Book of Abstracts - Geyseco
Book of Abstracts - Geyseco
Book of Abstracts - Geyseco
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03 - S - Selected <strong>Abstracts</strong> for Oral Presentations<br />
An increase in DNA methylation was found at later stages <strong>of</strong><br />
pollen embryogenesis, accompanying differentiation. BnMET-1<br />
expression was developmentally regulated in both pollen pathways,<br />
being upregulated during pollen maturation and tapetum<br />
PCD, and downregulated with the switch to embryogenesis. This<br />
report showed new evidences <strong>of</strong> changes in DNA methylation<br />
that accompany the reorganization <strong>of</strong> the nuclear architecture<br />
during plant cell differentiation, proliferation and PCD, giving<br />
new insights in the knowledge <strong>of</strong> the epigenetic control <strong>of</strong> plant<br />
development.<br />
Work supported by MICINN projects BFU2008-00203 and<br />
AGL2008-04255.<br />
.<br />
S13-001: TREHALOSE METABOLISM AND SUGAR SIG-<br />
NALLING IN PLANTS<br />
Lunn, J.* - Feil, R. - Yadav, U. P. - Martins, M. - Ivakov, A. -<br />
Krause, U. - Wahl, V. - Stitt, M.<br />
Max-Planck-Institute <strong>of</strong> Molecular Plant Physiology<br />
*Corresponding author e-mail: lunn@mpimp-golm.mpg.de<br />
Trehalose is a disaccharide sugar that is commonly found in bacteria,<br />
fungi and insects, where it can function as a compatible solute,<br />
storage reserve, transport sugar or stress protectant. Trehalose<br />
was once thought to be rare in higher plants, but genomic and<br />
other sequence data revealed that the capacity to synthesise trehalose<br />
is present throughout the plant kingdom.<br />
Mutants and transgenic plants with altered trehalose metabolism<br />
show pronounced morphological phenotypes, which are linked<br />
to changes in the level <strong>of</strong> trehalose 6-phosphate (Tre6P), the intermediate<br />
<strong>of</strong> trehalose synthesis, rather than to trehalose itself.<br />
Using a new mass spectrometry-based assay, we found that the<br />
amount <strong>of</strong> Tre6P in plant tissues reflects changes in the level <strong>of</strong><br />
sugars, particularly sucrose, leading us to propose that Tre6P<br />
acts as a signal <strong>of</strong> sucrose status [Lunn et al. (2006) Biochem. J.<br />
397; 139–148]. We are now investigating both the upstream and<br />
downstream pathways <strong>of</strong> Tre6P signalling in plants.<br />
Inhibitor studies showed that protein synthesis is required for the<br />
response <strong>of</strong> Tre6P to changes in sucrose content, and that phosphorylation<br />
and turnover <strong>of</strong> proteins could also be involved. Inducible<br />
over-expression <strong>of</strong> trehalose-phosphate synthase in Arabidopsis<br />
thaliana showed that night-time degradation <strong>of</strong> starch in<br />
leaves is sensitive to increased levels <strong>of</strong> Tre6P.<br />
This indicates that Tre6P could form part <strong>of</strong> a feedback loop linking<br />
starch turnover in the leaves to demand for sucrose from<br />
sink organs. We are also testing the hypothesis that Tre6P acts as<br />
a signal <strong>of</strong> sucrose status in meristems and organ primordia, thus<br />
tying the growth and development <strong>of</strong> the plant to the availability<br />
<strong>of</strong> sucrose from the leaves.<br />
S13-002: DOWNREGULATING SUBERIN BIOSYNTHE-<br />
TIC ENZYMES TO BETTER UNDERSTAND SUBERIN<br />
STRUCTURE AND PERIDERM PHYSIOLOGY.<br />
Serra, O.* - Soler, M. - Molinas, M. - Figueras, M.<br />
University <strong>of</strong> Girona<br />
*Corresponding author e-mail: olga.serra@udg.edu<br />
Periderm develops to protect mature stems, roots and tubers from<br />
dehydration and pathogens. It is composed <strong>of</strong> phellem or cork<br />
layer at the external side, phellogen or mother layer and phelloderm.<br />
The phellem cell walls are impermeable to water due to<br />
the deposition <strong>of</strong> suberin, a complex polymer made <strong>of</strong> an aliphatic<br />
domain linked to an aromatic domain. The aliphatic suberin<br />
is a polyester <strong>of</strong> fatty acids and derivatives (C16-C30), glycerol<br />
and ferulic acid. Although the chemical composition <strong>of</strong> suberin<br />
is widely known, the synthesis and polymerization <strong>of</strong> its aliphatic<br />
monomers and their contribution to the barrier function is poorly<br />
understood.<br />
To shed light in this subject, we constructed a phellem SSH library<br />
that yielded a list <strong>of</strong> suberin candidate genes (1) and developed<br />
a strategy to analyze their role using a reverse genetic<br />
approach. Three genes encoding key enzymes for aliphatic suberin<br />
biosynthesis have been characterized: a fatty ω-hydroxylase<br />
(P450) (2), a fatty acid elongase (3) and a BAHD acyl transferase<br />
(4). For each gene, the composition, ultrastructure and water permeability<br />
<strong>of</strong> tuber periderm has been analyzed in downregulated<br />
potato plants. Altogether, the results reveal the importance <strong>of</strong> suberin<br />
composition in the ultrastucture and physiological function<br />
<strong>of</strong> periderm.<br />
(1) P Phys 2007, 144:419;<br />
(2) P. Phys.2009, 149:1050;<br />
(3) J Exp Bot 2009) 60:697;<br />
(4) Plant J 2010, doi: 10.1111/j.1365-313X.2010.04144.x.<br />
S13-003: THE KEY ROLE OF FATTY ACID DESATURA-<br />
TION IN THE RESPONSE TO ENVIRONMENTAL FAC-<br />
TORS AND IN THE AROMA BIOGENESIS OF OLIVE<br />
AND TOMATO FRUITS<br />
Hernandez, L.¹* - Padilla, M.¹ - Domínguez, T.² - Sanmartin, M.²<br />
- Sanchez Serrano, J. J. ² - Sanz, C.¹ - Martinez-Rivas, J.M .¹<br />
¹Instituto de la Grasa (CSIC)<br />
²Centro Nacional de Biotecnologia (CSIC)<br />
*Corresponding author e-mail: mlhdez@cica.es<br />
The lipoxygenase (LOX) pathway is responsible for the biosynthesis<br />
<strong>of</strong> oxylipins and its involvement in different plant physiological<br />
processes such as stress resistance and aroma biogenesis<br />
has been long demonstrated.<br />
The first step <strong>of</strong> this pathway is catalyzed by LOXs enzymes that<br />
produce a fatty acid hydroperoxide, derived from the corresponding<br />
fatty acid. These hydroperoxides are subsequently metabolised<br />
through a number <strong>of</strong> potentially competing pathways to<br />
generate a wide array <strong>of</strong> oxylipins.<br />
Linoleic and linolenic acid, the main precursors <strong>of</strong> the LOX pathway,<br />
are synthesized from oleic acid by the consecutive action<br />
<strong>of</strong> ω-6 and ω-3 desaturases. In plants, two sets <strong>of</strong> these enzymes<br />
have been reported; one is located in the endoplasmic reticulum<br />
(FAD2 and FAD3) and the other in chloroplastic membranes<br />
(FAD6 and FAD7/8). In this work, we have studied in olive fruit<br />
the effect <strong>of</strong> different environmental stress situations such as low<br />
and high temperature, dark exposure and wounding, on the fatty<br />
acid composition and on the expression levels <strong>of</strong> FAD2, FAD3,<br />
FAD6 and FAD7/8, and LOX genes. The analytical and expression<br />
data indicate that some <strong>of</strong> these genes are coregulated at the<br />
transcriptional level.<br />
On the other hand, we have over-expressed the ω-3 desaturases<br />
FAD3 and FAD7 in tomato. Fruits and leaves <strong>of</strong> transgenic tomato<br />
plants exhibit a modification not only in the fatty acid composition<br />
by increasing the linolenic/linoleic acid ratio, but also<br />
in the aroma pr<strong>of</strong>ile with a significant alteration <strong>of</strong> the (Z)-hex-<br />
3-enal/hexanal ratio. The results obtained from both approaches<br />
point out the involvement <strong>of</strong> fatty acid desaturation in the response<br />
to environmental factors and in the aroma biogenesis <strong>of</strong> fruits.<br />
S13-004: DIGITALIS PURPUREA p5βr2 IS A NEW STE-<br />
ROID 5β- REDUCTASE THAT BELONGS TO THE NO-<br />
VEL SDR75R FAMILY<br />
Tuñón, I. 1 - Ferrer, S.² - Moya García, A.³ - Pérez-Bermúdez, P. 4 -<br />
Tarrío, R. 5 - Rodríguez-Trelles, F. 6 - Gavidia, I. 4 -<br />
1<br />
Dept. Química Física, Univ. Valencia, Burjassot, Spain<br />
²Dept. Química Física I Analítica, Univ. Jaume I, Castellon, Spain<br />
³CIBER de Enfermedades Raras, Dept. Biología Molecular y<br />
Bioquímica, Univ. Málaga. Spain<br />
4<br />
Dept. Biología Vegetal, Univ. Valencia, Burjassot, Spain<br />
5<br />
Grupo de Medicina Xenómica–CIBERER, Univ. Santiago de<br />
Compostela, Spain<br />
6<br />
Dept Genètica i Microbiologia, Univ. Autonòma de Barcelona,<br />
Bellaterra, Spain<br />
S