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.
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.
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.
Whole genome duplication in Brassica rapa is accompanied by both expansion of the circadian transcriptome and widespread temporal reconfiguration of gene regulatory networks consistent with subfunctionalization among pairs of paralogs.
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.
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.
First two transmembrane segments of Tim17 are involved in interaction with the channel and the second two with the motor of the presequence translocase suggesting how proteins are handed over during their translocation into mitochondria.
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.
Genetic and biochemical analysis reveal a variant in HSF2BP causing POI and C19ORF57/BRME1 as an interactor and stabilizer of HSF2BP by forming a complex with BRCA2, RAD51, RPA and PALB2.
