Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Tseng R 

PROVIDER: S-EPMC5441561 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications


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  ...[more]

Similar Datasets

| S-EPMC5806683 | biostudies-other
| S-EPMC2529086 | biostudies-literature
| S-EPMC8073545 | biostudies-literature
| S-EPMC6210193 | biostudies-literature
| S-EPMC1847943 | biostudies-literature
| S-EPMC1456936 | biostudies-literature
2018-10-01 | GSE116795 | GEO
| S-EPMC8789273 | biostudies-literature
| S-EPMC6137998 | biostudies-literature
| S-EPMC6479001 | biostudies-literature