Saini, Reena, Jaskolski, Mariusz and Davis, Seth Jon orcid.org/0000-0001-5928-9046 (2019) Circadian oscillator proteins across the kingdoms of life:Structural aspects 06 Biological Sciences 0601 Biochemistry and Cell Biology. BMC Biology. 13. ISSN 1741-7007
Abstract
Circadian oscillators are networks of biochemical feedback loops that generate 24-hour rhythms and control numerous biological processes in a range of organisms. These periodic rhythms are the result of a complex interplay of interactions among clock components. These components are specific to the organism but share molecular mechanisms that are similar across kingdoms. The elucidation of clock mechanisms in different kingdoms has recently started to attain the level of structural interpretation. A full understanding of these molecular processes requires detailed knowledge, not only of the biochemical and biophysical properties of clock proteins and their interactions, but also the three-dimensional structure of clockwork components. Posttranslational modifications (such as phosphorylation) and protein-protein interactions, have become a central focus of recent research, in particular the complex interactions mediated by the phosphorylation of clock proteins and the formation of multimeric protein complexes that regulate clock genes at transcriptional and translational levels. The three-dimensional structures for the cyanobacterial clock components are well understood, and progress is underway to comprehend the mechanistic details. However, structural recognition of the eukaryotic clock has just begun. This review serves as a primer as the clock communities move towards the exciting realm of structural biology.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Author(s). 2019 |
Keywords: | Circadian rhythms,Clock genes,Crystallography,Feedback loops,Homo-and heteroprotein complexes,Phosphorylation,Transcription factors |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 02 Jan 2019 11:20 |
Last Modified: | 16 Oct 2024 15:22 |
Published Version: | https://doi.org/10.1186/s12915-018-0623-3 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1186/s12915-018-0623-3 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:140408 |