Binding of de novo synthesized radiolabeled juvenile hormone (JH III) by JH receptors from the Cuban subterranean termite Prorhinotermes simplex and the German cockroach Blattella germanica
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903811" target="_blank" >RIV/60076658:12310/21:43903811 - isvavai.cz</a>
Alternative codes found
RIV/60077344:_____/21:00546812 RIV/61388963:_____/21:00546812
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0965174821001545?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0965174821001545?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ibmb.2021.103671" target="_blank" >10.1016/j.ibmb.2021.103671</a>
Alternative languages
Result language
angličtina
Original language name
Binding of de novo synthesized radiolabeled juvenile hormone (JH III) by JH receptors from the Cuban subterranean termite Prorhinotermes simplex and the German cockroach Blattella germanica
Original language description
Juvenile hormone (JH) controls insect reproduction and development through an intracellular receptor complex comprising two bHLH-PAS proteins, the JH-binding Methoprene-tolerant (Met) and its partner Taiman (Tai). Many hemimetabolous insects including cockroaches strictly depend on JH for stimulation of vitellogenesis. In termites, the eusocial hemimetabolans, JH also regulates the development of caste polyphenism. Studies addressing the agonist ligand binding to recombinant JH receptors currently include three species belonging to two holometabolous insect orders, but none that would represent any of the hemimetabolous orders. Here, we examined JH receptors in two representatives of Blattodea, the cockroach Blattella germanica and the termite Prorhinotermes simplex. To test the JH-binding capacity of Met proteins from these species, we performed chemical synthesis and tritium labeling of the natural blattodean JH homolog, JH III. Our improved protocol increased the yield and specific activity of [10-H-3]JH III relative to formerly available preparations. Met proteins from both species specifically bound [H-3]JH III with high affinity, whereas Met variants mutated at a critical position within the ligand-binding domain were incapable of such binding. Furthermore, JH III and the synthetic JH mimic fenoxycarb stimulated dimerization between Met and Tai components of the respective JH receptors of both species. These data present primary evidence for agonist binding by JH receptors in any hemimetabolous species and provide a molecular basis for JH action in cockroaches and termites.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10616 - Entomology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Insect Biochemistry and Molecular Biology
ISSN
0965-1748
e-ISSN
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Volume of the periodical
139
Issue of the periodical within the volume
DEC 2021
Country of publishing house
GB - UNITED KINGDOM
Number of pages
9
Pages from-to
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UT code for WoS article
000711780700006
EID of the result in the Scopus database
2-s2.0-85117203283