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Over 20 % of bacterial genes are regulated by structurally distinct, nucleic acid-containing riboswitches. These regulatory RNAs recruit cellular translation machinery to control the transcription and/or translation of their target mRNAs. Few, if any, have been characterized outside of their host organism. In addition, we still have much to learn about the regulatory complexity of their target mRNAs. Here, we report the characterization of a torsion riboswitch in Bacillus subtilis. This torsion riboswitch harbors an mRNA whose translation is suppressed by a fully base-paired, hairpin-forming, RNA structure. This mRNA contains a 3′ UTR which encodes the torsional state of the riboswitch. When base-pairing in the hairpin is disrupted, the mRNA is translated at higher rates. Through RNA secondary structure prediction and mutagenesis, we have determined the domains necessary and sufficient for torsion-dependent regulation.Project Summary/Abstract TGF-? signaling is a key developmental regulator with important roles in cell proliferation, differentiation and motility. TGF-? signaling directs specification of cell fate by controlling proteome remodeling, which is maintained by differential ubiquitin regulation of key transcription factors. The ubiquitin specific protease-4 (USP4) deubiquitinates a number of important proteins such as p53, Lrp6, Smad3 and Smad4, and regulates TGF-? signaling and cell fate specification. However, molecular mechanisms regulating TGF-? signaling output by USP4 remain ill-defined and the impact of drug-induced modulation of USP4 expression in tumor cells is unknown. Our studies indicate that USP4 is required for cellular migration, in part by regulation of key proteins involved in contractility, such as p130Cas, IQGAP1 and Pp1. We demonstrate that inhibition of USP4 blocks production of the contractile protein?-act

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