Abstract

BackgroundSmall heat shock proteins (sHSPs) are products of heat shock response and of other stress responses, and ubiquitous in all three domains of life, archaea, bacteria, and eukarya. They mainly function as molecular chaperones to protect proteins from being denatured in extreme conditions. Study on insect sHSPs could provide some insights into evolution of insects that have adapted to diverse niches in the world.ResultsTaking advantage of the newly assembled genome sequence, we performed a genome-wide analysis of the candidate sHSP genes in the silkworm, Bombyx mori. Based on known silkworm sHSP sequences, we identified 16 silkworm sHSP genes. Most of them are distributed on two silkworm chromosomes 5 and 27, respectively. 15 of 16 silkworm sHSPs have expression evidence. The comparative analysis of insect sHSPs from B. mori, Drosophila melanogaster, Apis mellifera, Tribolium castaneum, and Anopheles gambiae revealed that there is only one orthologous cluster whereas remaining clusters are species-specific on the phylogenetic tree. This suggested that most of sHSPs might have diverged in function across insects investigated. In addition, the data presented in this study also revealed that sHSPs in the insect orthologous cluster are highly conserved in both sequence and expression pattern. In sum, insect sHSPs show a completely different evolutionary pattern from that found in vertebrate sHSPs.ConclusionB. mori has the largest number of insect sHSP genes characterized to date, including 16 genes. The inference that most species-specific sHSPs might have diverged in function across insects investigated will help us understand the adaptability of these insects to diverse environments.

Highlights

  • Small heat shock proteins are products of heat shock response and of other stress responses, and ubiquitous in all three domains of life, archaea, bacteria, and eukarya

  • The molecular weight of each silkworm small heat shock proteins (sHSPs) gene was predicted by the online tool of ExPASy website

  • Compared with the conserved structure of C-terminal, the N-terminal regions of silkworm sHSP genes are relatively divergent in sequence length and order

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Summary

Introduction

Small heat shock proteins (sHSPs) are products of heat shock response and of other stress responses, and ubiquitous in all three domains of life, archaea, bacteria, and eukarya. They mainly function as molecular chaperones to protect proteins from being denatured in extreme conditions. There is a conserved β-sheet sandwich in sHSP secondary structure, and it is these βsheet structures that help several subunits of sHSP to form a large oligomer [2,9,10] This stable multimeric structure formed by sHSPs has the function of molecular chaperone, which binds to the proteins and prevents them from thermal denaturation [10,11,12]. The low molecular weight, the conserved secondary structure, and protein domain are principal features used to identify a protein belonging to sHSP family

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