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Identification, sequence and mRNA expression pattern during metamorphosis of a cDNA encoding a glycine-rich cuticular protein in Tenebrio molitor.

J Mathelin·H Bouhin·B Quennedey·A Courrent·J Delachambre
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Abstract

The study of insect cuticular proteins and their sequences is of interest because they are involved in protein-protein and protein-chitin interactions which confer the mechanical properties and fine architecture of the cuticle. Moreover, in the coleopteran Tenebrio molitor there is a dramatic change in cuticular architecture between pre- and postecdysial secretion. We report the isolation, by differential screening, and the sequence characterization of a cDNA clone encoding a cuticular protein of T. molitor, ACP17. After insertion in the expression vector pEX1, the recognition of the fusion protein by an anti-cuticular monoclonal antibody confirmed the cuticular nature of ACP17. Northern hybridization analysis showed that ACP17 mRNA expression begins weakly 3 days before adult ecdysis and strongly increases during the secretion of postecdysial adult cuticle, with a maximum just after ecdysis. In situ hybridization revealed that the ACP17 mRNA is only present in the epidermis which secretes hard cuticle. The deduced amino acid (aa) composition exhibits a high content of Gly (28%) and Ala (20%) and, particularly, two poly(Gx) stretches separated by repetitive motifs with proline AAPVA. A comparison is made with other cuticle aa sequences.

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Amino Acid SequenceAnimalsBase SequenceGene ExpressionIn Situ HybridizationInsect ProteinsMetamorphosis, BiologicalMolecular Sequence DataProtein BiosynthesisProteinsRNA, MessengerSequence Analysis, DNATenebrioTissue DistributionComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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J Mathelin, H Bouhin, B Quennedey, A Courrent, J Delachambre. 1995-04-24. Identification, sequence and mRNA expression pattern during metamorphosis of a cDNA encoding a glycine-rich cuticular protein in Tenebrio molitor.. https://doi.org/10.1016/0378-1119(94)00005-d

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