Growth dynamics of pentacene thin films

The recent demonstration of single-crystal organic optoelectronic devices has received widespread attention. But practical applications of such devices require the use of inexpensive organic films deposited on a wide variety of substrates. Unfortunately, the physical properties of these organic thin films do not compare favourably to those of single-crystal materials. Moreover, the basic physical principles governing organic thin-film growth and crystallization are not well understood. Here we report an in situ study of the evolution of pentacene thin films, utilizing the real-time imaging capabilities of photoelectron emission microscopy. By a combination of careful substrate preparation and surface energy control, we succeed in growing thin films with single-crystal grain sizes approaching 0.1 millimetre (a factor of 20-100 larger than previously achieved), which are large enough to fully contain a complete device. We find that organic thin-film growth closely mimics epitaxial growth of inorganic materials, and we expect that strategies and concepts developed for these inorganic systems will provide guidance for the further development and optimization of molecular thin-film devices.     

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.

In eukaryotic cells, incorrectly folded proteins in the endoplasmic reticulum (ER) are exported into the cytosol and degraded by the proteasome. This pathway is co-opted by some viruses. For example, the US11 protein of the human cytomegalovirus targets the major histocompatibility complex class I heavy chain for cytosolic degradation. How proteins are extracted from the ER membrane is unknown. In bacteria and mitochondria, members of the AAA ATPase family are involved in extracting and degrading membrane proteins. Here we demonstrate that another member of this family, Cdc48 in yeast and p97 in mammals, is required for the export of ER proteins into the cytosol. Whereas Cdc48/p97 was previously known to function in a complex with the cofactor p47 (ref. 5) in membrane fusion, we demonstrate that its role in ER protein export requires the interacting partners Ufd1 and Npl4. The AAA ATPase interacts with substrates at the ER membrane and is needed to release them as polyubiquitinated species into the cytosol. We propose that the Cdc48/p97-Ufd1-Npl4 complex extracts proteins from the ER membrane for cytosolic degradation.     

Distribution, abundance, and genetic population structure of Wood River sculpin, Cottus leiopomus

The Wood River sculpin Cottus leiopomus is endemic to the Wood River Basin in central Idaho and is a nongame species of concern because of its limited distribution. However, status and genetic population structure, 2 factors often central to the conservation and management of species of concern, have not been assessed for this species. We used backpack electrofishers to survey streams that were small enough (i.e., a priori to contain, possibly contain, or not contain the sculpin, respectively. Native redband trout Oncorhynchus mykiss gairdneri were present at 21 study sites, including 18 of the 20 sites that contained Wood River sculpin. Sixty-one study sites (60%) were dry or had too little water to contain any fish. We estimated that a minimum of 1.36 million Wood River sculpin (≥20 mm total length) currently reside in the basin. The presence of Wood River sculpin was positively associated with stream width:depth ratio and percent cobble/boulder substrate and negatively associated with stream gradient. Mitochondrial DNA haplotype differences were observed between and within the 3 major river subbasins supporting sculpin, with the most striking differences observed between populations in the Camas Creek subbasin and the other 2 subbasins, among which no haplotypes were shared, suggesting relatively long-term isolation. Our results suggest that the Wood River sculpin remains relatively widespread and abundant within its endemic range, despite obvious changes in historical stream connectivity caused by irrigation diversions and other chronic habitat alterations.     

Phylogenomic analyses unravel annelid evolution

Annelida, the ringed worms, is a highly diverse animal phylum that includes more than 15,000 described species and constitutes the dominant benthic macrofauna from the intertidal zone down to the deep sea. A robust annelid phylogeny would shape our understanding of animal body-plan evolution and shed light on the bilaterian ground pattern. Traditionally, Annelida has been split into two major groups: Clitellata (earthworms and leeches) and polychaetes (bristle worms), but recent evidence suggests that other taxa that were once considered to be separate phyla (Sipuncula, Echiura and Siboglinidae (also known as Pogonophora)) should be included in Annelida. However, the deep-level evolutionary relationships of Annelida are still poorly understood, and a robust reconstruction of annelid evolutionary history is needed. Here we show that phylogenomic analyses of 34 annelid taxa, using 47,953 amino acid positions, recovered a well-supported phylogeny with strong support for major splits. Our results recover chaetopterids, myzostomids and sipunculids in the basal part of the tree, although the position of Myzostomida remains uncertain owing to its long branch. The remaining taxa are split into two clades: Errantia (which includes the model annelid Platynereis), and Sedentaria (which includes Clitellata). Ancestral character trait reconstructions indicate that these clades show adaptation to either an errant or a sedentary lifestyle, with alteration of accompanying morphological traits such as peristaltic movement, parapodia and sensory perception. Finally, life history characters in Annelida seem to be phylogenetically informative.     

Plasma catecholamines in conscious rats: Influence of sodium,stress and heredity

Summary Plasma catecholamines are increased in sodium-loaded rats under both resting and stress conditions. Under stress, Na⁺ resistant rats have lower plasma catecholamines than salt-sensitive ones.Supported in part by grants from Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS) and Délégation Générale à la Recherche Scientifique et Technique (DGRST).