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Characterization of an Acyltransferase Capable of Synthesizing Benzylbenzoate and Other Volatile Esters in Flowers and Damaged Leaves of Clarkia Breweri1

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Characterization of an Acyltransferase Capable of Synthesizing Benzylbenzoate and Other Volatile Esters in Flowers and Damaged Leaves of Clarkia Breweri1 Characterization of an Acyltransferase Capable of Synthesizing Benzylbenzoate and Other Volatile Esters in Flowers and Damaged Leaves of Clarkia breweri1 John C. D’Auria, Feng Chen, and Eran Pichersky* Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109–1048 A cDNA encoding a protein with 456 amino acids whose sequence shows considerable similarity to plant acyltransferases was identified among 750 Clarkia breweri flower expressed sequence tags. The cDNA was expressed in Escherichia coli, and the protein produced was shown to encode the enzyme benzoyl-coenzyme A (CoA):benzyl alcohol benzoyl transferase (BEBT). BEBT catalyzes the formation of benzylbenzoate, a minor constituent of the C. breweri floral aroma, but it also has activity with a number of other alcohols and acyl CoAs. The BEBT gene is expressed in different parts of the flowers with maximal RNA transcript levels in the stigma, and no expression was observed in the leaves under normal conditions. However, BEBT expression was induced in damaged leaves, reaching a maximum 6 h after damage occurred. We also show here that a closely related tobacco (Nicotiana tabacum) gene previously shown to be induced in leaves after being challenged by phytopathogenic bacteria also has BEBT activity, whereas the most similar protein to BEBT in the Arabidopsis proteome does not use benzoyl CoA as a substrate and instead can use acetyl CoA to catalyze the formation of cis-3-hexen-1-yl acetate, a green-leaf volatile. Floral scents are often rich in volatile esters. In agents to prevent further spread of disease (Hamil- Clarkia breweri ([Gray] Greene; Onagraceae), an an- tonkemp et al., 1992; Croft et al., 1993; Deng et al., nual plant native to California, for example, benzyl- 1993). acetate constitutes 20% to 40% (w/w) of the total We have previously reported the characterization scent output (depending on the particular C. breweri of the enzyme acetyl CoA:benzyl alcohol acetyl trans- line), whereas the two other esters present in its ferase (BEAT), which is responsible for the produc- aroma, benzylbenzoate and methylsalicylate, each tion of the floral volatile benzylacetate in C. breweri contribute about 5% to the total volatile output (Ra- flowers (Dudareva et al., 1998a). The concurrent guso and Pichersky, 1995). characterization of BEAT and several other structur- Many plants also emit volatile esters from leaves ally similar enzymes has led to the recognition of a damaged by herbivores. The most commonly re- novel class of evolutionarily related acyltransferases ported volatile esters in this class are those derived (EC 2.3.1.x) commonly referred to as the BAHD fam- from the octadecanoid fatty acids, such as cis-3- ily of acyltransferases (St-Pierre and De Luca, 2000). hexen-1-yl acetate (Ozawa et al., 2000; Arimura et al., There are approximately 60 BAHD gene family mem- 2001; Mattiacci et al., 2001), and methylsalicylate, bers in the model organism Arabidopsis, although mostly likely derived from the phenylpropanoid to date, the substrates and products of the enzymes pathway (Lee et al., 1995) or the shikimate pathway encoded by these genes have not been determined. (Wildermuth et al., 2001), is also common (Pare and Members of the BAHD family have been identified in Tumlinson, 1996; Van Poecke et al., 2001). Total vola- other plant species through expressed sequence tag tiles (including, but not limited to, esters) emitted (EST) database construction and analyses, and in a from injured leaves have been shown to function as few cases, the biochemical function has been deter- orientation cues for predatory wasps and mites that mined as well. For example, benzoyl-CoA:anthrani- feed upon herbivorous insects (Turlings et al., 1990; late N-benzo-yltransferase (HCBT) from carnation De Moraes et al., 1998). In addition, some of these (Dianthus caryophyllus) is expressed during infection volatiles may serve as antimicrobial or antifungal with Fusarium oxysporum or Phytophthora parasitica and produces several different benzoylated and cou- 1 This work was supported by the National Science Foundation maroylated anthranilide phytoalexin derivatives (grant no. MCB–9974463), by Novartis Agribusiness Biotechnology (Yang et al., 1997). Other BAHD proteins that are also Research, Inc., and by a National Institutes of Health training grant known to be involved in plant defense are TAT and fellowship in genetics to J.C.D. (grant no. 5 T32 GM07544). * Corresponding author; e-mail: [email protected]; fax 734–647– DBAT from Taxus cuspidata, which catalyze the acet- 0884. ylation and benzoylation, respectively, of taxol pre- Article, publication date, and citation information can be found cursors (Walker and Croteau, 2000a, 2000b; Walker et at www.plantphysiol.org/cgi/doi/10.1104/pp.006460. al., 2000), MAT and DAT from Catharanthus roseus, 466 Plant Physiology, September 2002, Vol. 130, pp. 466–476, www.plantphysiol.org © 2002 American Society of Plant Biologists Damage-Inducible Acyltransferases which catalyze the acetylation of precursors of the alkaloid vindoline (Power et al., 1990; St-Pierre et al., 1998; Laflamme et al., 2001), and SALAT, which is involved in morphine biosynthesis (Grothe et al., 2001). BAHD enzymes involved in caffeoylation and malonylation of anthocyanin pigments have also been reported (Fujiwara et al., 1997, 1998; Yonekura- Sakakibara et al., 2000; Suzuki et al., 2001) as well as those involved in volatile production in strawberry (Fragaria spp.) fruit (Aharoni et al., 2000). It should be noted that the enzymes responsible for the synthesis of methyl esters such as methylsalicylate and meth- yljasmonate belong to a different family of enzymes (Ross et al., 1999; Seo et al., 2001). Figure 2. BEBT enzymatic activity in different floral tissues during Here, we report the characterization of the gene the lifespan of the flower. Petal and stigma tissues were collected and enzyme for the biosynthesis of the floral volatile from C. breweri flowers daily starting 2 d before flower opening (d benzylbenzoate in C. breweri. The gene for benzoyl- Ϫ2) and ending on d 4 postanthesis. For each data point, tissues from CoA:benzyl alcohol benzoyl transferase (BEBT) is ex- three different plants were combined for each assay, at least three pressed in flowers, but it is also expressed in leaf independent assays were conducted, and the mean was obtained. F, tissue after damage. The structure of BEBT indicates Petals; f, stigma. pkat, Picomoles of product per second. that it belongs to the BAHD family of acyltrans- ferases, and its wide substrate specificity may allow d 4, at which time BEBT levels were similar to those it to catalyze the formation of other esters as well. in the stigma (Fig. 2). RESULTS Isolation of a cDNA Clone Encoding BEBT Benzylbenzoate-Forming Activity in Flowers We have recently undertaken the sequencing of We have previously shown that flowers of C. brew- approximately 750 EST cDNAs from a C. breweri eri emit benzylbenzoate (Raguso and Pichersky, flower tissue cDNA library. Because the acylation 1995). The emission of this volatile is highest from the reaction performed by BEBT is similar in principle to stigma, with petals contributing most of the rest the acylation reactions performed by BAHD-type en- (Dudareva et al., 1998b). Total floral emission peaks zymes, we searched the database with BAHD-type 36 h postanthesis, with a second minor peak 72 h protein sequences, including C. breweri BEAT and postanthesis. putative BAHD proteins from Arabidopsis, using the To look at the synthesis of benzylbenzoate, we BLAST2 program (Altschul et al., 1990). The search developed an assay (see “Materials and Methods”)to identified one cDNA with homology to BAHD acyl- detect the enzymatic activity of BEBT, the hypothet- transferase sequences. Because this cDNA was in- ical enzyme (Croteau, 1977; Dudareva et al., 1998b) complete on both the 5Ј and 3Ј ends, we performed that would catalyze the formation of benzylbenzoate 5Ј- and 3Ј-RACE experiments to obtain a full-length from benzyl alcohol and benzoyl CoA (Fig. 1). Crude clone. The complete cDNA, which we tentatively extracts of stigma and petal tissues from flowers of designated BEBT, has an open reading frame encod- different ages were assayed. BEBT activity was de- ing a protein with 456 amino acid residues and a tected in both petals and stigma. In the stigma, it was calculated molecular mass of 50.6 kD. Protein se- high already in unopened flowers, and it peaked on quence comparisons indicate that BEBT is most sim- d 1 of anthesis (Fig. 2). On d 2, when the stigma ilar (72% identity) to a protein encoded by the to- becomes receptive, there was a precipitous drop in bacco (Nicotiana tabacum) hypersensitive response BEBT activity of about 3-fold, and activity remained cDNA HSR201 (Czernic et al., 1996) and to two low on d 3 and 4. In petals, BEBT activity was much BAHD-like Arabidopsis proteins (protein ID nos. lower than in stigma but it gradually increased until CAC01898.1 and AAF01587.1) that are 57% and 54% Figure 1. The reaction catalyzed by BEBT. Plant Physiol. Vol. 130, 2002 467 D’Auria et al. identical, respectively (Fig. 3). In addition, proteins the sequencing of the rice genome are also very sim- encoded by a cDNA from cantaloupe (Cucumis melo) ilar to BEBT, being 53% and 63% identical, respec- and a gene from rice (Oryza sativa) identified during tively, to BEBT. The proteins encoded by these genes all share the salient features of the BAHD protein family, most notably the HXXXD motif in the center of the protein believed to be involved in catalysis, and the DFGWG motif of unknown function near the C terminus (St-Pierre and De Luca, 2000). Enzymatic Characterization of C. breweri BEBT Expressed in Escherichia coli To determine whether the isolated C. breweri cDNA indeed encoded an enzyme with BEBT activity, we subcloned the complete open reading frame of BEBT into the expression vector pET11a, transformed E.
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