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

0546812 - BC 2022 RIV GB eng J - Článek v odborném periodiku
Miláček, Matěj - Bittová, Lenka - Tůmová, Šárka - Lukšan, Ondřej - Hanus, Robert - Kyjaková, Pavlína - Machara, Aleš - Marek, Aleš - Jindra, Marek
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.
Insect Biochemistry and Molecular Biology. Roč. 139, DEC 01 (2021), č. článku 103671. ISSN 0965-1748. E-ISSN 1879-0240
Grant CEP: GA ČR(CZ) GX20-05151X; GA MŠMT(CZ) LM2015064; GA MŠMT(CZ) LM2018131
Institucionální podpora: RVO:60077344 ; RVO:61388963
Klíčová slova: juvenile hormone * methoprene-tolerant * hormone receptor
Obor OECD: Biochemistry and molecular biology; Entomology (UOCHB-X)
Impakt faktor: 4.421, rok: 2021
Způsob publikování: Omezený přístup
https://www.sciencedirect.com/science/article/pii/S0965174821001545?via%3Dihub

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 [10-3H]JH III relative to formerly available preparations. Met proteins from both species specifically bound [3H]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.
Trvalý link: http://hdl.handle.net/11104/0326652