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Evolution of casein kinase 1 and functional analysis of new doubletime mutants in Drosophila

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F22%3A00565630" target="_blank" >RIV/60077344:_____/22:00565630 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/22:43906039

  • Result on the web

    <a href="https://www.frontiersin.org/articles/10.3389/fphys.2022.1062632/pdf" target="_blank" >https://www.frontiersin.org/articles/10.3389/fphys.2022.1062632/pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3389/fphys.2022.1062632" target="_blank" >10.3389/fphys.2022.1062632</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Evolution of casein kinase 1 and functional analysis of new doubletime mutants in Drosophila

  • Original language description

    Circadian clocks are timing devices that rhythmically adjust organism’s behavior, physiology, and metabolism to the 24-h day-night cycle. Eukaryotic circadian clocks rely on several interlocked transcription-translation feedback loops, where protein stability is the key part of the delay between transcription and the appearance of the mature proteins within the feedback loops. In bilaterian animals, including mammals and insects, the circadian clock depends on a homologous set of proteins. Despite mostly conserved clock components among the fruit fly Drosophila and mammals, several lineage-specific differences exist. Here we have systematically explored the evolution and sequence variability of insect DBT proteins and their vertebrate homologs casein kinase 1 delta (CKIδ) and epsilon (CKIε), dated the origin and separation of CKIδ from CKIε, and identified at least three additional independent duplications of the CKIδ/ε gene in Petromyzon, Danio, and Xenopus. We determined conserved regions in DBT specific to Diptera, and functionally tested a subset of those in D. melanogaster. Replacement of Lysine K224 with acidic residues strongly impacts the free-running period even in heterozygous flies, whereas homozygous mutants are not viable. K224D mutants have a temperature compensation defect with longer free-running periods at higher temperatures, which is exactly the opposite trend of what was reported for corresponding mammalian mutants. All DBTs of dipteran insects contain the NKRQK motif at positions 220–224. The occurrence of this motif perfectly correlates with the presence of BRIDE OF DOUBLETIME, BDBT, in Diptera. BDBT is a non-canonical FK506-binding protein that physically interacts with Drosophila DBT. The phylogeny of FK506-binding proteins suggests that BDBT is either absent or highly modified in non-dipteran insects. In addition to in silico analysis of DBT/CKIδ/ε evolution and diversity, we have identified four novel casein kinase 1 genes specific to the Drosophila genus.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10605 - Developmental biology

Result continuities

  • Project

    <a href="/en/project/GA22-10088S" target="_blank" >GA22-10088S: Functional Analysis of Drosophila Timeless Protein</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Frontiers in Physiology

  • ISSN

    1664-042X

  • e-ISSN

    1664-042X

  • Volume of the periodical

    13

  • Issue of the periodical within the volume

    DEC 14

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    17

  • Pages from-to

    1062632

  • UT code for WoS article

    000937214800001

  • EID of the result in the Scopus database

    2-s2.0-85145046184