Título:
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Molecular characterization of the Arginine decarboxylase gene family in rice
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Autor/a:
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Peremartí, Ariadna; Bassie Rene, Ludovic; Zhu, Changfu; Christou, Paul; Capell Capell, Teresa
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Notas:
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Arginine decarboxylase (ADC) is a key
enzyme in plants that converts arginine into putrescine,
an important mediator of abiotic stress tolerance.
Adc genes have been isolated from a number of
dicotyledonous plants but the oat and rice Adc genes
are the only representatives of monocotyledonous
species described thus far. Rice has a small family of
Adc genes, and OsAdc1 expression has been shown to
fluctuate under drought and chilling stress. We
identified and characterized a second rice Adc gene
(OsAdc2) which encodes a 629-amino-acid protein
with a predicted molecular mass of 67 kDa. An
unusual feature of the OsAdc2 gene is the presence
of an intron and a short upstream open reading frame
in the 50-UTR. Sequence comparisons showed that
OsAdc2 is more closely related to the oat Adc gene
than to OsAdc1 or to its dicot homologs, and mRNA
analysis showed that the two rice genes are also
differently regulated. Whereas OsAdc1 is expressed in
leaf, root and stem, OsAdc2 expression is restricted to
stem tissue. Protein expression was investigated with
specific antibodies against ADC1 and ADC2, corroborating
the mRNA data. We discuss the expression
profiles of OsAdc1 and OsAdc2 and potential functions
for the two corresponding proteins.
This work was supported by grants AGL2004-00444 and BIO2007-30738-E from the Ministerio de Ciencia y Tecnologia (MEC, Spain) to T. Capell. A. Peremarti is funded by a MEC FPI fellowship (BES-2005- 8900); L. Bassie is funded by a Juan de la Cierva fellowship; T. Capell is a tenure-track scientist of the Ramo´n y Cajal Programme; P. Christou is an ICREA researcher, all at the UdL. We would like to thank E. Perez for technical assistance |
Materia(s):
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-Arginine decarboxylase -Polyamines -Rice |
Derechos:
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(c) Springer Verlag, 2010
info:eu-repo/semantics/restrictedAccess |
Tipo de documento:
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article publishedVersion |
Editor:
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Springer Verlag
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