Evidence map›Paper›PMID 26353912›Full record

ArticlePlanta2016

A new amino acid substitution (Ala-205-Phe) in acetolactate synthase (ALS) confers broad spectrum resistance to ALS-inhibiting herbicides.

James T Brosnan, Jose J Vargas, Gregory K Breeden, Logan Grier, Raphael A Aponte, Stefan Tresch, Martin Laforest

Open access · hybridAbstract read
In one paragraph

Article in Planta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
8.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  7. Article
  8. Asp-376-Glu substitution endows target-site resistance to AHAS inhibitors inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Comprehensive understanding of acetohydroxyacid synthase inhibition by different herbicide families.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

James T BrosnanPlant Sciences Department, The University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN, 37996, USA. jbrosnan@utk.edu.
Jose J VargasPlant Sciences Department, The University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN, 37996, USA.
Gregory K BreedenPlant Sciences Department, The University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN, 37996, USA.
Logan GrierBASF Corporation, 26 Davis Dr., Research Triangle Park, NC, 27709, USA.
Raphael A AponteBASF SE, Speyerer Str. 2, 67117, Limburgerhof, Germany.
Stefan TreschBASF SE, Speyerer Str. 2, 67117, Limburgerhof, Germany.
Martin LaforestHorticulture R&D Center, Agriculture and Agri-Food Canada, St-Jean-sur-Richelieu, QC, Canada.
University of Tennessee at Knoxville · USAgriculture and Agri-Food Canada · CATriangle · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MAIN

conclusionThis is a first report of an Ala-205-Phe substitution in acetolactate synthase conferring resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides. Resistance to acetolactate synthase (ALS) and photosystem II inhibiting herbicides was confirmed in a population of allotetraploid annual bluegrass (Poa annua L.; POAAN-R3) selected from golf course turf in Tennessee. Genetic sequencing revealed that seven of eight POAAN-R3 plants had a point mutation in the psbA gene resulting in a known Ser-264-Gly substitution on the D1 protein. Whole plant testing confirmed that this substitution conferred resistance to simazine in POAAN-R3. Two homeologous forms of the ALS gene (ALSa and ALSb) were detected and expressed in all POAAN-R3 plants sequenced. The seven plants possessing the Ser-264-Gly mutation conferring resistance to simazine also had a homozygous Ala-205-Phe substitution on ALSb, caused by two nucleic acid substitutions in one codon. In vitro ALS activity assays with recombinant protein and whole plant testing confirmed that this Ala-205-Phe substitution conferred resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylamino-carbonyl- triazolinones, and pyrimidinyl (thio) benzoate herbicides. This is the first report of Ala-205-Phe mutation conferring wide spectrum resistance to ALS inhibiting herbicides.

Indexed as

Herbicide ResistanceAcetolactate SynthaseAlanineAmino Acid SubstitutionBase SequenceHerbicidesHomozygoteMolecular Sequence DataMutationPhenylalaninePoaRecombinant ProteinsSequence Analysis, DNAAcetolactate SynthaseAlanineHerbicidesPhenylalanineRecombinant ProteinsAcetolactate synthaseAnnual bluegrassPhenylalanineTurfWeed resistance

Identifiers

PMID26353912
PMCPMC4698308
OpenAlexW2156955738

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.