First published online July 17, 2003; 10.1104/pp.103.022277
Plant Physiology 132:2248-2255 (2003)
© 2003 American Society of Plant Biologists
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES
Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis1
Hakima Achkor,
Maykelis Díaz,
M. Rosario Fernández,
Josep Antoni Biosca,
Xavier Parés and
M. Carmen Martínez*
Departamento de Bioquímica y Biología Molecular, Facultad
de Ciencias, Universidad Autónoma de Barcelona, 08193 Bellaterra,
Barcelona, Spain
The ADH2 gene codes for the Arabidopsis glutathione-dependent
formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde
metabolism in eukaryotes. In the present work, we have investigated the
potential role of FALDH in detoxification of exogenous formaldehyde. We have
generated a yeast (Saccharomyces cerevisiae) mutant strain
(sfa1 ) by in vivo deletion of the SFA1 gene that
codes for the endogenous FALDH. Overexpression of Arabidopsis FALDH in this
mutant confers high resistance to formaldehyde added exogenously, which
demonstrates the functional conservation of the enzyme through evolution and
supports its essential role in formaldehyde metabolism. To investigate the
role of the enzyme in plants, we have generated Arabidopsis transgenic lines
with modified levels of FALDH. Plants overexpressing the enzyme show a 25%
increase in their efficiency to take up exogenous formaldehyde, whereas plants
with reduced levels of FALDH (due to either a cosuppression phenotype or to
the expression of an antisense construct) show a marked slower rate and
reduced ability for formaldehyde detoxification as compared with the wild-type
Arabidopsis. These results show that the capacity to take up and detoxify high
concentrations of formaldehyde is proportionally related to the FALDH activity
in the plant, revealing the essential role of this enzyme in formaldehyde
detoxification.
1 This work was supported by the Dirección General de Enseñanza
Superior (grant nos. PB96–1167 and PB98–0855), by the Comissionat
per a Universitats i Recerca (grant no. 1999SGR 00103), and by the Commission
of the European Union (grant no. BIO4–CT97–2123).
*
Corresponding author; e-mail
carmen.martinez{at}uab.es;
fax 34–93–5811264.
Received February 22, 2003;
returned for revision March 24, 2003;
accepted April 28, 2003.
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