ArticlePLoS biology2009
Structural and functional analyses of PAS domain interactions of the clock proteins Drosophila PERIOD and mouse PERIOD2.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- Functional deficiency of circadian regulator PER2 enhances breast cancer susceptibility and progression with immunosuppression.Oncogene · 2026Article
- Role of PER-WDR5 interactions in the mammalian circadian clock.Nature communications · 2026Article
- PAS-Domain Protein Orientation at a Polyelectrolyte Surface Revealed by Infrared Nanospectroscopy, Chiral Vibrational Spectroscopy, and Molecular Dynamics Simulations.Biomacromolecules · 2026Article
- The PER2:BRCA1:POU2F1(OCT-1) ternary complex represents a multi-component scaffold model for circadian gene regulation.Neurobiology of sleep and circadian rhythms · 2026Article
- Genomic Signatures of Speciation in Butterflies.Systematic biology · 2026Article
- Oligomerization of PER2 as a dynamic mode of regulation of the mammalian circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biochemical mechanism of the mammalian circadian clock.FEBS letters · 2026Review
- The Period (Animals : an open access journal from MDPI · 2026Article
- FLYWCH transcription factors act in a LIN-42/Period autoregulatory loop during gonad migration inbioRxiv : the preprint server for biology · 2025Article
- A wrinkle in timers: evolutionary rewiring of conserved biological timekeepers.Trends in biochemical sciences · 2025Review
- PERspectives on circadian cell biology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- The role of circadian rhythm regulator PERs in oxidative stress, immunity, and cancer development.Cell communication and signaling : CCS · 2025Review
- PERfect Day: reversible and dose-dependent control of circadian time-keeping in the mouse suprachiasmatic nucleus by translational switching of PERIOD2 protein expression.The European journal of neuroscience · 2024Article
- Clock gene homologs lin-42 and kin-20 regulate circadian rhythms in C. elegans.Scientific reports · 2024Article
- Hierarchical and scaffolded phosphorylation of two degrons controls PER2 stability.The Journal of biological chemistry · 2024Article
- Article
- Dimerization Rules of Mammalian PAS Proteins.Journal of molecular biology · 2024Review
- PAS Dimerization at the Nexus of the Mammalian Circadian Clock.Journal of molecular biology · 2024Review
- Mammalian circadian clock proteins form dynamic interacting microbodies distinct from phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mammalian circadian clock proteins form dynamic interacting microbodies distinct from phase separation.bioRxiv : the preprint server for biology · 2023Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PERIOD proteins are central components of the Drosophila and mammalian circadian clocks. The crystal structure of a Drosophila PERIOD (dPER) fragment comprising two PER-ARNT-SIM (PAS) domains (PAS-A and PAS-B) and two additional C-terminal alpha-helices (alphaE and alphaF) has revealed a homodimer mediated by intermolecular interactions of PAS-A with tryptophane 482 in PAS-B and helix alphaF. Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix. Moreover, we have solved the crystal structure of a PAS domain fragment of the mouse PERIOD homologue mPER2. The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419 (equivalent to Trp482dPER). We have validated and quantitatively analysed the homodimer interactions of dPER and mPER2 by site-directed mutagenesis using analytical gel filtration, analytical ultracentrifugation, and co-immunoprecipitation experiments. Furthermore we show, by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM). Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2. In addition, we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
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