Activity of the mammalian DNA transposon piggyBat from Myotis lucifugus is restricted by its own transposon ends.

Members of the piggyBac superfamily of DNA transposons are widely distributed in host genomes ranging from insects to mammals. The human genome has retained five piggyBac-derived genes as domesticated elements although they are no longer mobile. Here, we have investigated the transposition properties of piggyBat from Myotis lucifugus, the only known active mammalian DNA transposon, and show that its low activity in human cells is due to subterminal inhibitory DNA sequences.

Potential of root acid phosphatase activity to reduce phosphorus fertilization in maize cultivated in Brazil.

It is urgent to mitigate the environmental impacts resulting from agriculture, especially in highly biodiverse and threatened areas, as the Brazilian Cerrado. We aim to investigate whether root acid phosphatase activity is alternative plant strategies for nutrient acquisition in maize genotypes cultivated under fertilized and unfertilized conditions in Brazil, potentially contributing to reducing the use of phosphate fertilizers needed for production. Three experiments were performed: the first was conducted in a glasshouse, with 17 experimental maize inbred lines and two phosphorus (P) treatments; the second in the field, with three maize inbred lines and two treatments, one without fertilization and another with NPK fertilization; and the third was also carried out in the field, with 13 commercial hybrids, grown either under NK or under NPK treatment.

Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.

The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all.