Publications

• Characterization of a BAHD acyltransferase responsible for producing the green leaf volatile (Z)-3-hexen-1-yl acetate in Arabidopsis thaliana.

  D'Auria J.C., Pichersky E., Schaub A., Hansel A., Gershenzon J.

  Green-leaf volatiles are commonly emitted from mechanically and herbivore-damaged plants. Derived from the lipoxygenase pathway, these compounds may serve as attractants to predators and parasitoids of herbivores, prevent the spread of bacteria and fungi, and induce several important plant defense ... >> More

  Green-leaf volatiles are commonly emitted from mechanically and herbivore-damaged plants. Derived from the lipoxygenase pathway, these compounds may serve as attractants to predators and parasitoids of herbivores, prevent the spread of bacteria and fungi, and induce several important plant defense pathways. In Arabidopsis thaliana, the major volatile released upon mechanical wounding of the leaves is the GLV ester, (Z)-3-hexen-1-yl acetate. We have characterized a member of the BAHD acyltransferase gene family At3g03480 which catalyzes the formation of (Z)-3-hexen-1-yl acetate from acetyl-CoA and (Z)-3-hexen-1-ol. The encoded acetyl CoA:(Z)-3-hexen-1-ol acetyltransferase (CHAT) has the ability to accept several medium-chain-length aliphatic and benzyl-derived alcohols, but has highest catalytic efficiency with (Z)-3-hexen-1-ol. The highest expression of CHAT occurs in the leaves and stems. Upon mechanical damage, the (Z)-3-hexen-1-yl acetate emission peaked after 5 min and declined to pre-damage levels after 90 min. However, CHAT gene transcript levels increased much more slowly with the highest levels detected between 3 and 6 h after wounding. An increase in CHAT enzyme activity in vitro followed the transcript increase, with levels peaking between 10 and 12 h after wounding. Plants expressing either an RNAi cassette for the CHAT gene or plants harboring a T-DNA insertion in the CHAT coding region had greatly reduced (Z)-3-hexen-1-yl acetate emission, showing that the CHAT enzyme is responsible for the in planta production of this ester. << Less

  Plant J. 49:194-207(2007) [PubMed] [EuropePMC]

• Characterization of an acyltransferase capable of synthesizing benzylbenzoate and other volatile esters in flowers and damaged leaves of Clarkia breweri.

  D'Auria J.C., Chen F., Pichersky E.

  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 ... >> More

  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. << Less

  Plant Physiol. 130:466-476(2002) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.