The core of the motor domain determines the direction of myosin movement

Myosins constitute a superfamily of at least 18 known classes of molecular motors that move along actin filaments. Myosins move towards the plus end of F-actin filaments; however, it was shown recently that a certain class of myosin, class VI myosin, moves towards the opposite end of F-actin, that is, in the minus direction. As there is a large, unique insertion in the myosin VI head domain between the motor domain and the light-chain-binding domain (the lever arm), it was thought that this insertion alters the angle of the lever-arm switch movement, thereby changing the direction of motility. Here we determine the direction of motility of chimaeric myosins that comprise the motor domain and the lever-arm domain (containing an insert) from myosins that have movement in the opposite direction. The results show that the motor core domain, but neither the large insert nor the converter domain, determines the direction of myosin motility.     

Understanding and tuning the epitaxy of large aromatic adsorbates by molecular design

If the rich functionality of organic molecules is to be exploited in devices such as light-emitting diodes or field-effect transistors, interface properties of organic materials with various (metallic and insulating) substrates must be tailored carefully. In many cases, this calls for well-ordered interfaces. Organic epitaxy-that is, the growth of molecular films with a commensurate structural relationship to their crystalline substrates--relies on successful recognition of preferred epitaxial sites. For some large pi-conjugated molecules ('molecular platelets') this works surprisingly well, even if the substrate exhibits no template structure into which the molecules can lock. Here we present an explanation for site recognition in non-templated organic epitaxy, and thus resolve a long-standing puzzle. We propose that this form of site recognition relies on the existence of a local molecular reaction centre in the extended pi-electron system of the molecule. Its activity can be controlled by appropriate side groups and--in a certain regime--may also be probed by molecularly sensitized scanning tunnelling microscopy. Our results open the possibility of engineering epitaxial interfaces, as well as other interfacial nanostructures for which specific site recognition is essential.     

The microRNA-producing enzyme Dicer1 is essential for zebrafish development

MicroRNAs (miRNAs) are produced by the Dicer1 enzyme; the role of Dicer1 in vertebrate development is unknown. Here we report target-selected inactivation of the dicer1 gene in zebrafish. We observed an initial build-up of miRNA levels, produced by maternal Dicer1, in homozygous dicer1 mutants, but miRNA accumulation stopped after a few days. This resulted in developmental arrest around day 10. These results indicate that miRNA-producing Dicer1 is essential for vertebrate development.