SRSF1 regulates the alternative splicing of caspase 9 via a novel intronic splicing enhancer affecting the chemotherapeutic sensitivity of non-small cell lung cancer cells.

Increasing evidence points to the functional importance of alternative splice variations in cancer pathophysiology with the alternative pre-mRNA processing of caspase 9 as one example. In this study, we delve into the underlying molecular mechanisms that regulate the alternative splicing of caspase 9. Specifically, the pre-mRNA sequence of caspase 9 was analyzed for RNA cis-elements known to interact with SRSF1, a required enhancer for caspase 9 RNA splicing.

The carboxy terminal domain of Epr, a minor extracellular serine protease, is essential for the swarming motility of Bacillus subtilis 168.

In this study we have investigated the role of Epr, a minor extracellular serine protease, in the swarming motility of Bacillus subtilis 168. We identified that the protease activity of Epr was dispensable for swarming. Since the protease activity of Epr was confined to its N-terminal domain, we hypothesized instead that its C-terminal domain (CTD) could be critical for swarming.

Epr is transcribed from a final sigma(D) promoter and is involved in swarming of Bacillus subtilis.

Epr is a minor extracellular protease secreted by Bacillus subtilis 168. In this study, we show that epr is transcribed by E sigma(D), the RNA polymerase associated with transcription of genes involved in chemotaxis and motility. Disruption of epr abolished swarming of Bacillus subtilis, suggesting its involvement in motility.