Abstract
Apoptosis is executed through the activity of the caspases that are aspartyl-specific proteases. In this study, we isolated the caspase gene (Cscaspase-1) of Chilo suppressalis (one of the leading pests responsible for destruction of rice crops). It possesses the open reading frame (ORF) of 295 amino acids including prodomain, large subunit and small subunits, and two cleavage sites (Asp23 and Asp194) were found to be located among them. In addition to these profiles, Cscaspase-1 contains two active sites (His134 and Cys176). Genomic analysis demonstrated there was no intron in the genome of Cscaspase-1. The Cscaspase-1 transcripts were found in all tissues of the fifth instar larvae, and higher levels were found in the midgut, hindgut and Malpighian tubules. Examination of Cscaspase-1 expression in different developmental stages indicated low constitutive levels in the eggs and early larvae stages, and higher abundances were exhibited in the last larvae and pupae stages. The relative mRNA levels of Cscaspase-1 were induced by heat and cold temperatures. For example, the highest increase of Cscaspase-1 transcription was at −3 °C and 36 °C respectively. In a word, Cscaspase-1 plays a role of effector in the apoptosis of C. suppressalis. It also correlates with development, metamorphosis and thermotolerance of C. suppreassalis.
Highlights
Apoptosis was first described in the publication over forty years ago [1], it still draws great attention as a result of its role in development, host defense, and a response of cells to general stress [2,3,4,5]
Two cleavage sites were found to be located between the prodomain and large subunit at Asp23, and between the large and small subunits at Asp194
The Cscaspase-1 transcripts were found in all tissues of the fifth instar larvae screened in this study, and the higher levels were found in the midgut, hindgut and Malpighian tubules
Summary
Apoptosis was first described in the publication over forty years ago [1], it still draws great attention as a result of its role in development, host defense, and a response of cells to general stress [2,3,4,5]. The caspase family is divided into two groups: the initiators and the executors of apoptosis, each including three domains: an amino terminal domain, a large subunit and a small subunit [8]. Caspases play an important role in apoptosis [9]. The Drosophila genome contains seven caspase genes that function in both immune signaling pathways and development. Completed studies on the genome, structure and functions of caspases in insect were found infrequently, especially the relationship with thermotolerance [5,14,15,16,17]. When exposed to adverse temperatures, organisms may respond differently including the induction of caspases that causes the apoptosis. In order to understand the molecular mechanism of thermotolerance of insect, it’s necessary to study the relation between caspase and thermotolerance. Caspase-1 mRNA expression of different tissues (organs), developmental stages and temperatures was demonstrated
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