A protein fold switch joins the circadian oscillator to clock output in cyanobacteria
Open accessAbstract
Biochemical basis of a 24-hour clock: Circadian clocks keep organisms in synch with such daily cycles as illumination, activity, and food availability. The circadian clock in cyanobacteria has the necessary 24-hour period despite its three component proteins having biochemical activities that occur on a much faster time scale. Abe et al. focused on the cyanobacterial clock component KaiC, an adenosine triphosphatase (ATPase) that can autophosphorylate and autodephosphorylate. The slow ATPase activity of KaiC, which is linked to a peptide isomerisation, provided the slow kinetics that set the speed of the 24-hour clock. Chang et al. found that another clock component, KaiB, also has slow changes in its protein conformation that help to set the oscillation period of the clock and its signaling output. Science , this issue pp. 312 and 324
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Predictions of both conformations of KaiB were distributed in clusters across the KaiB family.
“Using this method, named AF-Cluster, we investigated the evolutionary distribution of predicted structures for the metamorphic protein KaiB5 and found that predictions of both conformations were distributed in clusters across the KaiB family.”
From Predicting multiple conformations via sequence clustering and AlphaFold2 (2024) · cites this paper as [5]
KaiBRS switches between two monomeric states as found using NMR.
“We used KaiB from R. sphaeroides32 (hereafter KaiBRS) for this test, which we found using NMR switches between two monomeric states, to eliminate the complicating factor of mutations contributing to ground-state tetramerization in the previously studied KaiBTE (ref. 5).”
From Predicting multiple conformations via sequence clustering and AlphaFold2 (2024) · cites this paper as [5]
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References 60 · Cited by 212
- Authors
- Chang, Y.-G., Cohen, S. E., Phong, C., Myers, W. K., Kim, Y.-I., Tseng, R., Lin, J., Zhang, L., Boyd, J. S., Lee, Y., Kang, S., Lee, D., Li, S., Britt, R. D., Rust, M. J., Golden, S. S., & LiWang, A.
- Affiliations
- University of California, Merced (US)
- University of California San Diego (US)
- University of Chicago (US)
- University of California, Davis (US)
- Corresponding author
- LiWang, Andy
- ORCID
- Venue
- Science
- Published
- 2015-07-17
- Volume
- 349
- Issue
- 6245
- Pages
- 324-328
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4506712
- OpenAlex
- W1550289833
- Cited by
- 212
- References
- 60
- Citations by year
- 2026: 23 · 2025: 22 · 2024: 15 · 2023: 19 · 2022: 22 · 2021: 24 · 2020: 20 · 2019: 15 · 2018: 19 · 2017: 14 · 2016: 11 · 2015: 8
- FWCI
- 9.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- NSF
- NIH (GM107521, GM100116, GM062419, AI081982, AI101436)
- American Cancer Society (PF-12-262-01-MPC)
- Air Force Office of Scientific Research (13RSL012)
- Army Research Office (W911NF1410056)
- Burroughs-Wellcome Career Award at the Scientific Interface
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- circadian clock, KaiABC oscillator, KaiB, protein folding, KaiC phosphorylation, time delay, phase transitions, cyanobacteria, KaiA
- MeSH terms
- Bacterial Proteins, Circadian Rhythm, Phosphorylation, Protein Structure, Secondary, Protein Folding, Synechococcus, Circadian Rhythm Signaling Peptides and Proteins
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