Architecture of the active post‐translational Sec translocon

In eukaryotes, most secretory and membrane proteins are targeted by an N‐terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein‐conducting channel (PCC). In the post‐translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre‐opened state. Here, we present a cryo‐EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N‐terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C‐terminus of Sec63. Together, we obtained a near‐complete and integrated model of the active Sec complex.     

Cytodifferentiation in the Pars Distalis of the Pituitary Gland in the Fetal and Juvenile Mink,Mustela vison

Hypophysial tissue of mink (Mustela vison) embryos, newborn young and kits aged 1 day to 27 weeks was examined by light and electron microscopy. Among the embryos five different ontogenetic stages were distinguished. It appears that the primordium of the pituitary gland differentiates in early embryonic life. Several types of glandular cells containing variable amounts of granular material were recognizable by the time of birth. The role of the granular cells and the origin of the lumina in the pars distalis are speculated upon (in the Discussion).