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75 Integrating Membrane Transport with Male Gametophyte ... - TAIR

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147 Systemic signal transduction of flowering and protein trafficking of FT<br />

Megumi Takahashi, Eiko Himi, Koji Goto<br />

Research Inst. Bio Scineces, Okayama<br />

Arabidopsis TERMINAL FLOWER 1 (TFL1) and FLOWERING LOCUS T (FT) are homologous proteins, that is<br />

54% of amino residues are conserved in the whole region. However, the developmental role of these proteins are opposite;<br />

while tfl1 mutants show early flowering, ft mutants show late flowering. In addition to the early flowering phenotype,<br />

tfl1 shows terminal flower, suggesting that TFL1 maintains inflorescence meristem (IM) and represses floral meristem<br />

(FM) formation. Since coordinate differentiation of three layers are essential for the floral primordia formation, TFL1<br />

function is supposed to be required in the whole region of IM, but its transcript was localized only inner region of L3<br />

layer of IM. We have revealed non-cell-autonomous function of TFL1 is conferred by its protein trafficking in the shoot<br />

apical meristem (SAM).<br />

We have also found that FT moves among cell layers of IM. The endogenous FT is, however, expressed in the<br />

vascular bundle of leaf apical region, and recent study revealed that FT interacts <strong>with</strong> FD and functions in the SAM.<br />

Taken together, the following scenario can be deduced; after long distance travel from leaves via vascular bundle, FT is<br />

unloaded near the SAM (vascular bundle is undifferentiated in the SAM) and then FT protein moves to spread into the<br />

SAM and interacts <strong>with</strong> FD to activate target genes.<br />

Another recent study suggests that FT RNA moves from the leaf to the SAM. To confirm this, we have developed<br />

grafting system using tobacco. As expected, transgenic tobacco carrying Arabidopsis FT gene showed early flowering,<br />

we used it as a rootstock and wild type scion was grafted. We found the scions acquired early flowering phenotype. Now<br />

we are investigating FT RNA and/or protein are transmitted from rootstock to scion by using modified FT genes.<br />

148 Deletion of core components of the plastid protein import machinery causes differential<br />

arrest of embryo development in Arabidopsis thaliana<br />

Bianca Hust, Michael Gutensohn<br />

Institute of Plant Physiology, Martin-Luther-University Halle-Wittenberg, Germany<br />

Among the genes that have recently been pinpointed to be essential for plant embryo development a large number<br />

encodes plastid proteins suggesting that embryogenesis is linked to plastid localized processes. However, nuclear<br />

encoded plastid proteins are synthesized as precursors in the cytosol and subsequently have to be transported across the<br />

plastid envelopes by a complex import machinery. We supposed that deletion of components of this machinery should<br />

allow a more general assessment of the role of plastids in embryogenesis since it will not only affect single proteins but<br />

instead inhibit the accumulation of most plastid proteins. Therefore we have characterized three Arabidopsis thaliana<br />

mutants lacking core components of the Toc complex, the protein translocase in the outer plastid envelope membrane,<br />

which indeed show embryo lethal phenotypes. Remarkably, embryo development in the atToc<strong>75</strong>-III mutant, lacking the<br />

pore forming component of the translocase, was arrested extremely early at the two-cell stage. In contrast, despite the<br />

complete or almost complete lack of the import receptors Toc34 and Toc159, embryo development in the atToc33/34<br />

and atToc132/159 mutants proceeded slowly and was arrested later at the transition to the globular and the heart stage,<br />

respectively. These data demonstrate a strict dependence of cell division and embryo development on functional plastids<br />

as well as specific functions of plastids at different stages of embryogenesis. In addition, our analyses suggest that not<br />

all components of the translocase are equally essential for plastid protein import in vivo.

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