X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

Cryo-electron microscopy structures show how the clinically used antimicrobial fidaxomicin binds and inhibits Mycobacterium tuberculosis RNA polymerase by acting like a doorstop to jam the enzyme in an open conformation via the general transcription factor RbpA.

Coupled physiology and gene expression, measured over a two-day time course, reveals specific time-of-day responses to the early stages of drought in Brassica rapa.

Biofilm matrix protein RbmA controls biofilm architecture through binary structural switching and exopolysaccharide binding.

hRPA permits the BLM helicase to bidirectionally unwind DNA from a nick which could potentially facilitate its function switching in DNA repair and promote end resection in homologous recombination.

The essential mycobacterial transcription factor RbpA interacts with promoter DNA and cooperates with another essential transcription factor, CarD, to stimulate the formation of an intermediate leading to the open promoter complex.

The influence of time on the drought response of Brassica rapa, an agriculturally important species of plant, has been clarified.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

A structural switch controls the architecture of Vibrio cholerae biofilms by mediating the interactions between two matrix components.

Variability in bacterial transcription start site selection involves DNA “scrunching” and “anti-scrunching,” which may represent a general mechanism for start site selection in all organisms.