No abstract

Heterostructure based interface engineering has been proved an effective method for finding new superconducting systems and raising superconductivity transition temperature (T C ) 1-7 . In previous work on one unit-cell (UC) thick FeSe films on SrTiO 3 (STO) substrate, a superconducting-like energy gap as large as 20 meV 8 , was revealed by in situ scanning tunneling microscopy/spectroscopy (STM/STS). Angle resolved photoemission spectroscopy (ARPES) further revealed a nearly isotropic gap of above 15 meV, which closes at a temperature of 65 ± 5 K 9-11 . If this transition is indeed the superconducting transition, then the 1-UC FeSe represents the thinnest high T C superconductor discovered so far. However, up to date direct transport measurement of the 1-UC FeSe films has not been reported, mainly because growth of large scale 1-UC FeSe films ischallenging and the 1-UC FeSe films are too thin to survive in atmosphere. In this work, we successfully prepared 1-UC FeSe films on insulating STO substrates with non-superconducting FeTe protection layers. By direct transport and magnetic measurements, we provide definitive evidence for high temperature superconductivity in the 1-UC FeSe films with an onset T C above 40 K and a extremely large critical current density J C ~ 1.7×10 6 A/cm 2 at 2 K. Our work may pave the way to enhancing and tailoring superconductivity by interface engineering.The FeSe films and FeTe protection layer are grown by molecular beam epitaxy (MBE) (see Methods).

SUMMARY Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207-phosphorylation provokes a new conformer of LysRS that inactivates its translational, but activates its transcriptional function. The crystal structure of an MSC sub-complex established that LysRS is held in the MSC by binding to the N-terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap4A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.

New domains were progressively added to cytoplasmic aminoacyl transfer RNA (tRNA) synthetases during evolution. One example is the UNE-S domain, appended to seryl-tRNA synthetase (SerRS) in species that developed closed circulatory systems. Here we show using solution and crystal structure analyses and in vitro and in vivo functional studies that UNE-S harbours a robust nuclear localization signal (NLS) directing SerRS to the nucleus where it attenuates vascular endothelial growth factor A expression. We also show that SerRS mutants previously linked to vasculature abnormalities either deleted the NLS or have the NLS sequestered in an alternative conformation. A structure-based second-site mutation, designed to release the sequestered NLS, restored normal vasculature. Thus, the essential function of SerRS in vascular development depends on UNE-S. These results are the first to show an essential role for a tRNA synthetase-associated appended domain at the organism level, and suggest that acquisition of UNE-S has a role in the establishment of the closed circulatory systems of vertebrates.