|ZHIGANOV, NIKITA - Moscow State University
|TERESHCHENKOVA, VALERIIA - Moscow State University
|FILIPPOVA, IRINA - Moscow State University
|BELYAEVA, NATALIYA - Moscow State University
|DUNAEVSKY, YAKOV - Moscow State University
|BELOZERSKY, MIKHAIL - Moscow State University
|ELPIDINA, ELENA - Moscow State University
Submitted to: Data in Brief
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/13/2021
Publication Date: 8/16/2021
Citation: Zhiganov, N.I., Tereshchenkova, V.F., Oppert, B.S., Filippova, I.Y., Belyaeva, N.V., Dunaevsky, Y.E., Belozersky, M.A., Elpidina, E.N. 2021. The dataset of trypsin type serine peptidases and their inactive homologs in Tenebrio molitor transcriptomes. Data in Brief. 38. Article 107301. https://doi.org/10.1016/j.dib.2021.107301.
Interpretive Summary: Enzymes called serine proteases are important for life processes in most living systems. In insects, they play a critical role in the digestion of food. Insects from the family of tenebrionid beetles, such as mealworms, are often damaging to post-harvest agricultural products. In addition, many of these beetles are being studied in the context of developing alternative protein for animal feed. We obtained genetic sequence data from the yellow mealworm and identified sequences that were likely encoding serine proteases. These enzymes were found in the gut and likely have a digestive function, and also in other parts of the insect body that contribute to other functions. These data are important in developing new insect pest management strategies for pest beetle, and also in research to improve insects for animal feed.
Technical Abstract: Tenebrio molitor is an important coleopteran model insect and agricultural pest from the Tenebrionidae family. We used RNA-Seq transcriptome data from T. molitor to annotate trypsin-like sequences from the chymotrypsin S1 family of serine peptidases, including sequences of active serine peptidases (SerP) and their inactive homologs (SerPH) in T. molitor transcriptomes. A total of 63 S1 family tryspin-like serine peptidase sequences were de novo assembled. Among the sequences, 58 were predicted to be active trypsins and five inactive SerPH. The length of preproenzyme and mature form of the predicted enzyme, position of signal peptide and proenzyme cleavage sites, molecular mass, active site and S1 substrate binding subsite residues, and transmembrane and regulatory domains were analyzed using bioinformatic tools. The data can be used for further physiological, biochemical, and phylogenetic study of tenebrionid pests and other animal systems.