Thermal Structure of Jupiter's Upper Atmosphere Derived from the Galileo Probe

Temperatures in Jupiter's atmosphere derived from Galileo Probe deceleration data increase from 109 kelvin at the 175-millibar level to 900 ± 40 kelvin at 1 nanobar, consistent with Voyager remote sensing data. Wavelike oscillations are present at all levels. Vertical wavelengths are 10 to 25 kilometers in the deep isothermal layer, which extends from 12 to 0.003 millibars. Above the 0.003-millibar level, only 90- to 270- kilometer vertical wavelengths survive, suggesting dissipation of wave energy as the probable source of upper atmosphere heating.     

High-Energy Charged Particles in the Innermost Jovian Magnetosphere

The energetic particles investigation carried by the Galileo probe measured the energy and angular distributions of the high-energy particles from near the orbit of Io to probe entry into the jovian atmosphere. Jupiter's inner radiation region had extremely large fluxes of energetic electrons and protons; intensities peaked at approximately2.2RJ (where RJ is the radius of Jupiter). Absorption of the measured particles was found near the outer edge of the bright dust ring. The instrument measured intense fluxes of high-energy helium ions (approximately62 megaelectron volts per nucleon) that peaked at approximately1.5RJ inside the bright dust ring. The abundances of all particle species decreased sharply at approximately1.35RJ; this decrease defines the innermost edge of the equatorial jovian radiation.     

Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution

Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.