ich is under the control of CAI-1 in the stationary phase. Nonetheless, it is suggested that V. harveyi needs all three AIs to time the onset and duration of certain AI-regulated processes during different stages of growth. Acknowledgments We are thankful to B. Look and S. Scheu for excellent technical assistance in HAI-1 analysis and phosphorylation experiments. We thank E. Rabener for help with the CAI-1 analysis. Tightly controlled programmed cell death is essential for the development and tissue homeostasis of all animals. Metazoan cells possess an evolutionary conserved 
network of proteins that execute appropriate life or death decisions in response to extrinsic and intrinsic cellular cues. Deregulated apoptosis underlies numerous human disease states including neurodegenerative disorders and cancer. The identification and molecular characterization of the 22177947 critical control points in apoptotic pathways is therefore essential to reveal novel therapeutic avenues to treat a broad array of human pathologies. Gene expression plays a key role in the response of cells to death-inducing stimuli. A growing body of evidence indicates that the levels of numerous death-related genes can be induced during apoptosis. The integration of cellular signals from diverse apoptotic pathways requires the finely balanced expression of proversus anti-apoptotic proteins. Gene expression patterns of proand anti-apoptotic genes, established by the levels of transcription as well as BIX-02189 cost alternative splicing, can dictate the life-or-death decisions of cells. The most intensely studied protein known to control apoptosis by altering gene expression is the p53 tumor suppressor. Current paradigms link the p53 16699066 tumor suppression function to its capacity to induce apoptosis in response to genotoxic stress. The pro-apoptotic activity of p53 depends largely on its function as a transcriptional activator that binds directly to the promoters of pro-apoptotic genes including FDXR, PUMA, Noxa, Bax and p53AIP1. TFIID is a multi-protein complex that plays a pivotal role in the transcription of protein-coding genes in eukaryotes. TFIID is composed of the TATA-binding protein and up to 14 evolutionarily conserved TBP-associated factors . TFIID can play a rate-limiting role in the regulation of transcription through the recognition of the core promoter elements such as the TATA-box, the initiator, and downstream promoter element . The TFIID complex also engages in direct contacts with DNAbinding transcriptional factors to co-activate gene expression. The architecture and integrity of TFIID complexes depends on a network of TAF-TAF interactions that are predominantly mediated by dimerization of TAFs via their interlocking histone fold motifs. Histone-fold pairs within TFIID include TAF6-TAF9, TAF4-TAF12, TAF11-13, TAF8-TAF10 and TAF3TAF10. TAF4 and TAF5 together with the histone fold containing TAF12, TAF9 and TAF6 are defined as core TAFs, since their depletion from Drosophila cells results in overall destabilization of TFIID complexes. The core TFIID subunit TAF6 has been shown to be broadly required for RNA polymerase II transcription in yeast when total poly+ mRNA levels were TAF6d Controls Death Sans p53 monitored. A more recent microarray analysis estimated that approximately 18% of the yeast Pol II transcriptome depends on TAF6. TAF6 has been shown to be essential for viability in yeast, plants, insects and fish. The requirement for TAF6 in all model organisms studied, togethe
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