Evidence map›Paper›PMID 23388462›Full record

ArticleCell cycle (Georgetown, Tex.)2013

Nature of KaiB-KaiC binding in the cyanobacterial circadian oscillator.

Rekha Pattanayek, Kirthi Kiran Yadagiri, Melanie D Ohi, Martin Egli

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Insight into cyanobacterial circadian timing from structural details of the KaiB-KaiC interaction.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Rekha PattanayekDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Kirthi Kiran Yadagiri
Melanie D Ohi
Martin Egli
Vanderbilt University · USNashville Oncology Associates · US

Funding

Structural Biology of the S. elongatus Circadian ClockR01GM073845 · NIGMS · VANDERBILT UNIVERSITY · PI EGLI, MARTIN · 2006 to 2013
$2.4M
NIGMS NIH HHS R01 GM073845
6 · The paper itself

Abstract

In the cyanobacteria Synechococcus elongatus and Thermosynechococcus elongatus, the KaiA, KaiB and KaiC proteins in the presence of ATP generate a post-translational oscillator (PTO) that can be reconstituted in vitro. KaiC is the result of a gene duplication and resembles a double doughnut with N-terminal CI and C-terminal CII hexameric rings. Six ATPs are bound between subunits in both the CI and CII ring. CI harbors ATPase activity, and CII catalyzes phosphorylation and dephosphorylation at T432 and S431 with a ca. 24-h period. KaiA stimulates KaiC phosphorylation, and KaiB promotes KaiC subunit exchange and sequesters KaiA on the KaiB-KaiC interface in the final stage of the clock cycle. Studies of the PTO protein-protein interactions are convergent in terms of KaiA binding to CII but have led to two opposing models of the KaiB-KaiC interaction. Electron microscopy (EM) and small angle X-ray scattering (SAXS), together with native PAGE using full-length proteins and separate CI and CII rings, are consistent with binding of KaiB to CII. Conversely, NMR together with gel filtration chromatography and denatured PAGE using monomeric CI and CII domains support KaiB binding to CI. To resolve the existing controversy, we studied complexes between KaiB and gold-labeled, full-length KaiC with negative stain EM. The EM data clearly demonstrate that KaiB contacts the CII ring. Together with the outcomes of previous analyses, our work establishes that only CII participates in interactions with KaiA and KaiB as well as with the His kinase SasA involved in the clock output pathway.

Indexed as

Circadian ClocksBacterial ProteinsCircadian Rhythm Signaling Peptides and ProteinsHistidineModels, MolecularNanostructuresNegative StainingOligopeptidesProtein BindingScattering, Small AngleStatic ElectricitySynechococcusX-Ray DiffractionBacterial ProteinsCircadian Rhythm Signaling Peptides and ProteinsHis-His-His-His-His-HisHistidineKaiB protein, cyanobacteriaKaiC protein, cyanobacteriaOligopeptidescircadian clockdephosphorylationEMnanogoldSynechococcus elongatus

Identifiers

PMID23388462
PMCPMC3610728
OpenAlexW2157757854

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.