Structural and Biochemical Characterization of a Cyanobacterium Circadian Clock-modifier Protein *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 282, Issue: 2, Page: 1128-1135
2007
- 29Citations
- 35Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations29
- Citation Indexes27
- 27
- CrossRef23
- Policy Citations2
- Policy Citation2
- Captures35
- Readers35
- 35
Article Description
Circadian clocks are self-sustained biochemical oscillators. The oscillator of cyanobacteria comprises the products of three kai genes ( kaiA, kaiB, and kaiC ). The autophosphorylation cycle of KaiC oscillates robustly in the cell with a 24-h period and is essential for the basic timing of the cyanobacterial circadian clock. Recently, period extender ( pex ), mutants of which show a short period phenotype, was classified as a resetting-related gene. In fact, pex mRNA and the pex protein (Pex) increase during the dark period, and a pex mutant subjected to diurnal light-dark cycles shows a 3-h advance in rhythm phase. Here, we report the x-ray crystallographic analysis and biochemical characterization of Pex from cyanobacterium Synechococcus elongatus PCC 7942. The molecule has an (α + β) structure with a winged-helix motif and is indicated to function as a dimer. The subunit arrangement in the dimer is unique and has not been seen in other winged-helix proteins. Electrophoresis mobility shift assay using a 25-base pair complementary oligonucleotide incorporating the kaiA upstream sequence demonstrates that Pex has an affinity for the double-stranded DNA. Furthermore, mutation analysis shows that Pex uses the wing region to recognize the DNA. The in vivo rhythm assay of Pex shows that the constitutive expression of the pex gene harboring the mutation that fails to bind to DNA lacks the period-prolongation activity in the pex -deficient Synechococcus, suggesting that Pex is a DNA-binding transcription factor.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820735404; http://dx.doi.org/10.1074/jbc.m608148200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33847691603&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17098741; http://www.jbc.org/lookup/doi/10.1074/jbc.M608148200; https://syndication.highwire.org/content/doi/10.1074/jbc.M608148200; https://linkinghub.elsevier.com/retrieve/pii/S0021925820735404; https://dx.doi.org/10.1074/jbc.m608148200
American Society for Biochemistry & Molecular Biology (ASBMB)
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