POSTERS - BLAST X - University of Utah
POSTERS - BLAST X - University of Utah
POSTERS - BLAST X - University of Utah
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<strong>BLAST</strong> X Mon. Evening Session<br />
A "FOUR COMPONENT" SIGNAL TRANSDUCTION SYSTEM REGULATES<br />
DEVELOPMENTAL PROGRESSION IN MYXOCOCCUS XANTHUS<br />
Sakthimala Jagadeesan, Bongsoo Lee, and Penelope I. Higgs<br />
Department <strong>of</strong> Ecophysiology, Max Planck Institute for Terrestrial Microbiology, D35043<br />
Marburg, Germany<br />
Myxococcus xanthus responds to starvation by entering a multicellular developmental<br />
program in which 10 5 cells first aggregate into mounds and then within these mounds,<br />
differentiate into environmentally resistant spores. Under standard laboratory conditions,<br />
formation <strong>of</strong> spores within the mounds (fruiting bodies) takes approximately 72 hours. We have<br />
previously demonstrated that progression through the developmental program appears to be<br />
regulated by an atypical two component signal (TCS) transduction system consisting <strong>of</strong> four<br />
TCS homologs (RedC, RedD, RedE, and RedF). While RedC appears to be a typical<br />
membrane bound histidine kinase, RedD consists solely <strong>of</strong> two receiver domains. RedE is a<br />
soluble histidine kinase-like protein, and RedF is a single receiver domain response regulator.<br />
Based on a combination <strong>of</strong> genetic and biochemical analyses, we propose a model for how<br />
these four Red proteins function together to regulate progression through the developmental<br />
program. Our data suggests that development is repressed when the RedC histidine kinase<br />
phosphorylates RedF, a single domain response regulator. Developmental repression is<br />
relieved when, in response to an unknown signal(s), RedC is instead induced to phosphorylate<br />
the response regulator RedD. Surprisingly, the phosphoryl group is then transferred from RedD<br />
to the histidine kinase-like protein, RedE. RedE is then likely made accessible to RedF-P,<br />
whereupon it removes RedF’s phosphoryl group. We present the data that supports this model.<br />
Furthermore, we will address how progression through the developmental program is modulated<br />
by the Red system.<br />
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