dictyNews
Electronic Edition
Volume 30, number 1
January 4, 2008

Please submit abstracts of your papers as soon as they have been
accepted for publication by sending them to dicty@northwestern.edu
or by using the form at
http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit.

Back issues of dictyNews, the Dicty Reference database and other
useful information is available at dictyBase - http://dictybase.org.


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Abstracts
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Cytokinins induce sporulation in Dictyostelium

Christophe Anjard and William F. Loomis*

Center for Molecular Genetics, Division of Biological Sciences,
University of California San Diego, La Jolla, CA 92093-0368


Development, in press

The social amoeba Dictyostelium discoideum diverged from the line leading 
to animals shortly after the separation of plants and animals but retained 
characteristics of both kingdoms. A GABAB-like receptor and a peptide, 
SDF-2, with homologs found only in animals, control sporulation, while 
cytokinins, which act as hormones in plants, keep spores dormant.  When 
SDF-2 binds its receptor, DhkA, it reduces the activity of the cAMP 
phosphodiesterase RegA such that  cAMP can increase. It has been proposed 
that the cytokinin, discadenine, also results in an increase in cAMP but 
acts through a different histidine kinase, DhkB. We have found that 
discadenine and its precursor, isopentenyl adenine, not only maintain 
spore dormancy but also initiate rapid encapsulation independently of the 
SDF-2 signal transduction pathway. DhkB and the adenylyl cyclase of late 
development, AcrA, are members of two component signal transduction 
families and both are required to transduce the cytokinin signal.  As 
expected, strains lacking the isopentenyl-transferase enzyme chiefly 
responsible for cytokinin synthesis are defective in sporulation. It 
appears that SDF-2 and cytokinins are secreted during late development to 
trigger signal transduction pathways that lead to an increase in the 
activity of the cAMP dependent protein kinase, PKA, which triggers rapid 
encapsulation as well as ensures spore dormancy.


Submitted by: Bill Loomis [wloomis@ucsd.edu]
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GBF-dependent family genes morphologically suppress the partially active 
Dictyostelium STATa strain

Nao Shimada, Naoko Kanno-Tanabe, Kakeru Minemura and Takefumi Kawata*

Department of Biology, Faculty of Science, Toho University, 2-2-1 
Miyama, Funabashi, Chiba 274-8510, Japan 
 
*Corresponding author 


Dev. Genes & Evol., In press

Transcription factor Dd-STATa, a functional Dictyostelium homologue of 
metazoan Signal Transducers and Activators of Transcription (STAT) proteins, 
is necessary for culmination during development. We have isolated more than 
18 putative multicopy suppressors of Dd-STATa using genetic screening. 
One was hssA gene, whose expression is known to be G-box binding factor 
(GBF)-dependent and which was specific to prestalk A (pst A) cells, where 
Dd-STATa is activated. Also, hssA mRNA was expressed in pstA cells in the 
Dd-STATa-null mutant. At least 40 hssA-related genes are present in the 
genome and constitute a multigene family. The tagged HssA protein was 
translated; hssA encodes an unusually high-glycine/serine-rich small 
protein (8.37 kDa), which has strong homology to previously reported 
cAMP-inducible 2C and 7E proteins. Overexpression of hssA mRNA as well 
as frame-shifted versions of hssA RNA suppressed the phenotype of the 
partially active Dd-STATa strain, suggesting that translation is not 
necessary for suppression. Although overexpression of prespore-specific 
genes among the family did not suppress the parental phenotype, 
prestalk-specific family members did. Although overexpression of the 
hssA did not revert the expression of Dd-STATa target genes, and 
although its suppression mechanism remains unknown, morphological 
reversion implies functional relationships between Dd-STATa and hssA. 


Submitted by: Takefumi Kawata [tkawata@bio.sci.toho-u.ac.jp]
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[End dictyNews, volume 30, number 1]