Molecular Plant Advance Access published online on November 10, 2009
Molecular Plant, doi:10.1093/mp/ssp091
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Farnesylcysteine Lyase is Involved in Negative Regulation of Abscisic Acid Signaling in Arabidopsis
a Department of Biology, Indiana University-Purdue University Indianapolis, 723 West Michigan Street, Indianapolis, IN 46202, USA
b Department of Chemistry, Indiana University-Purdue University Indianapolis, 402 N. Blackford Street, Indianapolis, IN 46202, USA
c Department of Chemistry, The College of New Jersey, 2000 Pennington Road, Ewing, NJ 08628, USA
d Department of Biological Sciences, Idaho State University, 650 Memorial Drive, Pocatello, ID 83209, USA
1 To whom correspondence should be addressed. E-mail crowdrin{at}isu.edu, fax 208-282-4570, tel. 208-282-3171.
The Arabidopsis FCLY gene encodes a specific farnesylcysteine (FC) lyase, which is responsible for the oxidative metabolism of FC to farnesal and cysteine. In addition, fcly mutants with quantitative decreases in FC lyase activity exhibit an enhanced response to ABA. However, the enzymological properties of the FCLY-encoded enzyme and its precise role in ABA signaling remain unclear. Here, we show that recombinant Arabidopsis FC lyase expressed in insect cells exhibits high selectivity for FC as a substrate and requires FAD and molecular oxygen for activity. Arabidopsis FC lyase is also shown to undergo post-translational N-glycosylation. FC, which is a competitive inhibitor of isoprenylcysteine methyltransferase (ICMT), accumulates in fcly mutants. Moreover, the enhanced response of fcly mutants to ABA is reversed by ICMT overexpression. These observations support the hypothesis that the ABA hypersensitive phenotype of fcly plants is the result of FC accumulation and inhibition of ICMT.
Key Words: Hormone biology primary metabolism seed biology stomata membrane proteins Arabidopsis