 67 populations. Sequencing of the whole ALS gene from wild‐type and resistant plants not carrying the above‐mentioned mutation revealed the presence of a Leu mutation at Trp 574 within two populations and an Asn mutation at Pro 197 within two populations. As the Pro 197 ‐Asn amino acid substitution is reported for the first time in a field‐selected weed population, a Cleaved Amplified Polymorphic Sequences (CAPS) marker was developed for its quick detection. In addition, one novel mutation was found within a population that coded for a His substitution at Arg 377 . Enzyme assays confirmed a significant reduction in inhibition of ALS activity compared with the wild type. This population showed resistance to sulfonylureas (SUs) and cross‐resistance to sulfonylaminocarbonyltriazolinones (SCTs) and triazolopyrimidines (TPs) within the whole‐plant bioassays. ALS protein sequence alignments from weedy and cultural plants revealed that the Arg377 is highly conserved among known wild‐type enzymes. In agreement with existing literature concerning the structure and mechanisms of inhibition of plant ALS, this mutation is probably involved in target‐site resistance to ALS inhibitors. Our results suggest that further single‐nucleotide polymorphisms impairing proper herbicide performance might be selected within field populations in the near future, making the short‐ and long‐range evolution of target‐site resistance difficult to predict depending solely on herbicide use history.