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Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis.
J Biol Chem. 2018 11 16; 293(46):17731-17738.JB

Abstract

Herbicide-resistance traits are the most widely used agriculture biotechnology products. Yet, to maintain their effectiveness and to mitigate selection of herbicide-resistant weeds, the discovery of new resistance traits that use different chemical modes of action is essential. In plants, the Gretchen Hagen 3 (GH3) acyl acid amido synthetases catalyze the conjugation of amino acids to jasmonate and auxin phytohormones. This reaction chemistry has not been explored as a possible approach for herbicide modification and inactivation. Here, we examined a set of Arabidopsis GH3 proteins that use the auxins indole-3-acetic acid (IAA) and indole-3-butyric acid (IBA) as substrates along with the corresponding auxinic phenoxyalkanoic acid herbicides 2,4-dichlorophenoxylacetic acid (2,4-D) and 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB). The IBA-specific AtGH3.15 protein displayed high catalytic activity with 2,4-DB, which was comparable to its activity with IBA. Screening of phenoxyalkanoic and phenylalkyl acids indicated that side-chain length of alkanoic and alkyl acids is a key feature of AtGH3.15's substrate preference. The X-ray crystal structure of the AtGH3.15·2,4-DB complex revealed how the herbicide binds in the active site. In root elongation assays, Arabidopsis AtGH3.15-knockout and -overexpression lines grown in the presence of 2,4-DB exhibited hypersensitivity and tolerance, respectively, indicating that the AtGH3.15-catalyzed modification inactivates 2,4-DB. These findings suggest a potential use for AtGH3.15, and perhaps other GH3 proteins, as herbicide-modifying enzymes that employ a mode of action different from those of currently available herbicide-resistance traits.

Authors+Show Affiliations

From the Department of Biology, Washington University, St. Louis, Missouri 63130.From the Department of Biology, Washington University, St. Louis, Missouri 63130.From the Department of Biology, Washington University, St. Louis, Missouri 63130.From the Department of Biology, Washington University, St. Louis, Missouri 63130. Electronic address: jjez@wustl.edu.

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

30315112

Citation

Sherp, Ashley M., et al. "Modification of Auxinic Phenoxyalkanoic Acid Herbicides By the Acyl Acid Amido Synthetase GH3.15 From Arabidopsis." The Journal of Biological Chemistry, vol. 293, no. 46, 2018, pp. 17731-17738.
Sherp AM, Lee SG, Schraft E, et al. Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis. J Biol Chem. 2018;293(46):17731-17738.
Sherp, A. M., Lee, S. G., Schraft, E., & Jez, J. M. (2018). Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis. The Journal of Biological Chemistry, 293(46), 17731-17738. https://doi.org/10.1074/jbc.RA118.004975
Sherp AM, et al. Modification of Auxinic Phenoxyalkanoic Acid Herbicides By the Acyl Acid Amido Synthetase GH3.15 From Arabidopsis. J Biol Chem. 2018 11 16;293(46):17731-17738. PubMed PMID: 30315112.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis. AU - Sherp,Ashley M, AU - Lee,Soon Goo, AU - Schraft,Evelyn, AU - Jez,Joseph M, Y1 - 2018/10/12/ PY - 2018/07/20/received PY - 2018/10/06/revised PY - 2018/10/14/pubmed PY - 2019/4/11/medline PY - 2018/10/14/entrez KW - 2,4-D KW - Arabidopsis KW - Arabidopsis thaliana KW - Gretchen Hagen 3 KW - X-ray crystallography KW - acyl acid amido synthetase KW - auxin KW - enzyme kinetics KW - herbicide tolerance KW - herbicides KW - protein structure KW - structure-activity relationship SP - 17731 EP - 17738 JF - The Journal of biological chemistry JO - J Biol Chem VL - 293 IS - 46 N2 - Herbicide-resistance traits are the most widely used agriculture biotechnology products. Yet, to maintain their effectiveness and to mitigate selection of herbicide-resistant weeds, the discovery of new resistance traits that use different chemical modes of action is essential. In plants, the Gretchen Hagen 3 (GH3) acyl acid amido synthetases catalyze the conjugation of amino acids to jasmonate and auxin phytohormones. This reaction chemistry has not been explored as a possible approach for herbicide modification and inactivation. Here, we examined a set of Arabidopsis GH3 proteins that use the auxins indole-3-acetic acid (IAA) and indole-3-butyric acid (IBA) as substrates along with the corresponding auxinic phenoxyalkanoic acid herbicides 2,4-dichlorophenoxylacetic acid (2,4-D) and 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB). The IBA-specific AtGH3.15 protein displayed high catalytic activity with 2,4-DB, which was comparable to its activity with IBA. Screening of phenoxyalkanoic and phenylalkyl acids indicated that side-chain length of alkanoic and alkyl acids is a key feature of AtGH3.15's substrate preference. The X-ray crystal structure of the AtGH3.15·2,4-DB complex revealed how the herbicide binds in the active site. In root elongation assays, Arabidopsis AtGH3.15-knockout and -overexpression lines grown in the presence of 2,4-DB exhibited hypersensitivity and tolerance, respectively, indicating that the AtGH3.15-catalyzed modification inactivates 2,4-DB. These findings suggest a potential use for AtGH3.15, and perhaps other GH3 proteins, as herbicide-modifying enzymes that employ a mode of action different from those of currently available herbicide-resistance traits. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/30315112/Modification_of_auxinic_phenoxyalkanoic_acid_herbicides_by_the_acyl_acid_amido_synthetase_GH3_15_from_Arabidopsis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)31231-X DB - PRIME DP - Unbound Medicine ER -