RCA Satcom: In-orbit experience

The system characteristics of the Satcom batteries and Satcom power system are briefly discussed. Performance of the nickel cadmium 22 cell batteries onboard in parallel with independent redundant charges providing the charge rates is reported. Performance onboard reconditioning with individual cell bypasses with 1 ohm resistors is discussed for the F-1 and F-2 spacecraft

Mapping biodiversity value worldwide: combining higher-taxon richness from different groups

Maps of large-scale biodiversity are urgently needed to guide conservation, and yet complete enumeration of organisms is impractical at present. One indirect approach is to measure richness at higher taxonomic ranks, such as families. The difficulty is how to combine information from different groups on numbers of higher taxa, when these taxa may in effect have been defined in different ways, particularly for more distantly related major groups. In this paper, the regional family richness of terrestrial and freshwater seed plants, amphibians, reptiles and mammals is mapped worldwide by combining: (i) absolute family richness; (ii) proportional family richness; and (iii) proportional family richness weighted for the total species richness in each major group. The assumptions of the three methods and their effects on the results are discussed, although for these data the broad pattern is surprisingly robust with respect to the method of combination. Scores from each of the methods of combining families are used to rank the top five richness hotspots and complementary areas, and hotspots of endemism are mapped by unweighted combination of range-size rarity scores

Landing gear Patent

Vertically descending flight vehicle landing gear for rough terrai

DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers

Protein self-organization is essential for the establishment and maintenance of nuclear architecture and for the regulation of gene expression. We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. We have also shown that many PRH target genes contain suitably spaced arrays of PRH sites that allow this protein to bind and regulate transcription. Here, we use analytical ultracentrifugation and electron microscopy to further characterize PRH oligomers. We use the same techniques to show that PRH oligomers bound to long DNA fragments self-associate to form highly ordered assemblies. Electron microscopy and linear dichroism reveal that PRH oligomers can form protein–DNA fibres and that PRH is able to compact DNA in the absence of other proteins. Finally, we show that DNA compaction is not sufficient for the repression of PRH target genes in cells. We conclude that DNA compaction is a consequence of the binding of large PRH oligomers to arrays of binding sites and that PRH is functionally and structurally related to the Lrp/AsnC family of proteins from bacteria and archaea, a group of proteins formerly thought to be without eukaryotic equivalents

DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers

Protein self-organization is essential for the establishment and maintenance of nuclear architecture and for the regulation of gene expression. We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. We have also shown that many PRH target genes contain suitably spaced arrays of PRH sites that allow this protein to bind and regulate transcription. Here, we use analytical ultracentrifugation and electron microscopy to further characterize PRH oligomers. We use the same techniques to show that PRH oligomers bound to long DNA fragments self-associate to form highly ordered assemblies. Electron microscopy and linear dichroism reveal that PRH oligomers can form protein–DNA fibres and that PRH is able to compact DNA in the absence of other proteins. Finally, we show that DNA compaction is not sufficient for the repression of PRH target genes in cells. We conclude that DNA compaction is a consequence of the binding of large PRH oligomers to arrays of binding sites and that PRH is functionally and structurally related to the Lrp/AsnC family of proteins from bacteria and archaea, a group of proteins formerly thought to be without eukaryotic equivalents

April 30, 1927

The Breeze is the student newspaper of James Madison University in Harrisonburg, Virginia