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Arabidopsis thaliana plants possess a specific farnesylcysteine lyase that is involved in detoxification and recycling of farnesylcysteine
Author(s) -
Crowell Dring N.,
Huizinga David H.,
Deem Angela K.,
Trobaugh Corey,
Denton Ryan,
Sen Stephanie E.
Publication year - 2007
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2007.03091.x
Subject(s) - arabidopsis , biology , arabidopsis thaliana , mutant , gene , meristem , microbiology and biotechnology , biochemistry , lyase , signal transduction , enzyme
Summary In plants, prenylated proteins are involved in actin organization, calcium‐mediated signal transduction, and many other biological processes. Arabidopsis thaliana mutants lacking functional protein prenyltransferase genes have also revealed roles for prenylated proteins in phytohormone signaling and meristem development. However, to date, the turnover of prenylated plant proteins and the fate of the prenylcysteine (PC) residue have not been described. We have detected an enzyme activity in Arabidopsis plants that metabolizes farnesylcysteine (FC) to farnesal, which is subsequently reduced to farnesol. Unlike its mammalian ortholog, Arabidopsis FC lyase exhibits specificity for FC over geranylgeranylcysteine (GGC), and recognizes N ‐acetyl‐FC (AFC). FC lyase is encoded by a gene on chromosome 5 of the Arabidopsis genome ( FCLY , At5g63910) and is ubiquitously expressed in Arabidopsis tissues and organs. Furthermore, T‐DNA insertions into the FCLY gene cause significant decreases in FC lyase activity and an enhanced response to abscisic acid (ABA) in seed germination assays. The effects of FCLY mutations on ABA sensitivity are even greater in the presence of exogenous FC. These data suggest that plants possess a specific FC detoxification and recycling pathway.