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Arabidopsis thaliana GH3.5 acyl acid amido synthetase mediates metabolic crosstalk in auxin and salicylic acid homeostasis.
Proc Natl Acad Sci U S A. 2016 11 29; 113(48):13917-13922.PN

Abstract

In Arabidopsis thaliana, the acyl acid amido synthetase Gretchen Hagen 3.5 (AtGH3.5) conjugates both indole-3-acetic acid (IAA) and salicylic acid (SA) to modulate auxin and pathogen response pathways. To understand the molecular basis for the activity of AtGH3.5, we determined the X-ray crystal structure of the enzyme in complex with IAA and AMP. Biochemical analysis demonstrates that the substrate preference of AtGH3.5 is wider than originally described and includes the natural auxin phenylacetic acid (PAA) and the potential SA precursor benzoic acid (BA). Residues that determine IAA versus BA substrate preference were identified. The dual functionality of AtGH3.5 is unique to this enzyme although multiple IAA-conjugating GH3 proteins share nearly identical acyl acid binding sites. In planta analysis of IAA, PAA, SA, and BA and their respective aspartyl conjugates were determined in wild-type and overexpressing lines of A thaliana This study suggests that AtGH3.5 conjugates auxins (i.e., IAA and PAA) and benzoates (i.e., SA and BA) to mediate crosstalk between different metabolic pathways, broadening the potential roles for GH3 acyl acid amido synthetases in plants.

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Authors+Show Affiliations

Westfall CS
Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.
Sherp AM
Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.
Zubieta C
Laboratoire de Physiologie Cellulaire et Vegetale, CNRS, Commissariat á l'Énergie Atomique et aux Énergies Alternatives, Institut National de la Recherche Agronomique, Université Grenoble Alpes, Institut de Biosciences et Biotechnologies de Grenoble, 38000 Grenoble, France.
Alvarez S
Donald Danforth Plant Science Center, St. Louis, MO 63132.
Schraft E
Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.
Marcellin R
Structural Biology Group, European Synchrotron Radiation Facility, 38043 Grenoble, France.
Ramirez L
Department of Biology, Washington University in St. Louis, St. Louis, MO 63130.
Jez JM
Department of Biology, Washington University in St. Louis, St. Louis, MO 63130; jjez@biology2.wustl.edu.

MeSH

Amino AcidsArabidopsisArabidopsis ProteinsCrystallography, X-RayGene Expression Regulation, PlantHomeostasisIndoleacetic AcidsLigasesSalicylic AcidSubstrate Specificity

Pub Type(s)

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

Language

eng

PubMed ID

27849615

Citation

Westfall, Corey S., et al. "Arabidopsis Thaliana GH3.5 Acyl Acid Amido Synthetase Mediates Metabolic Crosstalk in Auxin and Salicylic Acid Homeostasis." Proceedings of the National Academy of Sciences of the United States of America, vol. 113, no. 48, 2016, pp. 13917-13922.
Westfall CS, Sherp AM, Zubieta C, et al. Arabidopsis thaliana GH3.5 acyl acid amido synthetase mediates metabolic crosstalk in auxin and salicylic acid homeostasis. Proc Natl Acad Sci U S A. 2016;113(48):13917-13922.
Westfall, C. S., Sherp, A. M., Zubieta, C., Alvarez, S., Schraft, E., Marcellin, R., Ramirez, L., & Jez, J. M. (2016). Arabidopsis thaliana GH3.5 acyl acid amido synthetase mediates metabolic crosstalk in auxin and salicylic acid homeostasis. Proceedings of the National Academy of Sciences of the United States of America, 113(48), 13917-13922.
Westfall CS, et al. Arabidopsis Thaliana GH3.5 Acyl Acid Amido Synthetase Mediates Metabolic Crosstalk in Auxin and Salicylic Acid Homeostasis. Proc Natl Acad Sci U S A. 2016 11 29;113(48):13917-13922. PubMed PMID: 27849615.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Arabidopsis thaliana GH3.5 acyl acid amido synthetase mediates metabolic crosstalk in auxin and salicylic acid homeostasis. AU - Westfall,Corey S, AU - Sherp,Ashley M, AU - Zubieta,Chloe, AU - Alvarez,Sophie, AU - Schraft,Evelyn, AU - Marcellin,Romain, AU - Ramirez,Loren, AU - Jez,Joseph M, Y1 - 2016/11/14/ PY - 2016/11/17/pubmed PY - 2018/3/29/medline PY - 2016/11/17/entrez KW - Arabidopsis KW - auxin KW - plant biochemistry KW - plant hormone KW - protein structure SP - 13917 EP - 13922 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 113 IS - 48 N2 - In Arabidopsis thaliana, the acyl acid amido synthetase Gretchen Hagen 3.5 (AtGH3.5) conjugates both indole-3-acetic acid (IAA) and salicylic acid (SA) to modulate auxin and pathogen response pathways. To understand the molecular basis for the activity of AtGH3.5, we determined the X-ray crystal structure of the enzyme in complex with IAA and AMP. Biochemical analysis demonstrates that the substrate preference of AtGH3.5 is wider than originally described and includes the natural auxin phenylacetic acid (PAA) and the potential SA precursor benzoic acid (BA). Residues that determine IAA versus BA substrate preference were identified. The dual functionality of AtGH3.5 is unique to this enzyme although multiple IAA-conjugating GH3 proteins share nearly identical acyl acid binding sites. In planta analysis of IAA, PAA, SA, and BA and their respective aspartyl conjugates were determined in wild-type and overexpressing lines of A thaliana This study suggests that AtGH3.5 conjugates auxins (i.e., IAA and PAA) and benzoates (i.e., SA and BA) to mediate crosstalk between different metabolic pathways, broadening the potential roles for GH3 acyl acid amido synthetases in plants. SN - 1091-6490 UR - https://www.unboundmedicine.com/medline/citation/27849615/Arabidopsis_thaliana_GH3_5_acyl_acid_amido_synthetase_mediates_metabolic_crosstalk_in_auxin_and_salicylic_acid_homeostasis_ DB - PRIME DP - Unbound Medicine ER -