A novel amino acid substitution Trp574Arg in acetolactate synthase (ALS) confers broad resistance to ALS-inhibiting herbicides in crabgrass (Digitaria sanguinalis)

2017 ◽  
Vol 73 (12) ◽  
pp. 2538-2543 ◽  
Author(s):  
Jian Li ◽  
Mei Li ◽  
Xingxiang Gao ◽  
Feng Fang
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Acetolactate Synthase ◽  
Digitaria Sanguinalis

scholarly journals Distribution of Herbicide Resistances and Molecular Mechanisms Conferring Resistance in Missouri Waterhemp (Amaranthus rudisSauer) Populations

Weed Science ◽  
2015 ◽  
Vol 63 (1) ◽  
pp. 336-345 ◽  
Author(s):  
John L. Schultz ◽  
Laura A. Chatham ◽  
Chance W. Riggins ◽  
Patrick J. Tranel ◽  
Kevin W. Bradley
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Molecular Mechanisms ◽  
Dna Analysis ◽  
D1 Protein ◽  
Acetolactate Synthase ◽  
Glyphosate Resistance ◽  
Mechanisms Of Action ◽  
Resistance To Herbicides ◽  
Inhibitor Resistance

A survey of soybean fields containing waterhemp was conducted just prior to harvest in 2012 to determine the scope and extent of herbicide resistance and multiple herbicide resistances among a sample of Missouri waterhemp populations. Resistance was confirmed to glyphosate and to acetolactate synthase (ALS), protoporphyrinogen oxidase (PPO), photosystem II (PSII), and 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitors, but not to 2,4-D. Of the 187 populations tested, 186 exhibited resistance to chlorimuron. The proportions of populations with atrazine or glyphosate resistance were similar, with 30 and 29% of the populations surviving the 3× rates. Lactofen resistance was observed in 5% of the populations, whereas mesotrione resistance was only found in 1.6% of the populations. All populations tested were susceptible to 2,4-D at the 3× rate. At least 52% of the waterhemp populations tested exhibited resistance to herbicides from two mechanism of action. Resistance to atrazine plus chlorimuron as well as glyphosate plus chlorimuron was present in 29% of the populations. Three-way resistance, primarily comprised of resistance to atrazine plus chlorimuron plus glyphosate, was present in 11% of the populations. Resistance to herbicides from four mechanisms of action was found in 2% of the populations, and one population exhibited resistance to herbicides from five mechanisms of action. DNA analysis of a subsample of plants revealed that previously documented mechanisms of resistance in waterhemp, including the ΔG210 deletion conferring PPO-inhibitor resistance, the Trp574Leu amino acid substitution conferring ALS-inhibitor resistance, and elevated 5-enolypyruvyl-shikimate-3-phosphate synthase copy number and the Pro106Ser amino acid substitution resulting in glyphosate resistance, explained survival in many, but not all, instances. Atrazine resistance was not explained by the Ser264Gly D1 protein substitution. Overall, results from these experiments indicate that Missouri soybean fields contain waterhemp populations with resistance to glyphosate, ALS-, PPO-, PSII-, and HPPD-inhibiting herbicides, which are some of the most common mechanisms of action currently utilized for the control of this species in corn and soybean production systems. Additionally, these results indicate that slightly more than half of the populations tested exhibit resistance to more than one herbicide mechanisms of action. Managing the current resistance levels in existing populations is of utmost importance. The use of multiple, effective herbicide modes of action, both preemergence and postemergence, and the integration of optimum cultural and mechanical control practices will be vital in the management of Missouri waterhemp populations in the future.

A Trp574 to Leu Amino Acid Substitution in the ALS Gene of Annual Bluegrass (Poa annua) Is Associated with Resistance to ALS-Inhibiting Herbicides

Weed Science ◽  
2013 ◽  
Vol 61 (1) ◽  
pp. 21-25 ◽  
Author(s):  
J. Scott McElroy ◽  
Michael L. Flessner ◽  
Zhuoyu Wang ◽  
Fenny Dane ◽  
Robert H. Walker ◽  
...  
Keyword(s):  
Amino Acid ◽  
Point Mutation ◽  
Amino Acid Substitution ◽  
Acetolactate Synthase ◽  
Poa Annua ◽  
Golf Course ◽  
Missense Mutations ◽  
Gene Sequences ◽  
Susceptible Population ◽  
Annual Bluegrass

Annual bluegrass is commonly controlled by acetolactate synthase (ALS)-inhibiting herbicides in managed turfgrass. An annual bluegrass population with suspected resistance to ALS-inhibiting herbicides was collected from Grand National Golf Course in Opelika, AL (GN population). Subsequent testing confirmed resistance of the GN population to foramsulfuron, trifloxysulfuron, bispyribac-sodium (bispyribac), and imazaquin when compared to a susceptible population collected locally at Auburn University (AU population). Sequencing of the ALS gene revealed a point mutation resulting in an amino acid substitution at Trp574. Cloning of the ALS gene surrounding the Trp574 region yielded two distinct ALS gene sequences: one producing Trp574 and one producing Leu574. Trp574 to Leu has been previously correlated with resistance to ALS-inhibiting herbicides. Both AU and GN gene sequences contained other similar silent and missense mutations. This research confirms resistance of annual bluegrass to ALS-inhibiting herbicides with Trp574 to Leu amino acid substitution being the most likely mode of resistance based on past literature.

A New Mutation in PlantALSConfers Resistance to Five Classes of ALS-Inhibiting Herbicides

Weed Science ◽  
2007 ◽  
Vol 55 (2) ◽  
pp. 83-90 ◽  
Author(s):  
Cory M. Whaley ◽  
Henry P. Wilson ◽  
James H. Westwood
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Acetolactate Synthase ◽  
Single Nucleotide ◽  
Whole Plant ◽  
History Of ◽  
Als Inhibitor ◽  
Herbicide Use ◽  
Smooth Pigweed

Experiments were conducted to evaluate a biotype of smooth pigweed that had survived applications of sulfonylurea (SU) and imidazolinone (IMI) herbicides in a single season. The source field had a history of repeated acetolactate synthase (ALS)-inhibiting herbicide use over several years. Whole-plant response experiments evaluated the resistant (R11) biotype and an ALS-inhibitor susceptible (S) smooth pigweed biotype to herbicides from the SU, IMI, pyrimidinylthiobenzoate (PTB), and triazolopyrimidine sulfonanilide (TP) chemical families. The R11 biotype exhibited 60- to 3,200-fold resistance to all four ALS-Inhibiting herbicide chemistries compared with the S biotype. Nucleotide sequence comparison ofALSgenes from R11 and S biotypes revealed a single nucleotide difference that resulted in R11 having an amino acid substitution of aspartate to glutamate at position 376, as numbered relative to the protein sequence of mouseearcress. This is the first report of an amino acid substitution at this position of anALSgene isolated from a field-selected weed biotype. To verify the role of this mutation in herbicide resistance, theALSgene was cloned and expressed inArabidopsis. TransgenicArabidopsisexpressing thisALSgene exhibited resistance to SU, IMI, PTB, TP, and sulfonylaminocarbonyltriazolinone ALS-Inhibiting herbicide classes.

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

Planta ◽  
2015 ◽  
Vol 243 (1) ◽  
pp. 149-159 ◽  
Author(s):  
James T. Brosnan ◽  
Jose J. Vargas ◽  
Gregory K. Breeden ◽  
Logan Grier ◽  
Raphael A. Aponte ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Broad Spectrum ◽  
Acetolactate Synthase ◽  
Broad Spectrum Resistance

Hubsm: A Novel Amino Acid Substitution Matrix for Comparing Hub Proteins

2017 ◽  
Vol 7 (8) ◽  
pp. 212
Author(s):  
Renganayaki G. ◽  
Achuthsankar S. Nair
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Low Complexity ◽  
Database Search ◽  
Substitution Matrix ◽  
Compositional Bias ◽  
Sequence Alignments ◽  
Amino Acid Substitution Matrix ◽  
Alignment Algorithms ◽  
Hub Proteins

Sequence alignment algorithms and  database search methods use BLOSUM and PAM substitution matrices constructed from general proteins. These de facto matrices are not optimal to align sequences accurately, for the proteins with markedly different compositional bias in the amino acid.   In this work, a new amino acid substitution matrix is calculated for the disorder and low complexity rich region of Hub proteins, based on residue characteristics. Insights into the amino acid background frequencies and the substitution scores obtained from the Hubsm unveils the  residue substitution patterns which differs from commonly used scoring matrices .When comparing the Hub protein sequences for detecting homologs,  the use of this Hubsm matrix yields better results than PAM and BLOSUM matrices. Usage of Hubsm matrix can be optimal in database search and for the construction of more accurate sequence alignments of Hub proteins.

Sign in / Sign up

Export Citation Format

Share Document