DIFFERENTIAL INCORPORATION OF [3H]LYSINE INTO VISUAL CORTEX PROTEIN FRACTIONS DURING FIRST EXPOSURE TO LIGHT

—A resolution of the enhancement of protein synthesis in the visual cortex of rats during first exposure to light (Richardson and Rose , 1972) was achieved by polyacrylamide gel electrophoresis using a double-labelling technique. Differential incorporation of lysine was established between exposed and control animals in two fractions of the soluble proteins and seven fractions of the insoluble proteins. This suggests that exposure to a new experience of this type involves a specific effect on protein synthesis, rather than a general stimulation across all fractions.     

Halobates collected during the circumnavigational expedition 'Operation Drake'

Samples of marine pleuston were collected from the sea-surface along considerable sections of the track of Eye of the Wind during its 2-year circumnavigational expedition 'Operation Drake' from November 1978 to October 1980. One hundred and eleven of the tow samples contained insects of the genus Halobates . They were assigned to four oceanic species: H. micans, H. sericeus, H. germanus and H. splendens; two coastal species: H. maculatus, H. princeps, and one undescribed species. Various development stages of the oceanic species were found. The locations, time of collection and surface temperatures where sea-skaters were collected are tabulated. Distributional boundaries and population densities of the oceanic species collected are discussed.     

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP.

Ffh is a component of a bacterial ribonucleoprotein complex homologous to the signal recognition particle (SRP) of eukaryotes. It comprises three domains that mediate both binding to the hydrophobic signal sequence of the nascent polypeptide and the GTP-dependent interaction of Ffh with a structurally homologous GTPase of the SRP receptor. The X-ray structures of the two-domain 'NG' GTPase of Ffh in complex with Mg2+GDP and GDP have been determined at 2.0 A resolution. The structures explain the low nucleotide affinity of Ffh and locate two regions of structural mobility at opposite sides of the nucleotide-binding site. One of these regions includes highly conserved sequence motifs that presumably contribute to the structural trigger signaling the GTP-bound state. The other includes the highly conserved interface between the N and G domains, and supports the hypothesis that the N domain regulates or signals the nucleotide occupancy of the G domain.