Characterization and analysis of myosin gene family in the whitefly (<i>Bemisia tabaci</i>)

Abstract

<abstract> <p>Myosin is an actin-based motor protein that widely exists in muscle tissue and non-muscle tissue, and myosin of a diverse subfamily has obvious differences in structure and cell function. Many eukaryotes and even some unicellular organisms possess a variety of myosins. They have been well characterized in human, fungi and other organisms. However, the myosin gene family in <italic>Bemisia tabaci</italic> MEAM1 (Middle East-Asia Minor1 species) is poorly studied. In the study, we identified 15 myosin genes in <italic>B. tabaci</italic> MEAM1 based on a genome database. Myosin genes can be divided into ten classes, including subfamilies I, II, III, V, VI, VII, IX, XV, XVIII, XX in <italic>B. tabaci</italic> MEAM1. The amounts of myosin in Class I are the largest of the isoforms. Expression profiling of myosins by quantitative real-time PCR revealed that their expression differed among developmental stages and different tissues of <italic>B. tabaci</italic> MEAM1. The diversely may be related to the development characteristics of <italic>B. tabaci</italic> MEAM1. The <italic>BtaMyo-IIIb-like X1</italic> was highly expressed in nymphs 4 instar which may be related to the development process before metamorphosis. Our outcome contributes to the basis for further research on myosin gene function in <italic>B. tabaci</italic> MEAM1 and homologous myosins in other biology.</p> </abstract>