16.11.2013 Views

Book of Abstracts - Geyseco

Book of Abstracts - Geyseco

Book of Abstracts - Geyseco

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

P - Posters<br />

ponsible for the synthesis <strong>of</strong> the mesophyll isoenzyme, and its<br />

expression is up-regulated by light.<br />

b) ABA decreases the rate <strong>of</strong> PEPC-k degradation 3 . The rise in<br />

ABA level, as a consequence <strong>of</strong> salinity, might account for a<br />

lower rate <strong>of</strong> PEPC-k degradation.<br />

We have used LiCl, which decreases the degradation <strong>of</strong> PEPC-k 4 ,<br />

as a tool to investigate the molecular mechanisms controlling this<br />

process. PEPC-k has been has been proposed to be ubiquitinated<br />

and catabolised by the proteasome 5 . In this respect, the ubiquitination<br />

<strong>of</strong> 1-aminocyclopropane-1-carboxylate synthase (ACS)<br />

is regulated by phosphorylation by a calcium-dependent protein<br />

kinase (CDPK) 6 . The treatment with 10 mM LiCl <strong>of</strong> sorghum<br />

leaves causes a marked rise <strong>of</strong> a CDPK activity while decreasing<br />

the rate <strong>of</strong> PEPC-k disappearance. This late effect was lost in<br />

the presence <strong>of</strong> W7, an inhibitor <strong>of</strong> CDPK activity. These preliminary<br />

results suggest that the phosphorylation <strong>of</strong> PEPC-k by a<br />

CDPK could be regulating the degradation <strong>of</strong> the first.<br />

1.- Echevarría et al (2001) Planta, 214, 283-287.<br />

2.- García-Mauriño et al (2003). Planta, 216, 648-655.<br />

3.- Monreal et al (2007a). FEBS Lett., 581, 3468-3472.<br />

4.- Monreal et al (2007b). Planta, 225, 801-812.<br />

5.- Agetsuma et al (2005). Plant Cell Physiol, 46, 389-398<br />

6.- Tatsuki and Mori (2001). J Biol Chem, 276, 28051-28057.<br />

P01-027: INFLUENCES OF HIGH TEMPERATURE DU-<br />

RING GRAIN FILLING STAGE ON ACCUMULATION<br />

OF STORAGE PROTEINS AND GRAIN QUALITY IN<br />

RICE (ORYZA SATIVA L.)<br />

Lur, H. 1 * - Lin, SK. 2 - Liu, YH. 1 - Lin, CJ. 1<br />

1<br />

Department <strong>of</strong> Agronomy, National Taiwan University<br />

2<br />

Sustainable Environment Research Center, Natl. Cheng-Kung<br />

University<br />

*Corresponding author, e-mail: lurhs@ntu.edu.tw<br />

High temperature (HT) can reduce the grain yield and quality <strong>of</strong><br />

rice. Storage proteins are important for both the development and<br />

quality <strong>of</strong> rice grains, but effect <strong>of</strong> the HT on the accumulation<br />

<strong>of</strong> storage proteins is unclear. Our study was to understand the<br />

effects <strong>of</strong> HT during filling stage on the expression <strong>of</strong> storage<br />

proteins and the quality <strong>of</strong> rice grains. Storage proteins were<br />

analyzed by 1D SDS-PAGE, and differential expressed gel bands<br />

were further identified by LC\MS\MS. Transcriptions <strong>of</strong> the genes<br />

for key proteins were also determined. Results showed that<br />

HT reduced the wight, amylose content, and flour gel consistency<br />

<strong>of</strong> grains. HT increased accumulation <strong>of</strong> storage proteins at early<br />

filling stage, but decreased the accumulation <strong>of</strong> prolamines and<br />

globulins at maturation. Among storage proteins prolamins and<br />

globulins were most sensitive to HT. Proteins <strong>of</strong> cyclophilin 2,<br />

peroxireducxin, glyoxalase I, RAB24 and HSP16.9 were differentially<br />

enhanced by HT. At transcription level, HT enhanced<br />

the expressions <strong>of</strong> genes for glutelin, prolamins, globulins, and<br />

protein disulfide isomerase at early filling stage; but decreased<br />

that <strong>of</strong> these genes at later stage. HT also decreased the expressions<br />

<strong>of</strong> starch biosynthesis related genes GBSS and SSIIa, and<br />

HT increased the expression <strong>of</strong> stress responsive genes PRDX,<br />

RAB24, HSP16.9c, and GloI. A schematic model is proposed to<br />

depict the influence <strong>of</strong> HT on grain quality formation in rice.<br />

P01-028: THE IMPACT OF PROLINE ON POLYAMINE<br />

METABOLISM DURING HEAT STRESS RESPONSE IN<br />

TOBACCO PLANTS<br />

Martincova, O.*<br />

Institute <strong>of</strong> Experimental Botany v.v.i., AS CR, Rozvojová<br />

*Corresponding author, e-mail: martincovao@ueb.cas.cz<br />

Heat stress represents very fast, acute stress associated (at least<br />

at the initial phase) with the decrease <strong>of</strong> leaf water potential. Defense<br />

pathways include synthesis <strong>of</strong> osmolytes and production<br />

<strong>of</strong> other key protective compounds (polyamines, PAs). PA involvement<br />

in abiotic stress adaptation could be due to their roles in<br />

osmotic adjustment, membrane stability and free-radical scavenging.<br />

Responses to heat were compared in tobacco plants constitutively<br />

over-expressing a modified gene for the proline biosynthetic<br />

enzyme ∆1-pyrroline-5-carboxylate synthetase (TR) and in<br />

the corresponding wild-type (WT).<br />

Initial phase <strong>of</strong> heat stress (2 h at 40 °C) was associated with<br />

an increase in free PAs (more expressive in TR), especially <strong>of</strong><br />

spermidine and spermine in WT plants and in addition putrescine<br />

(Put) in TR. The rise in PA contents correlated with a stimulation<br />

<strong>of</strong> the activity <strong>of</strong> arginine, ornithine and S-adenosylmethionine<br />

decarboxylases. Decrease in free PAs, especially <strong>of</strong> Put, coincided<br />

with down-regulation <strong>of</strong> the activity <strong>of</strong> PA biosynthetic enzymes<br />

after 6 h <strong>of</strong> heat stress. The use <strong>of</strong> plants with elevated proline<br />

content enabled us to evaluate the effect <strong>of</strong> enhanced stress<br />

tolerance on the dynamics <strong>of</strong> PA levels during the heat stress.<br />

This work was supported by Ministry <strong>of</strong> Education CR project<br />

No. OC 08013.<br />

P01-029: PHYTOTOXICITY OF NANOSIZED MOLYBDE-<br />

NUM OCTAHEDRAL CLUSTERS<br />

Cabello-Hurtado, F.* - Aubert, T. - Esnault, MA. - Cordier, S.-<br />

Grasset, F.<br />

University <strong>of</strong> Rennes<br />

*Corresponding author, e-mail: francisco.cabello-hurtado@<br />

univ-rennes1.fr<br />

Manufactured nanoparticles (

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!