Publications

• Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis.

  Fitzpatrick A.H., Bhandari J., Crowell D.N.

  Farnesol, which is toxic to plant cells at high concentrations, is sequentially phosphorylated to farnesyl phosphate and farnesyl diphosphate. However, the genes responsible for the sequential phosphorylation of farnesol have not been identified and the physiological role of farnesol phosphorylati ... >> More

  Farnesol, which is toxic to plant cells at high concentrations, is sequentially phosphorylated to farnesyl phosphate and farnesyl diphosphate. However, the genes responsible for the sequential phosphorylation of farnesol have not been identified and the physiological role of farnesol phosphorylation has not been fully elucidated. To address these questions, we confirmed the presence of farnesol kinase activity in Arabidopsis (Arabidopsis thaliana) membranes and identified the corresponding gene (At5g58560, FOLK). Heterologous expression in recombinant yeast cells established farnesol as the preferred substrate of the FOLK-encoded kinase. Moreover, loss-of-function mutations in the FOLK gene abolished farnesol kinase activity, caused an abscisic acid-hypersensitive phenotype and promoted the development of supernumerary carpels under water-stress conditions. In wild-type plants, exogenous abscisic acid repressed FOLK gene expression. These observations demonstrate a role for farnesol kinase in negative regulation of abscisic acid signaling, and provide molecular evidence for a link between farnesol metabolism, abiotic stress signaling and flower development. << Less

  Plant J. 66:1078-1088(2011) [PubMed] [EuropePMC]

  This publication is cited by 4 other entries.

• Identification and characterization of geranylgeraniol kinase and geranylgeranyl phosphate kinase from the Archaebacterium Sulfolobus acidocaldarius.

  Ohnuma S., Watanabe M., Nishino T.

  Geranylgeranyl diphosphate is an important precursor of archaebacterial ether-linked lipids, and it has been thought that all of this compound is "de novo" synthesized by geranylgeranyl diphosphate synthase. We studied the phosphorylation of geranylgeraniol, which seems to be related to the salvag ... >> More

  Geranylgeranyl diphosphate is an important precursor of archaebacterial ether-linked lipids, and it has been thought that all of this compound is "de novo" synthesized by geranylgeranyl diphosphate synthase. We studied the phosphorylation of geranylgeraniol, which seems to be related to the salvage pathway of biosynthesis of archaebacterial ether-linked lipids, in the Archaebacterium Sulfolobus acidocaldarius. Activities of geranylgeraniol kinase and geranylgeranyl phosphate kinase were detected in a cell lysate of S. acidocaldarius. The two enzymes were easily separated by ultracentrifugation. The membrane fraction and the cytosolic fraction contained geranylgeraniol kinase activity and geranylgeranyl phosphate kinase activity, respectively. Geranylgeraniol kinase, which requires divalent cation such as Mg2+, Co2+, and Mn2+ and NTP (ATP, GTP, CTP, UTP), catalyzes monophosphorylation of (all-E)-geranylgeraniol to produce geranylgeranyl phosphate. (all-E)-Farnesol, (all-E)-hexaprenol, and (all-E)-octaprenol were also active substrates, though they were less effective than (all-E)-geranylgeraniol. However, neither geraniol nor (22E,6E,10Z,14Z,18Z,22Z,26Z,++ +30Z,34Z,38Z)-undecaprenol was active. This enzyme is extremely thermostable and its pH optimal is between 6.5 and 8.5. The Michaelis constants for (all-E)-geranylgeraniol and ATP are 27 nM and 650 microM, respectively. << Less

  J Biochem 119:541-547(1996) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.