In Science this week, an international team led by investigators in France reports on "the transcriptomes of Bacillus subtilis exposed to a wide range of environmental and nutritional conditions that the organism might encounter in nature." The team presents a "global classification of promoters and detailed description of TUs [transcription units]," which it says shows that "a large proportion of the detected antisense RNAs arose from potentially spurious transcription initiation by alternative sigma factors and from imperfect control of transcription termination."
In a paper published online in advance this week, researchers at Purdue University and Sentinext Therapeutics in Penang, Malaysia, report on the crystal structure of human enterovirus 71. The public-private team says that "unlike in other enteroviruses, the 'pocket factor' a small molecule that stabilizes the virus, is partly exposed on the floor of the canyon" in enterovirus 71. "Thus, the structure of antiviral compounds may require a hydrophilic head group designed to interact with residues at the entrance of the pocket," the researchers add.
Over in Science Signaling, a team led by the University of Dundee’s Nick Leslie show that both lipid- and protein-phosphatase activity "are required for PTEN to inhibit cellular invasion and to mediate most of its largest effects on gene expression." Leslie et al. also identify "a tumor-derived PTEN mutant selectively lacking protein phosphatase activity, indicating that in some circumstances the regulation of invasion and not that of AKT can correlate with PTEN-mediated tumor suppression," they write.