ABSTRACT
Large constellations of bright artificial satellites in low Earth orbit pose significant challenges to ground-based astronomy1. Current orbiting constellation satellites have brightnesses between apparent magnitudes 4 and 6, whereas in the near-infrared Ks band, they can reach magnitude 2 (ref. 2). Satellite operators, astronomers and other users of the night sky are working on brightness mitigation strategies3,4. Radio emissions induce further potential risk to ground-based radio telescopes that also need to be evaluated. Here we report the outcome of an international optical observation campaign of a prototype constellation satellite, AST SpaceMobile's BlueWalker 3. BlueWalker 3 features a 64.3 m2 phased-array antenna as well as a launch vehicle adaptor (LVA)5. The peak brightness of the satellite reached an apparent magnitude of 0.4. This made the new satellite one of the brightest objects in the night sky. Additionally, the LVA reached an apparent V-band magnitude of 5.5, four times brighter than the current International Astronomical Union recommendation of magnitude 7 (refs. 3,6); it jettisoned on 10 November 2022 (Universal Time), and its orbital ephemeris was not publicly released until 4 days later. The expected build-out of constellations with hundreds of thousands of new bright objects1 will make active satellite tracking and avoidance strategies a necessity for ground-based telescopes.
ABSTRACT
DNA mutagenesis is generally considered harmful. Yet activated B cells normally mutate the Ig loci. Because this somatic hypermutation is potentially dangerous, it has been hypothesized that mutations do not occur throughout the genome but instead are actively targeted to the Ig loci. Here we challenge this longstanding and widely accepted hypothesis. We demonstrate that hypermutation requires no Ig gene sequences. Instead, activation-induced cytidine deaminase and other trans-acting hypermutation factors may function as general mutators.
Subject(s)
Genome , Mutation , Cell Line , Genes, ReporterABSTRACT
Unrepaired DNA double-strand breaks can lead to apoptosis or tumorigenesis. In mammals double-strand breaks are repaired mainly by nonhomologous end-joining mediated by the DNA-PK complex. The core protein of this complex, DNA-PKcs, is a DNA-dependent serine/threonine kinase that phosphorylates protein targets as well as itself. Although the (auto)phosphorylation activity has been shown to be essential for repair of both random double-strand breaks and induced breaks at the immunoglobulin locus, the corresponding phosphatase has been elusive. In fact, to date, none of the putative phosphatases in DNA double-strand break repair has been identified. Here we show that protein phosphatase 5 interacts with DNA-PKcs and dephosphorylates with surprising specificity at least two functional sites. Cells with either hypo- or hyperphosphorylation of DNA-PKcs at these sites show increased radiation sensitivity.