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Functional analysis of C1 family cysteine peptidases in the larval gut of Tenebrio molitor and Tribolium castaneumстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 19 сентября 2019 г.
- Авторы: Martynov A.G., Elpidina E.N., Perkin L., Oppert B.
- Журнал: BMC Genomics
- Том: 16
- Номер: 75
- Год издания: 2015
- Издательство: BioMed Central
- Местоположение издательства: London
- DOI: 10.1186/s12864-015-1306-x
- Аннотация: Background Larvae of the tenebrionids Tenebrio molitor and Tribolium castaneum have highly compartmentalized guts, with primarily cysteine peptidases in the acidic anterior midgut that contribute to the early stages of protein digestion. Results High throughput sequencing was used to quantify and characterize transcripts encoding cysteine peptidases from the C1 papain family in the gut of tenebrionid larvae. For T. castaneum, 25 genes and one questionable pseudogene encoding cysteine peptidases were identified, including 11 cathepsin L or L-like, 11 cathepsin B or B-like, and one each F, K, and O. The majority of transcript expression was from two cathepsin L genes on chromosome 10 (LOC659441 and LOC659502). For cathepsin B, the major expression was from genes on chromosome 3 (LOC663145 and LOC663117). Some transcripts were expressed at lower levels or not at all in the larval gut, including cathepsin F, K, and O. For T. molitor, there were 29 predicted cysteine peptidase genes, including 14 cathepsin L or L-like, 13 cathepsin B or B-like, and one each cathepsin O and F. One orthologic cathepsin L and one cathepsin B were also highly expressed. Peptidases lacking conservation in C1 active site residues were identified in both insects, and sequence analysis of orthologs indicated that changes in these residues occurred prior to evolutionary divergence. Sequences from both insects have a high degree of variability in the substrate binding regions, consistent with the ability of these enzymes to degrade a variety of cereal seed storage proteins and inhibitors. Cathepsin B predicted peptidases included some with a shortened occluding loop without active site residues in the middle, apparently lacking exopeptidase activity and unique to tenebrionid insects. Docking of substrates with models of T. molitor cysteine peptidases indicated that, while some insect cathepsin B and L bind substrates with affinities similar to human cathepsin L, others do not and have presumably different substrate specificity. Conclusions These studies have refined our model of protein digestion in the larval gut of tenebrionid insects, and suggest genes that may be targeted by inhibitors or RNA interference for the control of cereal pests in storage areas.
- Добавил в систему: Элпидина Елена Николаевна