Lifshitz transition enabling superconducting dome around a charge-order critical point.

Superconductivity often emerges as a dome around a quantum critical point (QCP) where long-range order is suppressed to zero temperature, mostly in magnetically ordered materials. However, the emergence of superconductivity at charge-order QCPs remains shrouded in mystery, despite its relevance to high-temperature superconductors and other exotic phases of matter. Here, we present resistance measurements proving that a dome of superconductivity surrounds the putative charge-density-wave QCP in pristine samples of titanium diselenide tuned with hydrostatic pressure. In addition, our quantum oscillation measurements combined with electronic structure calculations show that superconductivity sets in precisely when large electron and hole pockets suddenly appear through an abrupt change of the Fermi surface topology, also known as a Lifshitz transition. Combined with the known repulsive interaction, this suggests that unconventional s± superconductivity is mediated by charge-density-wave fluctuations in titanium diselenide. These results highlight the importance of the electronic ground state and charge fluctuations in enabling unconventional superconductivity.

Ubiquitin-based pathway acts inside chloroplasts to regulate photosynthesis.

Photosynthesis is the energetic basis for most life on Earth, and in plants it operates inside double membrane-bound organelles called chloroplasts. The photosynthetic apparatus comprises numerous proteins encoded by the nuclear and organellar genomes. Maintenance of this apparatus requires the action of internal chloroplast proteases, but a role for the nucleocytosolic ubiquitin-proteasome system (UPS) was not expected, owing to the barrier presented by the double-membrane envelope. Here, we show that photosynthesis proteins (including those encoded internally by chloroplast genes) are ubiquitinated and processed via the CHLORAD pathway: They are degraded by the 26S proteasome following CDC48-dependent retrotranslocation to the cytosol. This demonstrates that the reach of the UPS extends to the interior of endosymbiotically derived chloroplasts, where it acts to regulate photosynthesis, arguably the most fundamental process of life.

Harvard delays in reporting fraud.

KIE: A detailed account of the John Darsee fraud case at the Harvard Medical School is presented, describing the nature of Darsee's work at Harvard and his relationships with colleagues and mentors both before and after his confession to fabrication of data. University authorities took little action against Darsee during the six months before NIH questioning of discrepancies in one of Darsee's studies led to public disclosure. Committees at Harvard and NIH will investigate.^ieng

Coping with fraud.

The tardiness of actions by Harvard officials when faced with confessed fraudulent research conducted by John Darsee is contrasted with the more rapid responses by authorities in the cases of William T. Summerlin (Sloan-Kettering) and Vijay Soman (Yale).

Researcher denied future U.S. funds.

KIE: Marc J. Straus, formerly senior investigator on a lung cancer treatment project at Boston University, has been barred from receiving any federal funding until 1986 because of alleged fabrication of drug reponse data. Straus maintains that he was the victim of a conspiracy by some disgruntled employees. This represents the first time that federal "debarment" regulations have been invoked over the misuse of grant monies.^ieng

Ubiquitin-dependent chloroplast-associated protein degradation in plants.

Chloroplasts contain thousands of nucleus-encoded proteins that are imported from the cytosol by translocases in the chloroplast envelope membranes. Proteolytic regulation of the translocases is critically important, but little is known about the underlying mechanisms. We applied forward genetics and proteomics in Arabidopsis to identify factors required for chloroplast outer envelope membrane (OEM) protein degradation. We identified SP2, an Omp85-type ß-barrel channel of the OEM, and CDC48, a cytosolic AAA+ (ATPase associated with diverse cellular activities) chaperone. Both proteins acted in the same pathway as the ubiquitin E3 ligase SP1, which regulates OEM translocase components. SP2 and CDC48 cooperated to bring about retrotranslocation of ubiquitinated substrates from the OEM (fulfilling conductance and motor functions, respectively), enabling degradation of the substrates by the 26S proteasome in the cytosol. Such chloroplast-associated protein degradation (CHLORAD) is vital for organellar functions and plant development.