Structural basis of the day-night transition in a bacterial circadian clock
Abstract
The cyanobacterial circadian clock oscillator can be reconstituted in a test tube from just three proteins—KaiA, KaiB, and KaiC—and adenosine triphosphate (ATP). Tseng et al. studied crystal and nuclear magnetic resonance structures of complexes of the oscillator proteins and their signaling output proteins and tested the in vivo effects of structure-based mutants. Large conformational changes in KaiB and ATP hydrolysis by KaiC are coordinated with binding to output protein, which couples signaling and the day-night transitions of the clock. Snijder et al. provide complementary analysis of the oscillator proteins by mass spectrometry and cryo–electron microscopy. Their results help to explain the structural basis for the dynamic assembly of the oscillator complexes.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Mar 17, 2017
- Source ID
- 10.1126/science.aag2516
Entities
People
- Alicia K. Michael
- Andy LiWang
- Archana Chavan
- Carrie L. Partch
- Jansen Luu
- Joel Heisler
- Nicolette Goularte
- Roger Tseng
- Sarvind Tripathi
- Sheng Li
- Susan E Cohen
- Susan Golden
- Yong-Gang Chang
Organizations
- Air Force Office of Scientific Research
- American Cancer Society
- National Institutes of Health
- National Science Foundation
- University of California
- University of California, San Diego
- University of California, Santa Cruz