Structural basis of the day-night transition in a bacterial circadian clock

article Structural basis of the day-night transition in a bacterial circadian clock published yes Roger Tseng author Nicolette F. Goularte author Archana Chavan author Jansen Luu author Susan E. Cohen author Yong-Gang Chang author Joel Heisler author Sheng Li author Alicia Kathleen Michael author 6437c950-2a03-11ee-914d-d6476dd7b75c Sarvind Tripathi author Susan S. Golden author Andy LiWang author Carrie L. Partch author Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC,KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post–adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA. American Association for the Advancement of Science2017 eng Multidisciplinary Science 0036-8075 1095-920310.1126/science.aag2516 35563301174-1180 yes Tseng R, Goularte NF, Chavan A, Luu J, Cohen SE, Chang Y-G, Heisler J, Li S, Michael AK, Tripathi S, Golden SS, LiWang A, Partch CL. 2017. Structural basis of the day-night transition in a bacterial circadian clock. Science. 355(6330), 1174–1180. Tseng, Roger, Nicolette F. Goularte, Archana Chavan, Jansen Luu, Susan E. Cohen, Yong-Gang Chang, Joel Heisler, et al. “Structural Basis of the Day-Night Transition in a Bacterial Circadian Clock.” Science. American Association for the Advancement of Science, 2017. <a href="https://doi.org/10.1126/science.aag2516">https://doi.org/10.1126/science.aag2516</a>. Tseng, Roger, et al. “Structural Basis of the Day-Night Transition in a Bacterial Circadian Clock.” Science, vol. 355, no. 6330, American Association for the Advancement of Science, 2017, pp. 1174–80, doi:<a href="https://doi.org/10.1126/science.aag2516">10.1126/science.aag2516</a>. R. Tseng, N.F. Goularte, A. Chavan, J. Luu, S.E. Cohen, Y.-G. Chang, J. Heisler, S. Li, A.K. Michael, S. Tripathi, S.S. Golden, A. LiWang, C.L. Partch, Science 355 (2017) 1174–1180. R. Tseng et al., “Structural basis of the day-night transition in a bacterial circadian clock,” Science, vol. 355, no. 6330. American Association for the Advancement of Science, pp. 1174–1180, 2017. Tseng, R., Goularte, N. F., Chavan, A., Luu, J., Cohen, S. E., Chang, Y.-G., … Partch, C. L. (2017). Structural basis of the day-night transition in a bacterial circadian clock. Science. American Association for the Advancement of Science. <a href="https://doi.org/10.1126/science.aag2516">https://doi.org/10.1126/science.aag2516</a> Tseng R, Goularte NF, Chavan A, et al. Structural basis of the day-night transition in a bacterial circadian clock. Science. 2017;355(6330):1174-1180. doi:<a href="https://doi.org/10.1126/science.aag2516">10.1126/science.aag2516</a> 151562024-03-21T07:56:24Z2024-03-25T12:16:44Z