Internal clocks driving rhythms of about a day (circadian) are ubiquitous in animals, allowing them to anticipate environmental changes. Genetic or environmental disturbances to circadian clocks or the rhythms they produce are commonly associated with illness, compromised performance or reduced survival. Nevertheless, some animals including Arctic mammals, open sea fish and social insects such as honeybees are active around-the-clock with no apparent ill effects. The mechanisms allowing this remarkable natural plasticity are unknown. We generated and validated a new and specific antibody against the clock protein PERIOD of the honeybee Apis mellifera (amPER) and used it to characterize the circadian network in the honeybee brain. We found many similarities to Drosophila melanogaster and other insects, suggesting common anatomical organization principles in the insect clock that have not been appreciated before. Time course analyses revealed strong daily oscillations in amPER levels in foragers, which show circadian rhythms, and also in nurses that do not, although the latter have attenuated oscillations in brain mRNA clock gene levels. The oscillations in nurses show that activity can be uncoupled from the circadian network and support the hypothesis that a ticking circadian clock is essential even in around-the-clock active animals in a constant physical environment.
Background: Cpa, the pilus adhesin from Streptococcus pyogenes, has an active thioester domain. Results: Cpa has a second thioester domain reactive toward biological amines. Conclusion: The crystal structure of spermidine-bound Cpa provides a model for covalent adhesion. Significance: Thioester domains and covalent adhesion may be common in Gram-positive pathogens.
Highlights d 3.7-Å structure and near-complete atomic model of autoinhibited Tel1 ATM d 2.8-Å active site with Mg 2+ -ATPgS reveals elements of catalysis and autoinhibition d PRD is locked by FATC and blocks active-site access as pseudo-substrate d The N-terminal solenoid has DNA binding activity
DNA double-strand breaks are repaired by two major pathways, homologous recombination or nonhomologous end joining. The commitment to one or the other pathway proceeds via different steps of resection of the DNA ends, which is controlled and executed by a set of DNA double-strand break sensors, endo-and exonucleases, helicases, and DNA damage response factors. The molecular choreography of the underlying protein machinery is beginning to emerge. In this review, we discuss the early steps of genetic recombination and double-strand break sensing with an emphasis on structural and molecular studies.
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