The transcriptional repressions driven by the circadian core clock repressors RevErbα, E4BP4, and CRY1/PER1 involve feedback loops which are mandatory for generating the circadian rhythms. These repressors are known to bind to cognate DNA binding sites, but how their circadian bindings trigger the cascade of events leading to these repressions remain to be elucidated. Through molecular and genetic analyses, we now demonstrate that the chromatin protein HP1α plays a key role in these transcriptional repressions of both the circadian clock (CC) genes and their cognate output genes (CCGs).
View Article and Find Full Text PDFComp Biochem Physiol B Biochem Mol Biol
November 2010
We cloned the complete cDNA of methionine rich hexamerin from rice moth, Corcyra cephalonica using RACE strategy. The amplicon size was 2.5 kb with an ORF of 2.
View Article and Find Full Text PDFThe insect development is intricately controlled by morphogenetic hormones, juvenile hormone (JH) and 20-hydroxyecdysone (20E) through the regulation of gene/protein expression. The role of hexamerins in the metamorphosis of insects and reproduction and their control by 20E at the gene level has been widely reported in insects. In the present study we for the first time report the role of ecdysteroids in the regulation of hexamerin synthesis in a lepidopteran insect Corcyra cephalonica.
View Article and Find Full Text PDFSelective receptor mediated uptake is a widely prevalent mechanism in insects by which important macromolecules are acquired. Among the various proteins sequestered by the insect fat body, the larval hexamerins form the major group. In the present work full length cDNA (2.
View Article and Find Full Text PDFHexamerins are stage specifically sequestered during the non-feeding stages mainly by the fat body cells from hemolymph through ecdysteroid regulated receptor-mediated endocytosis. 20-Hydroxyecdysone (20E) stimulates the tyrosine kinase-mediated phosphorylation of the 120kDa hexamerin receptor in the rice moth, Corcyra cephalonica. Here, we demonstrate that phosphorylation of the hexamerin receptor by HP19-regulated-20E-dependent-tyrosine kinase is a critical regulator for its activation, and is required for hexamerin uptake.
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