Evolutionary history of the GH3 family of acyl adenylases in rosids

Okrent, Rachel A.; Wildermuth, Mary C.

doi:10.1007/s11103-011-9776-y

Cited by 68 publications

(78 citation statements)

References 80 publications

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“…These data indicate that these genes are under a range of transcriptional controls. Similarly, variations in patterns of transcription have been observed in other species (Gee et al, 1991;Terol et al, 2006;Fu et al, 2011a;Okrent and Wildermuth, 2011;Kumar et al, 2012). If we conclude from the above evidence that there is a degree of specialization among the six grapevine IAA-conjugating enzymes, why are there likely to be only two JA-conjugating enzymes and one enzyme with unknown function?…”

Section: Discussionmentioning

confidence: 54%

“…A study of the evolutionary history of the GH3 family in rosids has indicated that grapevine is a basal rosid whose ancestor had nine GH3 genes (Okrent and Wildermuth, 2011). It was suggested that one of these genes has been lost during evolution to leave grapevine with the eight genes that the authors identified from the genomic sequence.…”

Section: Discussionmentioning

confidence: 99%

“…They are members of the ANL superfamily of adenylating enzymes, which are characterized by the employment of an adenylated reaction intermediate to attach organic acids to a variety of substrates (reviewed in Gulick, 2009;Schmelz and Naismith, 2009). The importance of GH3 proteins in plant development is indicated by the presence of families of these proteins throughout the plant kingdom, from mosses to flowering plants (Okrent and Wildermuth, 2011).…”

Section: Introductionmentioning

confidence: 99%

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Crystal Structure of an Indole-3-Acetic Acid Amido Synthetase from Grapevine Involved in Auxin Homeostasis

et al. 2012

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Auxins are important for plant growth and development, including the control of fruit ripening. Conjugation to amino acids by indole-3-acetic acid (IAA)-amido synthetases is an important part of auxin homeostasis. The structure of the auxinconjugating Gretchen Hagen3-1 (GH3-1) enzyme from grapevine (Vitis vinifera), in complex with an inhibitor (adenosine-59-[2-(1H-indol-3-yl)ethyl]phosphate), is presented. Comparison with a previously published benzoate-conjugating enzyme from Arabidopsis thaliana indicates that grapevine GH3-1 has a highly similar domain structure and also undergoes a large conformational change during catalysis. Mutational analyses and structural comparisons with other proteins have identified residues likely to be involved in acyl group, amino acid, and ATP substrate binding. Vv GH3-1 is a monomer in solution and requires magnesium ions solely for the adenlyation reaction. Modeling of IAA and two synthetic auxins, benzothiazole-2-oxyacetic acid (BTOA) and 1-naphthaleneacetic acid (NAA), into the active site indicates that NAA and BTOA are likely to be poor substrates for this enzyme, confirming previous enzyme kinetic studies. This suggests a reason for the increased effectiveness of NAA and BTOA as auxins in planta and provides a tool for designing new and effective auxins.

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Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Crystal Structure of an Indole-3-Acetic Acid Amido Synthetase from Grapevine Involved in Auxin Homeostasis

et al. 2012

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“…This diverse group of enzymes catalyzes the addition of AMP to carboxyl groups on a wide variety of substrates and typically contains three conserved motifs that form a binding pocket for ATP and AMP substrate intermediates (11). GH3 proteins regulate the activity of plant hormones through amino acid conjugation and have a substantial effect on plant metabolism and physiology (12). For example, FIN219 catalyzes the conjugation of isoleucine (Ile) to JA, forming jasmonoyl-isoleucine (JA-Ile).…”

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confidence: 99%

Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Chen

Kuo

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Far-red (FR) light-coupled jasmonate (JA) signaling is necessary for plant defense and development. FR insensitive 219 (FIN219) is a member of the Gretchen Hagen 3 (GH3) family of proteins in Arabidopsis and belongs to the adenylate-forming family of enzymes. It directly controls biosynthesis of jasmonoyl-isoleucine in JA-mediated defense responses and interacts with FIN219-interacting protein 1 (FIP1) under FR light conditions. FIN219 and FIP1 are involved in FR light signaling and are regulators of the interplay between light and JA signaling. However, how their interactions affect plant physiological functions remains unclear. Here, we demonstrate the crystal structures of FIN219-FIP1 while binding with substrates at atomic resolution. Our results show an unexpected FIN219 conformation and demonstrate various differences between this protein and other members of the GH3 family. We show that the rotated C-terminal domain of FIN219 alters ATP binding and the core structure of the active site. We further demonstrate that this unique FIN219-FIP1 structure is crucial for increasing FIN219 activity and determines the priority of substrate binding. We suggest that the increased FIN219 activity resulting from the complex form, a conformation for domain switching, allows FIN219 to switch to its high-affinity mode and thereby enhances JA signaling under continuous FR light conditions. jasmonate response | far-red light | signaling cross-talk | adenylation enzyme | phytohormone F ar-red (FR) insensitive 219 (FIN219) (1), also known as jasmonate (JA) resistant 1 (JAR1; AtGH3.11) (2), is a member of the auxin-regulated Gretchen Hagen 3 (GH3) family of proteins (3). The GH3 family in Arabidopsis is composed of 19 distinct proteins and is also conserved in plants such as rice (4-6), tomato (7,8), and maize (9), with 13, 15, and 13 members, respectively. Phylogenetically, the GH3 family is classified as part of the adenylate-forming enzyme superfamily, which contains proteins such as firefly luciferase-like enzymes (10). This diverse group of enzymes catalyzes the addition of AMP to carboxyl groups on a wide variety of substrates and typically contains three conserved motifs that form a binding pocket for ATP and AMP substrate intermediates (11). GH3 proteins regulate the activity of plant hormones through amino acid conjugation and have a substantial effect on plant metabolism and physiology (12). For example, FIN219 catalyzes the conjugation of isoleucine (Ile) to JA, forming jasmonoyl-isoleucine (JA-Ile). This reaction results in the degradation of the transcriptional repressor JA-ZIM (zinc-finger protein expressed in inflorescence meristem) domain (JAZ) proteins and the subsequent activation of downstream transcriptional responses (13).FIN219 has been identified in suppressor screenings using a temperature sensitive constitutive photomorphogenic 1 (cop1) mutant line. It is involved in FR light-mediated inhibition of hypocotyl elongation and regulates light inactivation of COP1 activity (1). Furthermore, FIN219 acts as a ...

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“…In the second transfer step, the amine group of an amino acid nucleophilically displaces AMP, yielding the conjugated acyl acid [10]. GH3 proteins regulate the levels of phytohormones, including JA and IAA [11]. Group I GH3 genes catalyze additional amino acids to phytohormone JA-Ile and Group II GH3 genes catalyze additional amino acids to phytohormone IAA.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary History of the GH3 Family Based on 48 Sequenced Plants and Identification of Jasmonic Acid-Relate GH3 Genes in <em>Solanum tuberosum</em>

Zhang¹,

Zhang²,

Wang³

et al. 2018

Preprint

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Glycoside Hydrolase 3 (GH3) is a phytohormone-responsive family of genes that has been found in many plant species. It is implicated in the biological activity of indolacetic (IAA) and jasmonic acids (JA), and also affects plant growth and developmental processes and some stresses. In this study, GH3 genes were identified in 48 plants, which belong to algae, moss, fern, gymnosperm and angiosperm. No GH3 representative gene has been found in algae, and our research identified 4 genes in mosses, 19 in ferns, 7 in gymnosperms, and numerous in Angiosperms. The results showed that GH3 genes mainly occur in seed plants. Phylogenetic analysis of all GH3 genes showed three separate clades. Group I was related to JA adenylation, group II was related to IAA adenylation, and group III was separated from group II but the function was not clear. The structure of GH3 protein indicated highly conserved sequence in the plant kingdom. The analysis of JA-adenylation related to gene expression of GH3 in potato (Solanum tuberosum) showed that StGH3.12 highly responded to Methyl Jasmonate (MeJA) treatment. Expression levels of StGH3. 1, StGH3.11, and StGH3.12 were high in flower and StGH3.11 expression was also high in stolon. Our research revealed the evolution of the GH3 family, which is useful for studying the precise function about JA-adenylation GH3 genes in S. tuberosum under development and biotic stresses.

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Evolutionary history of the GH3 family of acyl adenylases in rosids

Cited by 68 publications

References 80 publications

Crystal Structure of an Indole-3-Acetic Acid Amido Synthetase from Grapevine Involved in Auxin Homeostasis

Crystal Structure of an Indole-3-Acetic Acid Amido Synthetase from Grapevine Involved in Auxin Homeostasis

Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation

Evolutionary History of the GH3 Family Based on 48 Sequenced Plants and Identification of Jasmonic Acid-Relate GH3 Genes in <em>Solanum tuberosum</em>

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