Molecular cloning, characterization, genomic structure and functional analysis of catalase in Chilo suppressalis
Autor: | Jing Xu, Ming-Xing Lu, Yu-Zhou Du, Dong-lin Huang |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Malpighian tubule system biology Sequence analysis media_common.quotation_subject fungi Insect physiology Midgut Insect Molecular cloning Chilo suppressalis biology.organism_classification 03 medical and health sciences 030104 developmental biology Biochemistry Catalase Insect Science Botany biology.protein media_common |
Zdroj: | Journal of Asia-Pacific Entomology. 20:331-336 |
ISSN: | 1226-8615 |
DOI: | 10.1016/j.aspen.2016.08.006 |
Popis: | Catalase (CAT), one of the key enzymes involved in protecting organisms from reactive oxygen species (ROS), degrades hydrogen peroxide to oxygen and water. In this study, we isolated the catalase gene ( CsCAT ) from the striped stem borer, Chilo suppressalis , a serious pest of rice in Asia. Sequence analysis of the genomic DNA indicated that CsCAT contains a 1023 bp intron and a 1524 bp coding sequence. The predicted CsCAT protein contains 507 amino acids and includes the proximal active site (FXRERIPERVVHAKGXGA) and heme-ligand sequence (RLFSYNDTX) that are conserved in catalase enzymes. Phylogenetic analysis indicated that CAT from Lepidopteran moths could be assigned to one well-supported cluster. qRT-PCR indicated that CsCAT was expressed in insect heads, epidermis, fat body, foregut, midgut, hindgut, Malpighian tubules, and hemocytes. Expression of CsCAT was highest in the fat body and hemocytes of diapausing larvae, which suggests a potential important role in insect physiology during diapause period. Expression of CsCAT (measured by qRT-PCR) and enzymatic activity of CsCAT were not significantly altered by temperature stress, which indicates that CsCAT may insensitive to temperature. |
Databáze: | OpenAIRE |
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